Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans: implication of antibiotic resistance.

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Jie Nan

2009-10-01

Full Text Available As an oral bacterial pathogen, Streptococcus mutans has been known as the aetiologic agent of human dental caries. Among a total of 1960 identified proteins within the genome of this organism, there are about 500 without any known functions. One of these proteins, SMU.440, has very few homologs in the current protein databases and it does not fall into any protein functional families. Phylogenetic studies showed that SMU.440 is related to a particular ecological niche and conserved specifically in some oral pathogens, due to lateral gene transfer. The co-occurrence of a MarR protein within the same operon among these oral pathogens suggests that SMU.440 may be associated with antibiotic resistance. The structure determination of SMU.440 revealed that it shares the same fold and a similar pocket as polyketide cyclases, which indicated that it is very likely to bind some polyketide-like molecules. From the interlinking structural and bioinformatics studies, we have concluded that SMU.440 could be involved in polyketide-like antibiotic resistance, providing a better understanding of this hypothetical protein. Besides, the combination of multiple methods in this study can be used as a general approach for functional studies of a protein with unknown function.

Bioinformatics and structural characterization of a hypothetical protein from Streptococcus mutans

DEFF Research Database (Denmark)

Nan, Jie; Brostromer, Erik; Liu, Xiang-Yu

2009-01-01

. From the interlinking structural and bioinformatics studies, we have concluded that SMU.440 could be involved in polyketide-like antibiotic resistance, providing a better understanding of this hypothetical protein. Besides, the combination of multiple methods in this study can be used as a general...

Quantitative and functional characterization of the hyper-conserved protein of Prochlorococcus and marine Synechococcus.

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Caroline E Whidden

Full Text Available A large fraction of any bacterial genome consists of hypothetical protein-coding open reading frames (ORFs. While most of these ORFs are present only in one or a few sequenced genomes, a few are conserved, often across large phylogenetic distances. Such conservation provides clues to likely uncharacterized cellular functions that need to be elucidated. Marine cyanobacteria from the Prochlorococcus/marine Synechococcus clade are dominant bacteria in oceanic waters and are significant contributors to global primary production. A Hyper Conserved Protein (PSHCP of unknown function is 100% conserved at the amino acid level in genomes of Prochlorococcus/marine Synechococcus, but lacks homologs outside of this clade. In this study we investigated Prochlorococcus marinus strains MED4 and MIT 9313 and Synechococcus sp. strain WH 8102 for the transcription of the PSHCP gene using RT-Q-PCR, for the presence of the protein product through quantitative immunoblotting, and for the protein's binding partners in a pull down assay. Significant transcription of the gene was detected in all strains. The PSHCP protein content varied between 8±1 fmol and 26±9 fmol per ug total protein, depending on the strain. The 50 S ribosomal protein L2, the Photosystem I protein PsaD and the Ycf48-like protein were found associated with the PSHCP protein in all strains and not appreciably or at all in control experiments. We hypothesize that PSHCP is a protein associated with the ribosome, and is possibly involved in photosystem assembly.

Identification of a hypothetical membrane protein interactor of ...

Indian Academy of Sciences (India)

Unknown

characterized earlier through co-precipitation studies us- ing antibodies against this conserved carboxyl-terminal region (Rich and Steitz 1987). Protein P0 is also involved at the eEF2 elongation factor-binding domain, as demon- strated in yeast (Justice et al 1999). The P0 protein, and not P1 and P2 proteins, is essential for ...

Characterization of hypothetical proteins Cpn0146, 0147, 0284 & 0285 that are predicted to be in the Chlamydia pneumoniae inclusion membrane

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Liu Kaiyang

2007-05-01

Full Text Available Abstract Background Although more than 100 Chlamydia pneumoniae hypothetical proteins have been predicted to be inclusion membrane proteins, only a few have been experimentally demonstrated to be in the inclusion membrane. Using antibodies raised with fusion proteins, we characterized four such hypothetical proteins encoded by two gene clusters (Cpn0146-147 and Cpn0284-285 in the C. pneumoniae genome. Results Cpn0146 and 0147 were detected in the inclusion membrane while Cpn0284 and 0285 inside inclusion and mainly associated with reticulate bodies although all four proteins contain an N-terminal bi-lobed hydrophobic region, a signature motif assigned to inclusion membrane proteins. These four hypothetical proteins were only detected in cells infected with C. pneumoniae but not other chlamydial species, with Cpn0147 at 6 hours and Cpn0146, 0284 & 0285 at 24 hours after infection. Cpn0146 & 147 but not Cpn0284 and 285 co-localized with a host cell endoplasmic reticulum marker, a property known to be possessed by some chlamydial inclusion membrane proteins, when expressed in the host cell cytosol via transgenes. However, the endoplasmic reticulum localization of the C. pneumoniae inclusion membrane proteins did not result in inhibition of the subsequent C. pneumoniae infection. Conclusion The hypothetical proteins Cpn0146 & 0147 were localized in the C. pneumoniae inclusion membrane while Cpn0284 & 0285 within the inclusion although all four were predicted to be Inc proteins, suggesting the need to experimentally characterize the predicted Inc proteins.

Protein (Cyanobacteria): 495466071 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available conserved hypothetical protein, ribA/ribD-fused Moorea producens MTIYFYDISEKPYGCFSNFSPHGFELDGLWWPTSEHYFQAQK...FAGTSHVEEIRSCKTPAEAASMGRERTRPLRRDWEEIKEDVMGRGLLCKFQTHADIREILLGTGDELIVEDAPQDYYWGCGKDRSGKNRLGEILMEIRAILRES

The relationship of protein conservation and sequence length

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Panchenko Anna R

2002-11-01

Full Text Available Abstract Background In general, the length of a protein sequence is determined by its function and the wide variance in the lengths of an organism's proteins reflects the diversity of specific functional roles for these proteins. However, additional evolutionary forces that affect the length of a protein may be revealed by studying the length distributions of proteins evolving under weaker functional constraints. Results We performed sequence comparisons to distinguish highly conserved and poorly conserved proteins from the bacterium Escherichia coli, the archaeon Archaeoglobus fulgidus, and the eukaryotes Saccharomyces cerevisiae, Drosophila melanogaster, and Homo sapiens. For all organisms studied, the conserved and nonconserved proteins have strikingly different length distributions. The conserved proteins are, on average, longer than the poorly conserved ones, and the length distributions for the poorly conserved proteins have a relatively narrow peak, in contrast to the conserved proteins whose lengths spread over a wider range of values. For the two prokaryotes studied, the poorly conserved proteins approximate the minimal length distribution expected for a diverse range of structural folds. Conclusions There is a relationship between protein conservation and sequence length. For all the organisms studied, there seems to be a significant evolutionary trend favoring shorter proteins in the absence of other, more specific functional constraints.

Identification of functional candidates amongst hypothetical proteins of Treponema pallidum ssp. pallidum.

Science.gov (United States)

Naqvi, Ahmad Abu Turab; Shahbaaz, Mohd; Ahmad, Faizan; Hassan, Md Imtaiyaz

2015-01-01

Syphilis is a globally occurring venereal disease, and its infection is propagated through sexual contact. The causative agent of syphilis, Treponema pallidum ssp. pallidum, a Gram-negative sphirochaete, is an obligate human parasite. Genome of T. pallidum ssp. pallidum SS14 strain (RefSeq NC_010741.1) encodes 1,027 proteins, of which 444 proteins are known as hypothetical proteins (HPs), i.e., proteins of unknown functions. Here, we performed functional annotation of HPs of T. pallidum ssp. pallidum using various database, domain architecture predictors, protein function annotators and clustering tools. We have analyzed the sequences of 444 HPs of T. pallidum ssp. pallidum and subsequently predicted the function of 207 HPs with a high level of confidence. However, functions of 237 HPs are predicted with less accuracy. We found various enzymes, transporters, binding proteins in the annotated group of HPs that may be possible molecular targets, facilitating for the survival of pathogen. Our comprehensive analysis helps to understand the mechanism of pathogenesis to provide many novel potential therapeutic interventions.

Structure of a conserved hypothetical protein SA1388 from S. aureus reveals a capped hexameric toroid with two PII domain lids and a dinuclear metal center

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Leybourne Matthew

2006-12-01

Full Text Available Abstract Background The protein encoded by the SA1388 gene from Staphylococcus aureus was chosen for structure determination to elucidate its domain organization and confirm our earlier remote homology based prediction that it housed a nitrogen regulatory PII protein-like domain. SA1388 was predicted to contain a central PII-like domain and two flanking regions, which together belong to the NIF3-like protein family. Proteins like SA1388 remain a poorly studied group and their structural characterization could guide future investigations aimed at understanding their function. Results The structure of SA1388 has been solved to 2.0Å resolution by single wavelength anomalous dispersion phasing method using selenium anomalous signals. It reveals a canonical NIF3-like fold containing two domains with a PII-like domain inserted in the middle of the polypeptide. The N and C terminal halves of the NIF3-like domains are involved in dimerization, while the PII domain forms trimeric contacts with symmetry related monomers. Overall, the NIF3-like domains of SA1388 are organized as a hexameric toroid similar to its homologs, E. coli ybgI and the hypothetical protein SP1609 from Streptococcus pneumoniae. The openings on either side of the toroid are partially covered by trimeric "lids" formed by the PII domains. The junction of the two NIF3 domains has two zinc ions bound at what appears to be a histidine rich active site. A well-defined electron density corresponding to an endogenously bound ligand of unknown identity is observed in close proximity to the metal site. Conclusion SA1388 is the third member of the NIF3-like family of proteins to be structurally characterized, the other two also being hypothetical proteins of unknown function. The structure of SA1388 confirms our earlier prediction that the inserted domain that separates the two NIF3 domains adopts a PII-like fold and reveals an overall capped toroidal arrangement for the protein hexamer. The

Sequence Analysis of Hypothetical Proteins from 26695 to Identify Potential Virulence Factors

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Ahmad Abu Turab Naqvi

2016-09-01

Full Text Available Helicobacter pylori is a Gram-negative bacteria that is responsible for gastritis in human. Its spiral flagellated body helps in locomotion and colonization in the host environment. It is capable of living in the highly acidic environment of the stomach with the help of acid adaptive genes. The genome of H. pylori 26695 strain contains 1,555 coding genes that encode 1,445 proteins. Out of these, 340 proteins are characterized as hypothetical proteins (HP. This study involves extensive analysis of the HPs using an established pipeline which comprises various bioinformatics tools and databases to find out probable functions of the HPs and identification of virulence factors. After extensive analysis of all the 340 HPs, we found that 104 HPs are showing characteristic similarities with the proteins with known functions. Thus, on the basis of such similarities, we assigned probable functions to 104 HPs with high confidence and precision. All the predicted HPs contain representative members of diverse functional classes of proteins such as enzymes, transporters, binding proteins, regulatory proteins, proteins involved in cellular processes and other proteins with miscellaneous functions. Therefore, we classified 104 HPs into aforementioned functional groups. During the virulence factors analysis of the HPs, we found 11 HPs are showing significant virulence. The identification of virulence proteins with the help their predicted functions may pave the way for drug target estimation and development of effective drug to counter the activity of that protein.

Gene expression profile and immunological evaluation of unique hypothetical unknown proteins of Mycobacterium leprae by using quantitative real-time PCR.

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Kim, Hee Jin; Prithiviraj, Kalyani; Groathouse, Nathan; Brennan, Patrick J; Spencer, John S

2013-02-01

The cell-mediated immunity (CMI)-based in vitro gamma interferon release assay (IGRA) of Mycobacterium leprae-specific antigens has potential as a promising diagnostic means to detect those individuals in the early stages of M. leprae infection. Diagnosis of leprosy is a major obstacle toward ultimate disease control and has been compromised in the past by the lack of specific markers. Comparative bioinformatic analysis among mycobacterial genomes identified potential M. leprae-specific proteins called "hypothetical unknowns." Due to massive gene decay and the prevalence of pseudogenes, it is unclear whether any of these proteins are expressed or are immunologically relevant. In this study, we performed cDNA-based quantitative real-time PCR to investigate the expression status of 131 putative open reading frames (ORFs) encoding hypothetical unknowns. Twenty-six of the M. leprae-specific antigen candidates showed significant levels of gene expression compared to that of ESAT-6 (ML0049), which is an important T cell antigen of low abundance in M. leprae. Fifteen of 26 selected antigen candidates were expressed and purified in Escherichia coli. The seroreactivity to these proteins of pooled sera from lepromatous leprosy patients and cavitary tuberculosis patients revealed that 9 of 15 recombinant hypothetical unknowns elicited M. leprae-specific immune responses. These nine proteins may be good diagnostic reagents to improve both the sensitivity and specificity of detection of individuals with asymptomatic leprosy.

An in silico Approach for Structural and Functional Annotation of Salmonella enterica serovar typhimurium Hypothetical Protein R_27

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Arif Khan

2016-03-01

Full Text Available Typhoid fever is a major cause of illness in most developing countries, including Bangladesh. In quest of new potential drug against Typhoid fever, the current study was designed to elucidate structural and functional details of S. typhi hypothetical protein (HP R_27. HP R_27 has the primary amino acid sequences available only. The structural annotation was determined by ProtParam, SOPMA, and CELLO. The three-dimensional (3D structure of HP R_27 predicted through homology modeling by using Phyre2. The 3D structure then refined and verified by ModRefiner, PROCHECK, ERRAT, QMEAN. The functional annotation was also performed by InterProScan, SMART, Pfam, NCBI-CDD and found Phospholipase D-like and DNA repair activity. Multiple sequence alignment also supported the existence of PLD-like domain and DNA repair protein domain in the selected hypothetical protein sequences. Finally, the cavity of drug binding was also identified to assist further molecular docking study and potent inhibitor identification. This in silico approach can be further utilized in molecular drug design for other clinically significant pathogens.

Pleiotropic Regulation of Virulence Genes in Streptococcus mutans by the Conserved Small Protein SprV.

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Shankar, Manoharan; Hossain, Mohammad S; Biswas, Indranil

2017-04-15

Streptococcus mutans , an oral pathogen associated with dental caries, colonizes tooth surfaces as polymicrobial biofilms known as dental plaque. S. mutans expresses several virulence factors that allow the organism to tolerate environmental fluctuations and compete with other microorganisms. We recently identified a small hypothetical protein (90 amino acids) essential for the normal growth of the bacterium. Inactivation of the gene, SMU.2137, encoding this protein caused a significant growth defect and loss of various virulence-associated functions. An S. mutans strain lacking this gene was more sensitive to acid, temperature, osmotic, oxidative, and DNA damage-inducing stresses. In addition, we observed an altered protein profile and defects in biofilm formation, bacteriocin production, and natural competence development, possibly due to the fitness defect associated with SMU.2137 deletion. Transcriptome sequencing revealed that nearly 20% of the S. mutans genes were differentially expressed upon SMU.2137 deletion, thereby suggesting a pleiotropic effect. Therefore, we have renamed this hitherto uncharacterized gene as sprV ( s treptococcal p leiotropic r egulator of v irulence). The transcript levels of several relevant genes in the sprV mutant corroborated the phenotypes observed upon sprV deletion. Owing to its highly conserved nature, inactivation of the sprV ortholog in Streptococcus gordonii also resulted in poor growth and defective UV tolerance and competence development as in the case of S. mutans Our experiments suggest that SprV is functionally distinct from its homologs identified by structure and sequence homology. Nonetheless, our current work is aimed at understanding the importance of SprV in the S. mutans biology. IMPORTANCE Streptococcus mutans employs several virulence factors and stress resistance mechanisms to colonize tooth surfaces and cause dental caries. Bacterial pathogenesis is generally controlled by regulators of fitness that are

NCBI nr-aa BLAST: CBRC-BTAU-01-0778 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-BTAU-01-0778 ref|ZP_01680223.1| conserved hypothetical protein [Vibrio cholerae... V52] ref|ZP_01956103.1| conserved hypothetical protein [Vibrio cholerae MZO-3] gb|EAX62933.1| conserved hy...pothetical protein [Vibrio cholerae V52] gb|EAY41665.1| conserved hypothetical protein [Vibrio cholerae MZO-3] ZP_01680223.1 0.003 24% ...

A two-dimensional proteome reference map of Herbaspirillum seropedicae proteins.

Science.gov (United States)

Chaves, Daniela Fojo Seixas; Ferrer, Pércio Pereira; de Souza, Emanuel Maltempi; Gruz, Leonardo Magalhães; Monteiro, Rose Adele; de Oliveira Pedrosa, Fábio

2007-10-01

Herbaspirillum seropedicae is an endophytic diazotroph associated with economically important crops such as rice, sugarcane, and wheat. Here, we present a 2-D reference map for H. seropedicae. Using MALDI-TOF-MS we identified 205 spots representing 173 different proteins with a calculated average of 1.18 proteins/gene. Seventeen hypothetical or conserved hypothetical ORFs were shown to code for true gene products. These data will support the genome annotation process and provide a basis on which to undertake comparative proteomic studies.

Prediction of functional sites in proteins using conserved functional group analysis.

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Innis, C Axel; Anand, A Prem; Sowdhamini, R

2004-04-02

A detailed knowledge of a protein's functional site is an absolute prerequisite for understanding its mode of action at the molecular level. However, the rapid pace at which sequence and structural information is being accumulated for proteins greatly exceeds our ability to determine their biochemical roles experimentally. As a result, computational methods are required which allow for the efficient processing of the evolutionary information contained in this wealth of data, in particular that related to the nature and location of functionally important sites and residues. The method presented here, referred to as conserved functional group (CFG) analysis, relies on a simplified representation of the chemical groups found in amino acid side-chains to identify functional sites from a single protein structure and a number of its sequence homologues. We show that CFG analysis can fully or partially predict the location of functional sites in approximately 96% of the 470 cases tested and that, unlike other methods available, it is able to tolerate wide variations in sequence identity. In addition, we discuss its potential in a structural genomics context, where automation, scalability and efficiency are critical, and an increasing number of protein structures are determined with no prior knowledge of function. This is exemplified by our analysis of the hypothetical protein Ydde_Ecoli, whose structure was recently solved by members of the North East Structural Genomics consortium. Although the proposed active site for this protein needs to be validated experimentally, this example illustrates the scope of CFG analysis as a general tool for the identification of residues likely to play an important role in a protein's biochemical function. Thus, our method offers a convenient solution to rapidly and automatically process the vast amounts of data that are beginning to emerge from structural genomics projects.

[Interconnection between architecture of protein globule and disposition of conformational conservative oligopeptides in proteins from one protein family].

Science.gov (United States)

Batianovskiĭ, A V; Filatov, I V; Namiot, V A; Esipova, N G; Volotovskiĭ, I D

2012-01-01

It was shown that selective interactions between helical segments of macromolecules can realize in globular proteins in the segments characterized by the same periodicities of charge distribution i.e. between conformationally conservative oligopeptides. It was found that in the macromolecules of alpha-helical proteins conformationally conservative oligopeptides are disposed at a distance being characteristic of direct interactions. For representatives of many structural families of alpha-type proteins specific disposition of conformationally conservative segments is observed. This disposition is inherent to a particular structural family. Disposition of conformationally conservative segments is not related to homology of the amino acid sequence but reflects peculiarities of native 3D-architectures of protein globules.

Topology-function conservation in protein-protein interaction networks.

Science.gov (United States)

Davis, Darren; Yaveroğlu, Ömer Nebil; Malod-Dognin, Noël; Stojmirovic, Aleksandar; Pržulj, Nataša

2015-05-15

Proteins underlay the functioning of a cell and the wiring of proteins in protein-protein interaction network (PIN) relates to their biological functions. Proteins with similar wiring in the PIN (topology around them) have been shown to have similar functions. This property has been successfully exploited for predicting protein functions. Topological similarity is also used to guide network alignment algorithms that find similarly wired proteins between PINs of different species; these similarities are used to transfer annotation across PINs, e.g. from model organisms to human. To refine these functional predictions and annotation transfers, we need to gain insight into the variability of the topology-function relationships. For example, a function may be significantly associated with specific topologies, while another function may be weakly associated with several different topologies. Also, the topology-function relationships may differ between different species. To improve our understanding of topology-function relationships and of their conservation among species, we develop a statistical framework that is built upon canonical correlation analysis. Using the graphlet degrees to represent the wiring around proteins in PINs and gene ontology (GO) annotations to describe their functions, our framework: (i) characterizes statistically significant topology-function relationships in a given species, and (ii) uncovers the functions that have conserved topology in PINs of different species, which we term topologically orthologous functions. We apply our framework to PINs of yeast and human, identifying seven biological process and two cellular component GO terms to be topologically orthologous for the two organisms. © The Author 2015. Published by Oxford University Press.

Conservation and diversification of Msx protein in metazoan evolution.

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Takahashi, Hirokazu; Kamiya, Akiko; Ishiguro, Akira; Suzuki, Atsushi C; Saitou, Naruya; Toyoda, Atsushi; Aruga, Jun

2008-01-01

Msx (/msh) family genes encode homeodomain (HD) proteins that control ontogeny in many animal species. We compared the structures of Msx genes from a wide range of Metazoa (Porifera, Cnidaria, Nematoda, Arthropoda, Tardigrada, Platyhelminthes, Mollusca, Brachiopoda, Annelida, Echiura, Echinodermata, Hemichordata, and Chordata) to gain an understanding of the role of these genes in phylogeny. Exon-intron boundary analysis suggested that the position of the intron located N-terminally to the HDs was widely conserved in all the genes examined, including those of cnidarians. Amino acid (aa) sequence comparison revealed 3 new evolutionarily conserved domains, as well as very strong conservation of the HDs. Two of the three domains were associated with Groucho-like protein binding in both a vertebrate and a cnidarian Msx homolog, suggesting that the interaction between Groucho-like proteins and Msx proteins was established in eumetazoan ancestors. Pairwise comparison among the collected HDs and their C-flanking aa sequences revealed that the degree of sequence conservation varied depending on the animal taxa from which the sequences were derived. Highly conserved Msx genes were identified in the Vertebrata, Cephalochordata, Hemichordata, Echinodermata, Mollusca, Brachiopoda, and Anthozoa. The wide distribution of the conserved sequences in the animal phylogenetic tree suggested that metazoan ancestors had already acquired a set of conserved domains of the current Msx family genes. Interestingly, although strongly conserved sequences were recovered from the Vertebrata, Cephalochordata, and Anthozoa, the sequences from the Urochordata and Hydrozoa showed weak conservation. Because the Vertebrata-Cephalochordata-Urochordata and Anthozoa-Hydrozoa represent sister groups in the Chordata and Cnidaria, respectively, Msx sequence diversification may have occurred differentially in the course of evolution. We speculate that selective loss of the conserved domains in Msx family

The multiple roles of hypothetical gene BPSS1356 in Burkholderia pseudomallei.

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Hokchai Yam

Full Text Available Burkholderia pseudomallei is an opportunistic pathogen and the causative agent of melioidosis. It is able to adapt to harsh environments and can live intracellularly in its infected hosts. In this study, identification of transcriptional factors that associate with the β' subunit (RpoC of RNA polymerase was performed. The N-terminal region of this subunit is known to trigger promoter melting when associated with a sigma factor. A pull-down assay using histidine-tagged B. pseudomallei RpoC N-terminal region as bait showed that a hypothetical protein BPSS1356 was one of the proteins bound. This hypothetical protein is conserved in all B. pseudomallei strains and present only in the Burkholderia genus. A BPSS1356 deletion mutant was generated to investigate its biological function. The mutant strain exhibited reduced biofilm formation and a lower cell density during the stationary phase of growth in LB medium. Electron microscopic analysis revealed that the ΔBPSS1356 mutant cells had a shrunken cytoplasm indicative of cell plasmolysis and a rougher surface when compared to the wild type. An RNA microarray result showed that a total of 63 genes were transcriptionally affected by the BPSS1356 deletion with fold change values of higher than 4. The expression of a group of genes encoding membrane located transporters was concurrently down-regulated in ΔBPSS1356 mutant. Amongst the affected genes, the putative ion transportation genes were the most severely suppressed. Deprivation of BPSS1356 also down-regulated the transcriptions of genes for the arginine deiminase system, glycerol metabolism, type III secretion system cluster 2, cytochrome bd oxidase and arsenic resistance. It is therefore obvious that BPSS1356 plays a multiple regulatory roles on many genes.

Hierarchical partitioning of metazoan protein conservation profiles provides new functional insights.

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Jonathan Witztum

Full Text Available The availability of many complete, annotated proteomes enables the systematic study of the relationships between protein conservation and functionality. We explore this question based solely on the presence or absence of protein homologues (a.k.a. conservation profiles. We study 18 metazoans, from two distinct points of view: the human's and the fly's. Using the GOrilla gene ontology (GO analysis tool, we explore functional enrichment of the "universal proteins", those with homologues in all 17 other species, and of the "non-universal proteins". A large number of GO terms are strongly enriched in both human and fly universal proteins. Most of these functions are known to be essential. A smaller number of GO terms, exhibiting markedly different properties, are enriched in both human and fly non-universal proteins. We further explore the non-universal proteins, whose conservation profiles are consistent with the "tree of life" (TOL consistent, as well as the TOL inconsistent proteins. Finally, we applied Quantum Clustering to the conservation profiles of the TOL consistent proteins. Each cluster is strongly associated with one or a small number of specific monophyletic clades in the tree of life. The proteins in many of these clusters exhibit strong functional enrichment associated with the "life style" of the related clades. Most previous approaches for studying function and conservation are "bottom up", studying protein families one by one, and separately assessing the conservation of each. By way of contrast, our approach is "top down". We globally partition the set of all proteins hierarchically, as described above, and then identify protein families enriched within different subdivisions. While supporting previous findings, our approach also provides a tool for discovering novel relations between protein conservation profiles, functionality, and evolutionary history as represented by the tree of life.

In silico functional elucidation of uncharacterized proteins of Chlamydia abortus strain LLG.

Science.gov (United States)

Singh, Gagandeep; Sharma, Dixit; Singh, Vikram; Rani, Jyoti; Marotta, Francessco; Kumar, Manoj; Mal, Gorakh; Singh, Birbal

2017-03-01

This study reports structural modeling, molecular dynamics profiling of hypothetical proteins in Chlamydia abortus genome database. The hypothetical protein sequences were extracted from C. abortus LLG Genome Database for functional elucidation using in silico methods. Fifty-one proteins with their roles in defense, binding and transporting other biomolecules were unraveled. Forty-five proteins were found to be nonhomologous to proteins present in hosts infected by C. abortus . Of these, 31 proteins were related to virulence. The structural modeling of two proteins, first, WP_006344020.1 (phosphorylase) and second, WP_006344325.1 (chlamydial protease/proteasome-like activity factor) were accomplished. The conserved active sites necessary for the catalytic function were analyzed. The finally concluded proteins are envisioned as possible targets for developing drugs to curtail chlamydial infections, however, and should be validated by molecular biological methods.

Characterization of a DUF820 family protein Alr3200 of the ...

Indian Academy of Sciences (India)

The hypothetical protein 'Alr3200' of Anabaena sp. strain PCC7120 is highly conserved among cyanobacterialspecies. It is a member of the DUF820 (Domain of Unknown Function) protein family, and is predicted to have aDNase domain. Biochemical analysis revealed a Mg(II)-dependent DNase activity for Alr3200 with a ...

Identification of functional candidates amongst hypothetical proteins of Mycobacterium leprae Br4923, a causative agent of leprosy.

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Naqvi, Ahmad Abu Turab; Ahmad, Faizan; Hassan, Md Imtaiyaz

2015-01-01

Mycobacterium leprae is an intracellular obligate parasite that causes leprosy in humans, and it leads to the destruction of peripheral nerves and skin deformation. Here, we report an extensive analysis of the hypothetical proteins (HPs) from M. leprae strain Br4923, assigning their functions to better understand the mechanism of pathogenesis and to search for potential therapeutic interventions. The genome of M. leprae encodes 1604 proteins, of which the functions of 632 are not known (HPs). In this paper, we predicted the probable functions of 312 HPs. First, we classified all HPs into families and subfamilies on the basis of sequence similarity, followed by domain assignment, which provides many clues for their possible function. However, the functions of 320 proteins were not predicted because of low sequence similarity with proteins of known function. Annotated HPs were categorized into enzymes, binding proteins, transporters, and proteins involved in cellular processes. We found several novel proteins whose functions were unknown for M. leprae. These proteins have a requisite association with bacterial virulence and pathogenicity. Finally, our sequence-based analysis will be helpful for further validation and the search for potential drug targets while developing effective drugs to cure leprosy.

Conservation potential of agricultural water conservation subsidies

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Huffaker, Ray

2008-07-01

A current policy subsidizes farmers to invest in improved on-farm irrigation efficiency, expecting water to be conserved off farm. Contrary to expectation, water has been increasingly depleted in some regions after such improvements. This paper investigates the policy's failure to conserve water consistently by (1) formulating an economic model of irrigated crop production to determine a profit-maximizing irrigator's range of responses to a subsidy and (2) embedding these responses into hypothetical streamflow diagrams to ascertain their potential to conserve water under various hydrologic regimes. Testable hypotheses are developed to predict the conservation potential of a subsidy in real-world application.

Solution NMR Structure of Hypothetical Protein CV_2116 Encoded by a Viral Prophage Element in Chromobacterium violaceum

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Yunhuang Yang

2012-06-01

Full Text Available CV_2116 is a small hypothetical protein of 82 amino acids from the Gram-negative coccobacillus Chromobacterium violaceum. A PSI-BLAST search using the CV_2116 sequence as a query identified only one hit (E = 2e⁻⁰⁷ corresponding to a hypothetical protein OR16_04617 from Cupriavidus basilensis OR16, which failed to provide insight into the function of CV_2116. The CV_2116 gene was cloned into the p15TvLic expression plasmid, transformed into E. coli, and ¹³C- and ¹⁵N-labeled NMR samples of CV_2116 were overexpressed in E. coli and purified for structure determination using NMR spectroscopy. The resulting high-quality solution NMR structure of CV_2116 revealed a novel α + β fold containing two anti-parallel β -sheets in the N-terminal two-thirds of the protein and one α-helix in the C-terminal third of the protein. CV_2116 does not belong to any known protein sequence family and a Dali search indicated that no similar structures exist in the protein data bank. Although no function of CV_2116 could be derived from either sequence or structural similarity searches, the neighboring genes of CV_2116 encode various proteins annotated as similar to bacteriophage tail assembly proteins. Interestingly, C. violaceum exhibits an extensive network of bacteriophage tail-like structures that likely result from lateral gene transfer by incorporation of viral DNA into its genome (prophages due to bacteriophage infection. Indeed, C. violaceum has been shown to contain four prophage elements and CV_2116 resides in the fourth of these elements. Analysis of the putative operon in which CV_2116 resides indicates that CV_2116 might be a component of the bacteriophage tail-like assembly that occurs in C. violaceum.

On the relationship between residue structural environment and sequence conservation in proteins.

Science.gov (United States)

Liu, Jen-Wei; Lin, Jau-Ji; Cheng, Chih-Wen; Lin, Yu-Feng; Hwang, Jenn-Kang; Huang, Tsun-Tsao

2017-09-01

Residues that are crucial to protein function or structure are usually evolutionarily conserved. To identify the important residues in protein, sequence conservation is estimated, and current methods rely upon the unbiased collection of homologous sequences. Surprisingly, our previous studies have shown that the sequence conservation is closely correlated with the weighted contact number (WCN), a measure of packing density for residue's structural environment, calculated only based on the C α positions of a protein structure. Moreover, studies have shown that sequence conservation is correlated with environment-related structural properties calculated based on different protein substructures, such as a protein's all atoms, backbone atoms, side-chain atoms, or side-chain centroid. To know whether the C α atomic positions are adequate to show the relationship between residue environment and sequence conservation or not, here we compared C α atoms with other substructures in their contributions to the sequence conservation. Our results show that C α positions are substantially equivalent to the other substructures in calculations of various measures of residue environment. As a result, the overlapping contributions between C α atoms and the other substructures are high, yielding similar structure-conservation relationship. Take the WCN as an example, the average overlapping contribution to sequence conservation is 87% between C α and all-atom substructures. These results indicate that only C α atoms of a protein structure could reflect sequence conservation at the residue level. © 2017 Wiley Periodicals, Inc.

NCBI nr-aa BLAST: CBRC-TTRU-01-0103 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0103 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.012 24% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0519 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0519 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.11 25% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-1354 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-1354 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.062 22% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0280 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0280 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.028 24% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0528 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0528 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.039 24% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0560 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0560 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.14 21% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0973 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0973 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.041 21% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0552 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0552 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.022 20% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0021 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0021 ref|YP_001678281.1| hypothetical protein Fphi_1554 [Francisella philomiragia subsp. philo...miragia ATCC 25017] ref|ZP_04755921.1| hypothetical protein FphipA2_06231 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249586.1| conserved hypothetical protein [Francisella philo...ical membrane protein [Francisella philomiragia subsp. philomiragia ATCC 25017] gb|EET21311.1| conserved hyp...othetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] YP_001678281.1 0.23 23% ...

NCBI nr-aa BLAST: CBRC-HSAP-07-0021 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-HSAP-07-0021 ref|YP_798483.1| hypothetical protein LBL_2137 [Leptospira borgpeter...senii serovar Hardjo-bovis L550] ref|YP_801392.1| hypothetical protein LBJ_2143 [Leptospira borgpeterseni...i serovar Hardjo-bovis JB197] gb|ABJ79550.1| Conserved hypothetical protein [Leptospira borgpetersenii serov...ar Hardjo-bovis L550] gb|ABJ76634.1| Conserved hypothetical protein [Leptospira borgpetersenii serovar Hardjo-bovis JB197] YP_798483.1 0.026 28% ...

NCBI nr-aa BLAST: CBRC-OCUN-01-1280 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OCUN-01-1280 ref|YP_798310.1| hypothetical protein LBL_1947 [Leptospira borgpeter...senii serovar Hardjo-bovis L550] ref|YP_801037.1| hypothetical protein LBJ_1728 [Leptospira borgpeterseni...i serovar Hardjo-bovis JB197] gb|ABJ79377.1| Conserved hypothetical protein [Leptospira borgpetersenii serov...ar Hardjo-bovis L550] gb|ABJ76279.1| Conserved hypothetical protein [Leptospira borgpetersenii serovar Hardjo-bovis JB197] YP_798310.1 4.1 31% ...

Ubiquitin--conserved protein or selfish gene?

Science.gov (United States)

Catic, André; Ploegh, Hidde L

2005-11-01

The posttranslational modifier ubiquitin is encoded by a multigene family containing three primary members, which yield the precursor protein polyubiquitin and two ubiquitin moieties, Ub(L40) and Ub(S27), that are fused to the ribosomal proteins L40 and S27, respectively. The gene encoding polyubiquitin is highly conserved and, until now, those encoding Ub(L40) and Ub(S27) have been generally considered to be equally invariant. The evolution of the ribosomal ubiquitin moieties is, however, proving to be more dynamic. It seems that the genes encoding Ub(L40) and Ub(S27) are actively maintained by homologous recombination with the invariant polyubiquitin locus. Failure to recombine leads to deterioration of the sequence of the ribosomal ubiquitin moieties in several phyla, although this deterioration is evidently constrained by the structural requirements of the ubiquitin fold. Only a few amino acids in ubiquitin are vital for its function, and we propose that conservation of all three ubiquitin genes is driven not only by functional properties of the ubiquitin protein, but also by the propensity of the polyubiquitin locus to act as a 'selfish gene'.

Soil carbon sequestration, carbon markets, and conservation agriculture practices: A hypothetical examination in Mozambique

Directory of Open Access Journals (Sweden)

Timoteo E. Simone

2017-09-01

Full Text Available Payments for Environmental Services (PES are relatively novel mechanisms whereby the adoption of sustainable management practices by a stakeholder is rewarded by incentives linked to external markets. Adoption of PES for conservation agricultural practices (CAPS by smallholder farmers may provide opportunities to increase household income or cover the technology costs of adoption if the carbon sequestration benefits of CAPS are quantifiable, adoption rates are accelerated and maintained, a mechanism exists whereby carbon sequestration services can be compensated, and carbon offset exchange markets are viable. This research suggests a methodology to examine a PES market for carbon offsets generated by the adoption of CAPS by farmers in Mozambique. Assuming a cumulative adoption of 60% over a 20-year period, revenue from PES market participation to CA adopters was two times higher than revenue earned when disadoption occurred midway through the simulation. Lower adoption targets are associated with higher per household returns when fertilizer rates typical to the region are increased. Establishing and maintaining a sustainable PES system in the study region would require significant investment in time and resources. The lack of on-the-ground institutions or local support for such a program would also challenge successful implementation. Finally, the programs where participant success depends on external markets, such as the hypothetical one suggested here, are subject to the ebb and flow of foreign demand for carbon offsets. Addressing these three broad constraints to a PES/CAPS program in the region would require grass-roots driven policy initiatives with buy-in at multiple social, economic, and political levels.

NCBI nr-aa BLAST: CBRC-MDOM-03-0050 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-MDOM-03-0050 ref|ZP_04755880.1| hypothetical protein FphipA2_06026 [Francisella philo...miragia subsp. philomiragia ATCC 25015] ref|ZP_05249544.1| conserved hypothetical protein [Francisella philo...miragia subsp. philomiragia ATCC 25015] gb|EET21269.1| conserved hypothetical protein [Francisella philomiragia subsp. philomiragia ATCC 25015] ZP_04755880.1 0.048 28% ...

NCBI nr-aa BLAST: CBRC-EEUR-01-1367 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-EEUR-01-1367 ref|XP_001566741.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM40257.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001566741.1 1.0 26% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-0258 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-0258 ref|XP_001568170.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43274.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568170.1 2.3 27% ...

Radiological consequences of a hypothetical ''roof breakdown'' accident of the Chernobyl sarcophagus

International Nuclear Information System (INIS)

Pretzsch, G.

1997-01-01

On behalf of the German Federal Ministry for Environment, Nature Conservation and Nuclear Safety GRS performed investigations with the aim to improve the safety of the Chernobyl Unit 4 shelter in close connection with the Ministry for Environment and Nuclear Safety of the Ukraina from 1992 to 1995. One of the tasks of the working programme was concerned with the analysis of hypothetical accidents of the present shelter, which comprises the newly built Sarcophagus and the remaining ruins of Unit 4. In close collaboration with Ukrainian and Russian experts the maximum hypothetical accident was defined to be the breakdown of the roof of the Sarcophagus and subsequent release of the radioactive dust which is mainly located in the destroyed reactor hall and the neighboring rooms

NCBI nr-aa BLAST: CBRC-TSYR-01-0087 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TSYR-01-0087 ref|YP_002824787.1| conserved hypothetical protein, contains ice nucleation... protein domain [Rhizobium sp. NGR234] gb|ACP24034.1| conserved hypothetical protein, contains ice nucleation protein domain [Rhizobium sp. NGR234] YP_002824787.1 1e-17 20% ...

NCBI nr-aa BLAST: CBRC-TSYR-01-0156 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TSYR-01-0156 ref|YP_002824783.1| conserved hypothetical protein, contains ice nucleation... protein domain [Rhizobium sp. NGR234] gb|ACP24030.1| conserved hypothetical protein, contains ice nucleation protein domain [Rhizobium sp. NGR234] YP_002824783.1 3e-18 20% ...

NCBI nr-aa BLAST: CBRC-TSYR-01-1411 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TSYR-01-1411 ref|YP_002824787.1| conserved hypothetical protein, contains ice nucleation... protein domain [Rhizobium sp. NGR234] gb|ACP24034.1| conserved hypothetical protein, contains ice nucleation protein domain [Rhizobium sp. NGR234] YP_002824787.1 4e-43 18% ...

NCBI nr-aa BLAST: CBRC-TSYR-01-0087 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TSYR-01-0087 ref|YP_002824783.1| conserved hypothetical protein, contains ice nucleation... protein domain [Rhizobium sp. NGR234] gb|ACP24030.1| conserved hypothetical protein, contains ice nucleation protein domain [Rhizobium sp. NGR234] YP_002824783.1 2e-18 19% ...

NCBI nr-aa BLAST: CBRC-DDIS-05-0136 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DDIS-05-0136 ref|XP_001569189.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM44328.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001569189.1 1e-26 29% ...

NCBI nr-aa BLAST: CBRC-BTAU-01-2711 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-BTAU-01-2711 ref|XP_001568632.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43752.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568632.1 6e-17 29% ...

NCBI nr-aa BLAST: CBRC-PABE-20-0089 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PABE-20-0089 ref|XP_001568148.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43250.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568148.1 4e-08 29% ...

NCBI nr-aa BLAST: CBRC-MMUS-01-0068 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-MMUS-01-0068 ref|XP_001568148.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43250.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568148.1 4e-14 29% ...

NCBI nr-aa BLAST: CBRC-XTRO-01-0977 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-XTRO-01-0977 ref|XP_001568632.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43752.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568632.1 1e-11 28% ...

NCBI nr-aa BLAST: CBRC-XTRO-01-3332 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-XTRO-01-3332 ref|XP_001568148.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43250.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568148.1 1e-32 27% ...

NCBI nr-aa BLAST: CBRC-CELE-05-0449 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CELE-05-0449 ref|XP_001568148.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43250.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568148.1 3e-25 48% ...

NCBI nr-aa BLAST: CBRC-PABE-08-0005 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PABE-08-0005 ref|XP_001568632.1| hypothetical protein, conserved [Leishmania brazil...iensis] emb|CAM43752.1| hypothetical protein, conserved [Leishmania braziliensis] XP_001568632.1 1e-09 30% ...

Conservation of Oxidative Protein Stabilization in an Insect Homologue of Parkinsonism-Associated Protein DJ-1

Energy Technology Data Exchange (ETDEWEB)

Lin, Jiusheng; Prahlad, Janani; Wilson, Mark A. (UNL)

2012-08-21

DJ-1 is a conserved, disease-associated protein that protects against oxidative stress and mitochondrial damage in multiple organisms. Human DJ-1 contains a functionally essential cysteine residue (Cys106) whose oxidation is important for regulating protein function by an unknown mechanism. This residue is well-conserved in other DJ-1 homologues, including two (DJ-1{alpha} and DJ-1{beta}) in Drosophila melanogaster. Because D. melanogaster is a powerful model system for studying DJ-1 function, we have determined the crystal structure and impact of cysteine oxidation on Drosophila DJ-1{beta}. The structure of D. melanogaster DJ-1{beta} is similar to that of human DJ-1, although two important residues in the human protein, Met26 and His126, are not conserved in DJ-1{beta}. His126 in human DJ-1 is substituted with a tyrosine in DJ-1{beta}, and this residue is not able to compose a putative catalytic dyad with Cys106 that was proposed to be important in the human protein. The reactive cysteine in DJ-1 is oxidized readily to the cysteine-sulfinic acid in both flies and humans, and this may regulate the cytoprotective function of the protein. We show that the oxidation of this conserved cysteine residue to its sulfinate form (Cys-SO{sub 2{sup -}}) results in considerable thermal stabilization of both Drosophila DJ-1{beta} and human DJ-1. Therefore, protein stabilization is one potential mechanism by which cysteine oxidation may regulate DJ-1 function in vivo. More generally, most close DJ-1 homologues are likely stabilized by cysteine-sulfinic acid formation but destabilized by further oxidation, suggesting that they are biphasically regulated by oxidative modification.

NCBI nr-aa BLAST: CBRC-AGAM-03-0017 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-AGAM-03-0017 ref|ZP_01512956.1| conserved hypothetical protein [Burkholderia phytofirm...ans PsJN] gb|EAV02438.1| conserved hypothetical protein [Burkholderia phytofirmans PsJN] ZP_01512956.1 0.070 25% ...

NCBI nr-aa BLAST: CBRC-DSIM-02-0067 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DSIM-02-0067 ref|ZP_00538033.1| conserved hypothetical protein [Exiguobacterium sibi...ricum 255-15] gb|EAM88856.1| conserved hypothetical protein [Exiguobacterium sibiricum 255-15] ZP_00538033.1 2.9 36% ...

NCBI nr-aa BLAST: CBRC-DYAK-01-0020 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DYAK-01-0020 ref|ZP_02017389.1| conserved hypothetical protein [Methylobacterium extorque...ns PA1] gb|EDN55077.1| conserved hypothetical protein [Methylobacterium extorquens PA1] ZP_02017389.1 2.0 31% ...

NCBI nr-aa BLAST: CBRC-PCAP-01-1406 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PCAP-01-1406 ref|XP_001213293.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU35917.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001213293.1 0.97 28% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-2770 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-2770 ref|XP_001208647.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU38039.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001208647.1 8.7 27% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-1000 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-1000 ref|XP_001215926.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU33292.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001215926.1 0.54 32% ...

NCBI nr-aa BLAST: CBRC-GACU-03-0029 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-GACU-03-0029 ref|XP_001216777.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU31329.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001216777.1 3.1 39% ...

NCBI nr-aa BLAST: CBRC-ACAR-01-0231 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-ACAR-01-0231 ref|XP_001209722.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU32420.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001209722.1 0.48 31% ...

NCBI nr-aa BLAST: CBRC-BTAU-01-2657 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-BTAU-01-2657 ref|XP_001214433.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU34324.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001214433.1 0.46 34% ...

NCBI nr-aa BLAST: CBRC-TBEL-01-0313 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TBEL-01-0313 ref|XP_001213187.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU35811.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001213187.1 6.7 43% ...

NCBI nr-aa BLAST: CBRC-OSAT-04-0037 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OSAT-04-0037 ref|XP_001215089.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU33672.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001215089.1 0.019 28% ...

NCBI nr-aa BLAST: CBRC-PTRO-01-0109 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PTRO-01-0109 ref|XP_001218166.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU29735.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001218166.1 0.007 31% ...

NCBI nr-aa BLAST: CBRC-ETEL-01-0740 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-ETEL-01-0740 ref|XP_001217896.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU30411.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001217896.1 0.82 29% ...

NCBI nr-aa BLAST: CBRC-ACAR-01-0164 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-ACAR-01-0164 ref|XP_001209232.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU38624.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001209232.1 1.5 24% ...

NCBI nr-aa BLAST: CBRC-DSIM-01-0068 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DSIM-01-0068 ref|XP_001215680.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU33046.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001215680.1 4.4 30% ...

NCBI nr-aa BLAST: CBRC-CBRE-01-0099 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CBRE-01-0099 ref|ZP_01187451.1| conserved hypothetical protein [Bacillus weihenstep...hanensis KBAB4] gb|EAR73176.1| conserved hypothetical protein [Bacillus weihenstephanensis KBAB4] ZP_01187451.1 0.60 31% ...

NCBI nr-aa BLAST: CBRC-SARA-01-1488 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-SARA-01-1488 ref|ZP_01187451.1| conserved hypothetical protein [Bacillus weihenstep...hanensis KBAB4] gb|EAR73176.1| conserved hypothetical protein [Bacillus weihenstephanensis KBAB4] ZP_01187451.1 0.78 25% ...

Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway*

Science.gov (United States)

Barta, Michael L.; Thomas, Keisha; Yuan, Hongling; Lovell, Scott; Battaile, Kevin P.; Schramm, Vern L.; Hefty, P. Scott

2014-01-01

The obligate intracellular human pathogen Chlamydia trachomatis is the etiological agent of blinding trachoma and sexually transmitted disease. Genomic sequencing of Chlamydia indicated this medically important bacterium was not exclusively dependent on the host cell for energy. In order for the electron transport chain to function, electron shuttling between membrane-embedded complexes requires lipid-soluble quinones (e.g. menaquionone or ubiquinone). The sources or biosynthetic pathways required to obtain these electron carriers within C. trachomatis are poorly understood. The 1.58Å crystal structure of C. trachomatis hypothetical protein CT263 presented here supports a role in quinone biosynthesis. Although CT263 lacks sequence-based functional annotation, the crystal structure of CT263 displays striking structural similarity to 5′-methylthioadenosine nucleosidase (MTAN) enzymes. Although CT263 lacks the active site-associated dimer interface found in prototypical MTANs, co-crystal structures with product (adenine) or substrate (5′-methylthioadenosine) indicate that the canonical active site residues are conserved. Enzymatic characterization of CT263 indicates that the futalosine pathway intermediate 6-amino-6-deoxyfutalosine (kcat/Km = 1.8 × 103 m−1 s−1), but not the prototypical MTAN substrates (e.g. S-adenosylhomocysteine and 5′-methylthioadenosine), is hydrolyzed. Bioinformatic analyses of the chlamydial proteome also support the futalosine pathway toward the synthesis of menaquinone in Chlamydiaceae. This report provides the first experimental support for quinone synthesis in Chlamydia. Menaquinone synthesis provides another target for agents to combat C. trachomatis infection. PMID:25253688

NCBI nr-aa BLAST: CBRC-DMEL-02-0082 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DMEL-02-0082 ref|ZP_01510105.1| conserved hypothetical protein [Burkholderia phytofirm...ans PsJN] gb|EAV05658.1| conserved hypothetical protein [Burkholderia phytofirmans PsJN] ZP_01510105.1 5e-08 25% ...

NCBI nr-aa BLAST: CBRC-OSAT-04-0001 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OSAT-04-0001 ref|ZP_02021447.1| conserved hypothetical protein [Methylobacterium extorque...ns PA1] gb|EDN51662.1| conserved hypothetical protein [Methylobacterium extorquens PA1] ZP_02021447.1 8e-05 30% ...

NCBI nr-aa BLAST: CBRC-DDIS-03-0039 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DDIS-03-0039 ref|XP_001209647.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU32345.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001209647.1 2e-30 37% ...

NCBI nr-aa BLAST: CBRC-DDIS-06-0058 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DDIS-06-0058 ref|XP_001216414.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU32055.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001216414.1 4e-75 44% ...

NCBI nr-aa BLAST: CBRC-DDIS-03-0055 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DDIS-03-0055 ref|XP_001211162.1| conserved hypothetical protein [Aspergillus terre...us NIH2624] gb|EAU36946.1| conserved hypothetical protein [Aspergillus terreus NIH2624] XP_001211162.1 1e-10 22% ...

NCBI nr-aa BLAST: CBRC-FRUB-02-0883 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-FRUB-02-0883 ref|ZP_01184818.1| conserved hypothetical protein [Bacillus weihenstep...hanensis KBAB4] gb|EAR75842.1| conserved hypothetical protein [Bacillus weihenstephanensis KBAB4] ZP_01184818.1 4e-58 59% ...

NCBI nr-aa BLAST: CBRC-OLAT-20-0021 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OLAT-20-0021 ref|ZP_01185507.1| conserved hypothetical protein [Bacillus weihenstep...hanensis KBAB4] gb|EAR75137.1| conserved hypothetical protein [Bacillus weihenstephanensis KBAB4] ZP_01185507.1 3e-27 45% ...

NCBI nr-aa BLAST: CBRC-DDIS-02-0008 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DDIS-02-0008 ref|ZP_00515102.1| conserved hypothetical protein [Crocosphaera watson...ii WH 8501] gb|EAM51937.1| conserved hypothetical protein [Crocosphaera watsonii WH 8501] ZP_00515102.1 5e-10 32% ...

Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.

Science.gov (United States)

Varadi, Mihaly; Zsolyomi, Fruzsina; Guharoy, Mainak; Tompa, Peter

2015-01-01

Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disordered protein segments in RNA-binding is two-fold: first, these regions establish extended, conserved electrostatic interfaces with RNAs via induced fit. Second, conformational flexibility enables them to target different RNA partners, providing multi-functionality, while also ensuring specificity. These findings emphasize the functional importance of intrinsically disordered regions in RNA-binding proteins.

Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.

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Mihaly Varadi

Full Text Available Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disordered protein segments in RNA-binding is two-fold: first, these regions establish extended, conserved electrostatic interfaces with RNAs via induced fit. Second, conformational flexibility enables them to target different RNA partners, providing multi-functionality, while also ensuring specificity. These findings emphasize the functional importance of intrinsically disordered regions in RNA-binding proteins.

NCBI nr-aa BLAST: CBRC-OCUN-01-1138 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OCUN-01-1138 ref|ZP_01462700.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU66540.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01462700.1 2e-04 25% ...

NCBI nr-aa BLAST: CBRC-SARA-01-0322 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-SARA-01-0322 ref|ZP_01459778.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU69359.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01459778.1 5.2 34% ...

NCBI nr-aa BLAST: CBRC-AGAM-01-0080 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-AGAM-01-0080 ref|ZP_01467057.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU62171.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01467057.1 4e-06 30% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-2878 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-2878 ref|ZP_01460012.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU69116.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01460012.1 3.2 36% ...

NCBI nr-aa BLAST: CBRC-XTRO-01-3254 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-XTRO-01-3254 ref|ZP_01462094.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU67090.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01462094.1 3e-07 26% ...

NCBI nr-aa BLAST: CBRC-OANA-01-2012 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OANA-01-2012 ref|ZP_01465587.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU63646.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01465587.1 0.73 40% ...

NCBI nr-aa BLAST: CBRC-OCUN-01-0401 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OCUN-01-0401 ref|ZP_01467058.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU62172.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01467058.1 0.003 26% ...

NCBI nr-aa BLAST: CBRC-MDOM-03-0382 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-MDOM-03-0382 ref|ZP_01466460.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU62763.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01466460.1 0.010 27% ...

NCBI nr-aa BLAST: CBRC-OCUN-01-1138 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-OCUN-01-1138 ref|ZP_01467057.1| conserved hypothetical protein [Stigmatella au...rantiaca DW4/3-1] gb|EAU62171.1| conserved hypothetical protein [Stigmatella aurantiaca DW4/3-1] ZP_01467057.1 0.001 27% ...

Functionality of system components: Conservation of protein function in protein feature space

DEFF Research Database (Denmark)

Jensen, Lars Juhl; Ussery, David; Brunak, Søren

2003-01-01

well on organisms other than the one on which it was trained. We evaluate the performance of such a method, ProtFun, which relies on protein features as its sole input, and show that the method gives similar performance for most eukaryotes and performs much better than anticipated on archaea......Many protein features useful for prediction of protein function can be predicted from sequence, including posttranslational modifications, subcellular localization, and physical/chemical properties. We show here that such protein features are more conserved among orthologs than paralogs, indicating...... they are crucial for protein function and thus subject to selective pressure. This means that a function prediction method based on sequence-derived features may be able to discriminate between proteins with different function even when they have highly similar structure. Also, such a method is likely to perform...

Structure-sequence based analysis for identification of conserved regions in proteins

Science.gov (United States)

Zemla, Adam T; Zhou, Carol E; Lam, Marisa W; Smith, Jason R; Pardes, Elizabeth

2013-05-28

Disclosed are computational methods, and associated hardware and software products for scoring conservation in a protein structure based on a computationally identified family or cluster of protein structures. A method of computationally identifying a family or cluster of protein structures in also disclosed herein.

Protein conservation and variation suggest mechanisms of cell type-specific modulation of signaling pathways.

Directory of Open Access Journals (Sweden)

Martin H Schaefer

2014-06-01

Full Text Available Many proteins and signaling pathways are present in most cell types and tissues and yet perform specialized functions. To elucidate mechanisms by which these ubiquitous pathways are modulated, we overlaid information about cross-cell line protein abundance and variability, and evolutionary conservation onto functional pathway components and topological layers in the pathway hierarchy. We found that the input (receptors and the output (transcription factors layers evolve more rapidly than proteins in the intermediary transmission layer. In contrast, protein expression variability decreases from the input to the output layer. We observed that the differences in protein variability between the input and transmission layer can be attributed to both the network position and the tendency of variable proteins to physically interact with constitutively expressed proteins. Differences in protein expression variability and conservation are also accompanied by the tendency of conserved and constitutively expressed proteins to acquire somatic mutations, while germline mutations tend to occur in cell type-specific proteins. Thus, conserved core proteins in the transmission layer could perform a fundamental role in most cell types and are therefore less tolerant to germline mutations. In summary, we propose that the core signal transmission machinery is largely modulated by a variable input layer through physical protein interactions. We hypothesize that the bow-tie organization of cellular signaling on the level of protein abundance variability contributes to the specificity of the signal response in different cell types.

Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea

OpenAIRE

Guo, Li; Feng, Yingang; Zhang, Zhenfeng; Yao, Hongwei; Luo, Yuanming; Wang, Jinfeng; Huang, Li

2007-01-01

Archaea contain a variety of chromatin proteins consistent with the evolution of different genome packaging mechanisms. Among the two main kingdoms in the Archaea, Euryarchaeota synthesize histone homologs, whereas Crenarchaeota have not been shown to possess a chromatin protein conserved at the kingdom level. We report the identification of Cren7, a novel family of chromatin proteins highly conserved in the Crenarchaeota. A small, basic, methylated and abundant protein, Cren7 displays a high...

Effect of the deletion of qmoABC and the promoter distal gene encoding a hypothetical protein on sulfate-reduction in Desulfovibrio vulgaris Hildenborough

Energy Technology Data Exchange (ETDEWEB)

Zane, Grant M.; Yen, Huei-chi Bill; Wall, Judy D.

2010-03-18

The pathway of electrons required for the reduction of sulfate in sulfate-reducing bacteria (SRB) is not yet fully characterized. In order to determine the role of a transmembrane protein complex suggested to be involved in this process, a deletion of Desulfovibrio vulgaris Hildenborough was created by marker exchange mutagenesis that eliminated four genes putatively encoding the QmoABC complex and a hypothetical protein (DVU0851). The Qmo complex (quinone-interacting membrane-bound oxidoreductase) is proposed to be responsible for transporting electrons to the dissimilatory adenosine-5?phosphosulfate (APS) reductase in SRB. In support of the predicted role of this complex, the deletion mutant was unable to grow using sulfate as its sole electron acceptor with a range of electron donors. To explore a possible role for the hypothetical protein in sulfate reduction, a second mutant was constructed that had lost only the gene that codes for DVU0851. The second constructed mutant grew with sulfate as the sole electron acceptor; however, there was a lag that was not present with the wild-type or complemented strain. Neither deletion strain was significantly impaired for growth with sulfite or thiosulfate as terminal electron acceptor. Complementation of the D(qmoABC-DVU0851) mutant with all four genes or only the qmoABC genes restored its ability to grow by sulfate respiration. These results confirmed the prediction that the Qmo complex is in the electron pathway for sulfate-reduction and revealed that no other transmembrane complex could compensate when Qmo was lacking.

The conservation pattern of short linear motifs is highly correlated with the function of interacting protein domains

Directory of Open Access Journals (Sweden)

Wang Yiguo

2008-10-01

Full Text Available Abstract Background Many well-represented domains recognize primary sequences usually less than 10 amino acids in length, called Short Linear Motifs (SLiMs. Accurate prediction of SLiMs has been difficult because they are short (often Results Our combined approach revealed that SLiMs are highly conserved in proteins from functional classes that are known to interact with a specific domain, but that they are not conserved in most other protein groups. We found that SLiMs recognized by SH2 domains were highly conserved in receptor kinases/phosphatases, adaptor molecules, and tyrosine kinases/phosphatases, that SLiMs recognized by SH3 domains were highly conserved in cytoskeletal and cytoskeletal-associated proteins, that SLiMs recognized by PDZ domains were highly conserved in membrane proteins such as channels and receptors, and that SLiMs recognized by S/T kinase domains were highly conserved in adaptor molecules, S/T kinases/phosphatases, and proteins involved in transcription or cell cycle control. We studied Tyr-SLiMs recognized by SH2 domains in more detail, and found that SH2-recognized Tyr-SLiMs on the cytoplasmic side of membrane proteins are more highly conserved than those on the extra-cellular side. Also, we found that SH2-recognized Tyr-SLiMs that are associated with SH3 motifs and a tyrosine kinase phosphorylation motif are more highly conserved. Conclusion The interactome of protein domains is reflected by the evolutionary conservation of SLiMs recognized by these domains. Combining scoring matrixes derived from peptide libraries and conservation analysis, we would be able to find those protein groups that are more likely to interact with specific domains.

Bacterial periplasmic sialic acid-binding proteins exhibit a conserved binding site

Energy Technology Data Exchange (ETDEWEB)

Gangi Setty, Thanuja [Institute for Stem Cell Biology and Regenerative Medicine, NCBS Campus, GKVK Post, Bangalore, Karnataka 560 065 (India); Cho, Christine [Carver College of Medicine, University of Iowa, Iowa City, IA 52242-1109 (United States); Govindappa, Sowmya [Institute for Stem Cell Biology and Regenerative Medicine, NCBS Campus, GKVK Post, Bangalore, Karnataka 560 065 (India); Apicella, Michael A. [Carver College of Medicine, University of Iowa, Iowa City, IA 52242-1109 (United States); Ramaswamy, S., E-mail: ramas@instem.res.in [Institute for Stem Cell Biology and Regenerative Medicine, NCBS Campus, GKVK Post, Bangalore, Karnataka 560 065 (India)

2014-07-01

Structure–function studies of sialic acid-binding proteins from F. nucleatum, P. multocida, V. cholerae and H. influenzae reveal a conserved network of hydrogen bonds involved in conformational change on ligand binding. Sialic acids are a family of related nine-carbon sugar acids that play important roles in both eukaryotes and prokaryotes. These sialic acids are incorporated/decorated onto lipooligosaccharides as terminal sugars in multiple bacteria to evade the host immune system. Many pathogenic bacteria scavenge sialic acids from their host and use them for molecular mimicry. The first step of this process is the transport of sialic acid to the cytoplasm, which often takes place using a tripartite ATP-independent transport system consisting of a periplasmic binding protein and a membrane transporter. In this paper, the structural characterization of periplasmic binding proteins from the pathogenic bacteria Fusobacterium nucleatum, Pasteurella multocida and Vibrio cholerae and their thermodynamic characterization are reported. The binding affinities of several mutations in the Neu5Ac binding site of the Haemophilus influenzae protein are also reported. The structure and the thermodynamics of the binding of sugars suggest that all of these proteins have a very well conserved binding pocket and similar binding affinities. A significant conformational change occurs when these proteins bind the sugar. While the C1 carboxylate has been identified as the primary binding site, a second conserved hydrogen-bonding network is involved in the initiation and stabilization of the conformational states.

Bacterial periplasmic sialic acid-binding proteins exhibit a conserved binding site

International Nuclear Information System (INIS)

Gangi Setty, Thanuja; Cho, Christine; Govindappa, Sowmya; Apicella, Michael A.; Ramaswamy, S.

2014-01-01

Structure–function studies of sialic acid-binding proteins from F. nucleatum, P. multocida, V. cholerae and H. influenzae reveal a conserved network of hydrogen bonds involved in conformational change on ligand binding. Sialic acids are a family of related nine-carbon sugar acids that play important roles in both eukaryotes and prokaryotes. These sialic acids are incorporated/decorated onto lipooligosaccharides as terminal sugars in multiple bacteria to evade the host immune system. Many pathogenic bacteria scavenge sialic acids from their host and use them for molecular mimicry. The first step of this process is the transport of sialic acid to the cytoplasm, which often takes place using a tripartite ATP-independent transport system consisting of a periplasmic binding protein and a membrane transporter. In this paper, the structural characterization of periplasmic binding proteins from the pathogenic bacteria Fusobacterium nucleatum, Pasteurella multocida and Vibrio cholerae and their thermodynamic characterization are reported. The binding affinities of several mutations in the Neu5Ac binding site of the Haemophilus influenzae protein are also reported. The structure and the thermodynamics of the binding of sugars suggest that all of these proteins have a very well conserved binding pocket and similar binding affinities. A significant conformational change occurs when these proteins bind the sugar. While the C1 carboxylate has been identified as the primary binding site, a second conserved hydrogen-bonding network is involved in the initiation and stabilization of the conformational states

NCBI nr-aa BLAST: CBRC-XTRO-01-1320 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-XTRO-01-1320 ref|YP_001100294.1| hypothetical protein HEAR2027 [Herminiimonas arsenico...xydans] emb|CAL62171.1| conserved hypothetical protein; putative membrane protein [Herminiimonas arsenicoxydans] YP_001100294.1 0.0 93% ...

When Heterotrimeric G Proteins Are Not Activated by G Protein-Coupled Receptors: Structural Insights and Evolutionary Conservation.

Science.gov (United States)

DiGiacomo, Vincent; Marivin, Arthur; Garcia-Marcos, Mikel

2018-01-23

Heterotrimeric G proteins are signal-transducing switches conserved across eukaryotes. In humans, they work as critical mediators of intercellular communication in the context of virtually any physiological process. While G protein regulation by G protein-coupled receptors (GPCRs) is well-established and has received much attention, it has become recently evident that heterotrimeric G proteins can also be activated by cytoplasmic proteins. However, this alternative mechanism of G protein regulation remains far less studied than GPCR-mediated signaling. This Viewpoint focuses on recent advances in the characterization of a group of nonreceptor proteins that contain a sequence dubbed the "Gα-binding and -activating (GBA) motif". So far, four proteins present in mammals [GIV (also known as Girdin), DAPLE, CALNUC, and NUCB2] and one protein in Caenorhabditis elegans (GBAS-1) have been described as possessing a functional GBA motif. The GBA motif confers guanine nucleotide exchange factor activity on Gαi subunits in vitro and activates G protein signaling in cells. The importance of this mechanism of signal transduction is highlighted by the fact that its dysregulation underlies human diseases, such as cancer, which has made the proteins attractive new candidates for therapeutic intervention. Here we discuss recent discoveries on the structural basis of GBA-mediated activation of G proteins and its evolutionary conservation and compare them with the better-studied mechanism mediated by GPCRs.

NCBI nr-aa BLAST: CBRC-MMUR-01-0729 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-MMUR-01-0729 ref|YP_001601963.1| hypothetical protein GDI_1718 [Gluconacetobacter diazo...trophicus PAl 5] ref|YP_002277838.1| hypothetical protein Gdia_3499 [Gluconacetobacter diazotrophic...us PAl 5] emb|CAP55661.1| putative membrane protein [Gluconacetobacter diazotrophicus PAl 5] gb|ACI53223.1| ...conserved hypothetical protein [Gluconacetobacter diazotrophicus PAl 5] YP_001601963.1 0.11 24% ...

Conservation and variability of dengue virus proteins: implications for vaccine design.

Directory of Open Access Journals (Sweden)

Asif M Khan

2008-08-01

Full Text Available Genetic variation and rapid evolution are hallmarks of RNA viruses, the result of high mutation rates in RNA replication and selection of mutants that enhance viral adaptation, including the escape from host immune responses. Variability is uneven across the genome because mutations resulting in a deleterious effect on viral fitness are restricted. RNA viruses are thus marked by protein sites permissive to multiple mutations and sites critical to viral structure-function that are evolutionarily robust and highly conserved. Identification and characterization of the historical dynamics of the conserved sites have relevance to multiple applications, including potential targets for diagnosis, and prophylactic and therapeutic purposes.We describe a large-scale identification and analysis of evolutionarily highly conserved amino acid sequences of the entire dengue virus (DENV proteome, with a focus on sequences of 9 amino acids or more, and thus immune-relevant as potential T-cell determinants. DENV protein sequence data were collected from the NCBI Entrez protein database in 2005 (9,512 sequences and again in 2007 (12,404 sequences. Forty-four (44 sequences (pan-DENV sequences, mainly those of nonstructural proteins and representing approximately 15% of the DENV polyprotein length, were identical in 80% or more of all recorded DENV sequences. Of these 44 sequences, 34 ( approximately 77% were present in >or=95% of sequences of each DENV type, and 27 ( approximately 61% were conserved in other Flaviviruses. The frequencies of variants of the pan-DENV sequences were low (0 to approximately 5%, as compared to variant frequencies of approximately 60 to approximately 85% in the non pan-DENV sequence regions. We further showed that the majority of the conserved sequences were immunologically relevant: 34 contained numerous predicted human leukocyte antigen (HLA supertype-restricted peptide sequences, and 26 contained T-cell determinants identified by

Global Conservation of Protein Status between Cell Lines and Xenografts

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Julian Biau

2016-08-01

Full Text Available Common preclinical models for testing anticancer treatment include cultured human tumor cell lines in monolayer, and xenografts derived from these cell lines in immunodeficient mice. Our goal was to determine how similar the xenografts are compared with their original cell line and to determine whether it is possible to predict the stability of a xenograft model beforehand. We studied a selection of 89 protein markers of interest in 14 human cell cultures and respective subcutaneous xenografts using the reverse-phase protein array technology. We specifically focused on proteins and posttranslational modifications involved in DNA repair, PI3K pathway, apoptosis, tyrosine kinase signaling, stress, cell cycle, MAPK/ERK signaling, SAPK/JNK signaling, NFκB signaling, and adhesion/cytoskeleton. Using hierarchical clustering, most cell culture-xenograft pairs cluster together, suggesting a global conservation of protein signature. Particularly, Akt, NFkB, EGFR, and Vimentin showed very stable protein expression and phosphorylation levels highlighting that 4 of 10 pathways were highly correlated whatever the model. Other proteins were heterogeneously conserved depending on the cell line. Finally, cell line models with low Akt pathway activation and low levels of Vimentin gave rise to more reliable xenograft models. These results may be useful for the extrapolation of cell culture experiments to in vivo models in novel targeted drug discovery.

Proteomic Analysis of Pathogenic Fungi Reveals Highly Expressed Conserved Cell Wall Proteins

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Jackson Champer

2016-01-01

Full Text Available We are presenting a quantitative proteomics tally of the most commonly expressed conserved fungal proteins of the cytosol, the cell wall, and the secretome. It was our goal to identify fungi-typical proteins that do not share significant homology with human proteins. Such fungal proteins are of interest to the development of vaccines or drug targets. Protein samples were derived from 13 fungal species, cultured in rich or in minimal media; these included clinical isolates of Aspergillus, Candida, Mucor, Cryptococcus, and Coccidioides species. Proteomes were analyzed by quantitative MSE (Mass Spectrometry—Elevated Collision Energy. Several thousand proteins were identified and quantified in total across all fractions and culture conditions. The 42 most abundant proteins identified in fungal cell walls or supernatants shared no to very little homology with human proteins. In contrast, all but five of the 50 most abundant cytosolic proteins had human homologs with sequence identity averaging 59%. Proteomic comparisons of the secreted or surface localized fungal proteins highlighted conserved homologs of the Aspergillus fumigatus proteins 1,3-β-glucanosyltransferases (Bgt1, Gel1-4, Crf1, Ecm33, EglC, and others. The fact that Crf1 and Gel1 were previously shown to be promising vaccine candidates, underlines the value of the proteomics data presented here.

Relationships between residue Voronoi volume and sequence conservation in proteins.

Science.gov (United States)

Liu, Jen-Wei; Cheng, Chih-Wen; Lin, Yu-Feng; Chen, Shao-Yu; Hwang, Jenn-Kang; Yen, Shih-Chung

2018-02-01

Functional and biophysical constraints can cause different levels of sequence conservation in proteins. Previously, structural properties, e.g., relative solvent accessibility (RSA) and packing density of the weighted contact number (WCN), have been found to be related to protein sequence conservation (CS). The Voronoi volume has recently been recognized as a new structural property of the local protein structural environment reflecting CS. However, for surface residues, it is sensitive to water molecules surrounding the protein structure. Herein, we present a simple structural determinant termed the relative space of Voronoi volume (RSV); it uses the Voronoi volume and the van der Waals volume of particular residues to quantify the local structural environment. RSV (range, 0-1) is defined as (Voronoi volume-van der Waals volume)/Voronoi volume of the target residue. The concept of RSV describes the extent of available space for every protein residue. RSV and Voronoi profiles with and without water molecules (RSVw, RSV, VOw, and VO) were compared for 554 non-homologous proteins. RSV (without water) showed better Pearson's correlations with CS than did RSVw, VO, or VOw values. The mean correlation coefficient between RSV and CS was 0.51, which is comparable to the correlation between RSA and CS (0.49) and that between WCN and CS (0.56). RSV is a robust structural descriptor with and without water molecules and can quantitatively reflect evolutionary information in a single protein structure. Therefore, it may represent a practical structural determinant to study protein sequence, structure, and function relationships. Copyright © 2017 Elsevier B.V. All rights reserved.

Some epitopes conservation in non structural 3 protein dengue virus serotype 4

Directory of Open Access Journals (Sweden)

Tegar A. P. Siregar

2016-03-01

Full Text Available AbstrakLatar belakang: Protein Non Struktural 3 (NS3 virus dengue menginduksi respon antibodi netralisasidan respon sel T CD4+ dan CD8+, serta berperan dalam replikasi virus. Protein NS3 memiliki epitopepitopsel T dan B yang terdapat perbedaan kelestarian pada berbagai strain virus dengue serotipe 4(DENV-4. Penelitian ini bertujuan untuk mengetahui kelestarian epitop sel T dan B pada protein NS3DENV-4 strain-strain dunia dan keempat serotipe virus dengue strain Indonesia.Metode: Penelitian ini dilakukan di Departemen Mikrobiologi Fakultas Kedokteran UI sejak Juni 2013 - April2014. Sekuens asam amino NS3 DENV-4 strain 081 didapatkan setelah produk PCR gen NS3 DENV-4 081disekuensing. Epitop-epitop sel T dan sel B protein NS3 DENV-4 081 dianalisis dan dibandingkan dengansekuens asam amino protein NS3 dari 124 strain DENV-4 di dunia dan keempat serotipe DENV strain Indonesia.Strain-strain dunia merupakan strain yang ada di benua Amerika (Venezuela, Colombia, dll dan Asia (Cina,Singapura, dll. Referensi posisi epitop sel T dan B protein NS3 diperoleh dari laporan penelitian terdahulu.Hasil: Delapan epitop sel T dan 2 epitop sel B dari protein NS3 DENV-4 081 ternyata identik dan lestaripada protein NS3 dari 124 strain DENV-4 dunia. Epitop sel B di posisi asam amino 537-544 pada proteinNS3 DENV-4 081 ternyata identik dan lestari dengan epitop sel B protein NS3 dari keempat serotipeDENV strain Indonesia.Kesimpulan: Kelestarian yang luas dari epitop sel T dan B pada hampir seluruh strain DENV-4 dunia danserotipe-serotipe DENV strain Indonesia. (Health Science Journal of Indonesia 2015;6:126-31Kata kunci: virus dengue, protein NS3, epitop sel T, epitop sel B AbstractBackground: Non Structural 3 (NS3 protein of dengue virus (DENV is known to induce antibody, CD4+and CD8+ T cell responses, and playing role in viral replication. NS3 protein has T and B cell epitopes,which has conservation difference between DENV-4 strains. This study aimed to identify

Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea.

Science.gov (United States)

Guo, Li; Feng, Yingang; Zhang, Zhenfeng; Yao, Hongwei; Luo, Yuanming; Wang, Jinfeng; Huang, Li

2008-03-01

Archaea contain a variety of chromatin proteins consistent with the evolution of different genome packaging mechanisms. Among the two main kingdoms in the Archaea, Euryarchaeota synthesize histone homologs, whereas Crenarchaeota have not been shown to possess a chromatin protein conserved at the kingdom level. We report the identification of Cren7, a novel family of chromatin proteins highly conserved in the Crenarchaeota. A small, basic, methylated and abundant protein, Cren7 displays a higher affinity for double-stranded DNA than for single-stranded DNA, constrains negative DNA supercoils and is associated with genomic DNA in vivo. The solution structure and DNA-binding surface of Cren7 from the hyperthermophilic crenarchaeon Sulfolobus solfataricus were determined by NMR. The protein adopts an SH3-like fold. It interacts with duplex DNA through a beta-sheet and a long flexible loop, presumably resulting in DNA distortions through intercalation of conserved hydrophobic residues into the DNA structure. These data suggest that the crenarchaeal kingdom in the Archaea shares a common strategy in chromatin organization.

Homologous high-throughput expression and purification of highly conserved E coli proteins

Directory of Open Access Journals (Sweden)

Duchmann Rainer

2007-06-01

Full Text Available Abstract Background Genetic factors and a dysregulated immune response towards commensal bacteria contribute to the pathogenesis of Inflammatory Bowel Disease (IBD. Animal models demonstrated that the normal intestinal flora is crucial for the development of intestinal inflammation. However, due to the complexity of the intestinal flora, it has been difficult to design experiments for detection of proinflammatory bacterial antigen(s involved in the pathogenesis of the disease. Several studies indicated a potential association of E. coli with IBD. In addition, T cell clones of IBD patients were shown to cross react towards antigens from different enteric bacterial species and thus likely responded to conserved bacterial antigens. We therefore chose highly conserved E. coli proteins as candidate antigens for abnormal T cell responses in IBD and used high-throughput techniques for cloning, expression and purification under native conditions of a set of 271 conserved E. coli proteins for downstream immunologic studies. Results As a standardized procedure, genes were PCR amplified and cloned into the expression vector pQTEV2 in order to express proteins N-terminally fused to a seven-histidine-tag. Initial small-scale expression and purification under native conditions by metal chelate affinity chromatography indicated that the vast majority of target proteins were purified in high yields. Targets that revealed low yields after purification probably due to weak solubility were shuttled into Gateway (Invitrogen destination vectors in order to enhance solubility by N-terminal fusion of maltose binding protein (MBP, N-utilizing substance A (NusA, or glutathione S-transferase (GST to the target protein. In addition, recombinant proteins were treated with polymyxin B coated magnetic beads in order to remove lipopolysaccharide (LPS. Thus, 73% of the targeted proteins could be expressed and purified in large-scale to give soluble proteins in the range of 500

NCBI nr-aa BLAST: CBRC-BTAU-01-2645 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-BTAU-01-2645 ref|YP_069190.1| hypothetical protein YPTB0648 [Yersinia pseudotuberculosis... IP 32953] emb|CAH19888.1| conserved hypothetical protein [Yersinia pseudotuberculosis IP 32953] YP_069190.1 0.001 29% ...

NCBI nr-aa BLAST: CBRC-LAFR-01-0236 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-LAFR-01-0236 ref|NP_336748.1| hypothetical protein MT2277 [Mycobacterium tuberculosis... CDC1551] gb|AAK46562.1| conserved hypothetical protein [Mycobacterium tuberculosis CDC1551] NP_336748.1 2.0 34% ...

NCBI nr-aa BLAST: CBRC-LAFR-01-0796 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-LAFR-01-0796 ref|YP_956143.1| hypothetical protein Mvan_5366 [Mycobacterium vanba...alenii PYR-1] gb|ABM16137.1| conserved hypothetical protein [Mycobacterium vanbaalenii PYR-1] YP_956143.1 0.011 41% ...

NCBI nr-aa BLAST: CBRC-CJAC-01-0736 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CJAC-01-0736 ref|YP_953764.1| hypothetical protein Mvan_2952 [Mycobacterium vanba...alenii PYR-1] gb|ABM13758.1| conserved hypothetical protein [Mycobacterium vanbaalenii PYR-1] YP_953764.1 0.60 31% ...

NCBI nr-aa BLAST: CBRC-ACAR-01-0074 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-ACAR-01-0074 ref|YP_317715.1| hypothetical protein Nwi_1101 [Nitrobacter winogradsky...i Nb-255] gb|ABA04363.1| conserved hypothetical protein [Nitrobacter winogradskyi Nb-255] YP_317715.1 6.5 24% ...

NCBI nr-aa BLAST: CBRC-EEUR-01-0426 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-EEUR-01-0426 ref|YP_069190.1| hypothetical protein YPTB0648 [Yersinia pseudotuberculosis... IP 32953] emb|CAH19888.1| conserved hypothetical protein [Yersinia pseudotuberculosis IP 32953] YP_069190.1 3e-11 31% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-2631 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-2631 ref|YP_016140.1| hypothetical protein MMOB4430 [Mycoplasma mobile... 163K] gb|AAT27929.1| conserved hypothetical membrane protein [Mycoplasma mobile 163K] YP_016140.1 0.008 27% ...

NCBI nr-aa BLAST: CBRC-TGUT-17-0005 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TGUT-17-0005 ref|YP_864863.1| hypothetical protein Mmc1_0939 [Magnetococcus sp.... MC-1] gb|ABK43457.1| conserved hypothetical protein [Magnetococcus sp. MC-1] YP_864863.1 0.94 32% ...

NCBI nr-aa BLAST: CBRC-LAFR-01-1699 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-LAFR-01-1699 ref|YP_065279.1| hypothetical protein DP1543 [Desulfotalea psychr...ophila LSv54] emb|CAG36272.1| conserved hypothetical protein [Desulfotalea psychrophila LSv54] YP_065279.1 0.69 29% ...

NCBI nr-aa BLAST: CBRC-ETEL-01-0213 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-ETEL-01-0213 ref|YP_065102.1| hypothetical protein DP1366 [Desulfotalea psychr...ophila LSv54] emb|CAG36095.1| conserved hypothetical protein [Desulfotalea psychrophila LSv54] YP_065102.1 6.0 22% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-0335 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-0335 ref|YP_001430589.1| hypothetical protein Rcas_0440 [Roseiflexus c...astenholzii DSM 13941] gb|ABU56571.1| conserved hypothetical protein [Roseiflexus castenholzii DSM 13941] YP_001430589.1 1.6 30% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0933 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0933 ref|YP_001430412.1| hypothetical protein Rcas_0261 [Roseiflexus c...astenholzii DSM 13941] gb|ABU56394.1| conserved hypothetical protein [Roseiflexus castenholzii DSM 13941] YP_001430412.1 4.6 32% ...

NCBI nr-aa BLAST: CBRC-BTAU-01-2676 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-BTAU-01-2676 ref|YP_678738.1| hypothetical protein CHU_2133 [Cytophaga hutchinson...ii ATCC 33406] gb|ABG59396.1| conserved hypothetical protein [Cytophaga hutchinsonii ATCC 33406] YP_678738.1 0.11 23% ...

NCBI nr-aa BLAST: CBRC-PMAR-01-0373 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PMAR-01-0373 ref|YP_676710.1| hypothetical protein CHU_0076 [Cytophaga hutchinson...ii ATCC 33406] gb|ABG57370.1| conserved hypothetical protein [Cytophaga hutchinsonii ATCC 33406] YP_676710.1 8.8 25% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-1085 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-1085 ref|YP_678347.1| hypothetical protein CHU_1738 [Cytophaga hutchinson...ii ATCC 33406] gb|ABG59005.1| conserved hypothetical protein [Cytophaga hutchinsonii ATCC 33406] YP_678347.1 0.90 23% ...

NCBI nr-aa BLAST: CBRC-XTRO-01-2145 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-XTRO-01-2145 ref|YP_676712.1| hypothetical protein CHU_0078 [Cytophaga hutchinson...ii ATCC 33406] gb|ABG57372.1| conserved hypothetical protein [Cytophaga hutchinsonii ATCC 33406] YP_676712.1 0.16 24% ...

NCBI nr-aa BLAST: CBRC-PMAR-01-0605 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PMAR-01-0605 ref|YP_950947.1| hypothetical protein Mvan_0090 [Mycobacterium vanba...alenii PYR-1] gb|ABM10941.1| conserved hypothetical protein [Mycobacterium vanbaalenii PYR-1] YP_950947.1 1e-06 28% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-1927 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-1927 ref|YP_001357187.1| hypothetical protein NIS_1724 [Nitratiruptor ...sp. SB155-2] dbj|BAF70830.1| conserved hypothetical protein [Nitratiruptor sp. SB155-2] YP_001357187.1 2.1 27% ...

NCBI nr-aa BLAST: CBRC-GGAL-35-0388 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-GGAL-35-0388 ref|YP_184257.1| hypothetical protein TK1844 [Thermococcus kodaka...rensis KOD1] dbj|BAD86033.1| hypothetical membrane protein, conserved [Thermococcus kodakarensis KOD1] YP_184257.1 5.1 30% ...

NCBI nr-aa BLAST: CBRC-PMAR-01-0384 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PMAR-01-0384 ref|YP_439624.1| hypothetical protein BTH_II1428 [Burkholderia thailand...ensis E264] gb|ABC34039.1| conserved hypothetical protein [Burkholderia thailandensis E264] YP_439624.1 2.3 36% ...

NCBI nr-aa BLAST: CBRC-DRER-14-0059 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DRER-14-0059 ref|YP_683352.1| hypothetical protein RD1_3158 [Roseobacter denit...rificans OCh 114] gb|ABG32666.1| conserved hypothetical protein [Roseobacter denitrificans OCh 114] YP_683352.1 2.5 41% ...

NCBI nr-aa BLAST: CBRC-DRER-26-0529 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DRER-26-0529 ref|YP_683352.1| hypothetical protein RD1_3158 [Roseobacter denit...rificans OCh 114] gb|ABG32666.1| conserved hypothetical protein [Roseobacter denitrificans OCh 114] YP_683352.1 2.5 41% ...

NCBI nr-aa BLAST: CBRC-CJAC-01-0362 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CJAC-01-0362 ref|YP_001431476.1| hypothetical protein Rcas_1362 [Roseiflexus c...astenholzii DSM 13941] gb|ABU57458.1| conserved hypothetical protein [Roseiflexus castenholzii DSM 13941] YP_001431476.1 9e-05 36% ...

NCBI nr-aa BLAST: CBRC-TTRU-01-0085 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TTRU-01-0085 ref|YP_001648035.1| hypothetical protein BcerKBAB4_5264 [Bacillus weihenstep...hanensis KBAB4] gb|ABY46407.1| conserved hypothetical protein [Bacillus weihenstephanensis KBAB4] YP_001648035.1 0.002 26% ...

NCBI nr-aa BLAST: CBRC-SARA-01-1309 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-SARA-01-1309 ref|YP_001125845.1| hypothetical protein GTNG_1736 [Geobacillus thermoden...itrificans NG80-2] gb|ABO67100.1| Conserved hypothetical protein [Geobacillus thermodenitrificans NG80-2] YP_001125845.1 0.47 23% ...

NCBI nr-aa BLAST: CBRC-DNOV-01-2770 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DNOV-01-2770 ref|YP_925972.1| hypothetical protein Sama_0090 [Shewanella amazon...ensis SB2B] gb|ABL98302.1| conserved hypothetical protein [Shewanella amazonensis SB2B] YP_925972.1 1.8 34% ...

NCBI nr-aa BLAST: CBRC-DRER-26-0448 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-DRER-26-0448 ref|YP_682608.1| hypothetical protein RD1_2346 [Roseobacter denit...rificans OCh 114] gb|ABG31922.1| conserved hypothetical protein [Roseobacter denitrificans OCh 114] YP_682608.1 2e-89 38% ...

NCBI nr-aa BLAST: CBRC-PHAM-01-0706 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-PHAM-01-0706 ref|YP_001504998.1| hypothetical protein Franean1_0633 [Frankia s...p. EAN1pec] gb|ABW10092.1| conserved hypothetical protein [Frankia sp. EAN1pec] YP_001504998.1 0.63 35% ...

NCBI nr-aa BLAST: CBRC-LAFR-01-1090 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-LAFR-01-1090 ref|YP_001404451.1| hypothetical protein Mboo_1290 [Candidatus Methanoregula boo...nei 6A8] gb|ABS55808.1| conserved hypothetical protein [Candidatus Methanoregula boonei 6A8] YP_001404451.1 0.018 21% ...

Click chemistry for the conservation of cellular structures and fluorescent proteins: ClickOx.

Science.gov (United States)

Löschberger, Anna; Niehörster, Thomas; Sauer, Markus

2014-05-01

Reactive oxygen species (ROS), including hydrogen peroxide, are known to cause structural damage not only in living, but also in fixed, cells. Copper-catalyzed azide-alkyne cycloaddition (click chemistry) is known to produce ROS. Therefore, fluorescence imaging of cellular structures, such as the actin cytoskeleton, remains challenging when combined with click chemistry protocols. In addition, the production of ROS substantially weakens the fluorescence signal of fluorescent proteins. This led us to develop ClickOx, which is a new click chemistry protocol for improved conservation of the actin structure and better conservation of the fluorescence signal of green fluorescent protein (GFP)-fusion proteins. Herein we demonstrate that efficient oxygen removal by addition of an enzymatic oxygen scavenger system (ClickOx) considerably reduces ROS-associated damage during labeling of nascent DNA with ATTO 488 azide by Cu(I)-catalyzed click chemistry. Standard confocal and super-resolution fluorescence images of phalloidin-labeled actin filaments and GFP/yellow fluorescent protein-labeled cells verify the conservation of the cytoskeleton microstructure and fluorescence intensity, respectively. Thus, ClickOx can be used advantageously for structure preservation in conventional and most notably in super-resolution microscopy methods. Copyright © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

A computational tool to predict the evolutionarily conserved protein-protein interaction hot-spot residues from the structure of the unbound protein.

Science.gov (United States)

Agrawal, Neeraj J; Helk, Bernhard; Trout, Bernhardt L

2014-01-21

Identifying hot-spot residues - residues that are critical to protein-protein binding - can help to elucidate a protein's function and assist in designing therapeutic molecules to target those residues. We present a novel computational tool, termed spatial-interaction-map (SIM), to predict the hot-spot residues of an evolutionarily conserved protein-protein interaction from the structure of an unbound protein alone. SIM can predict the protein hot-spot residues with an accuracy of 36-57%. Thus, the SIM tool can be used to predict the yet unknown hot-spot residues for many proteins for which the structure of the protein-protein complexes are not available, thereby providing a clue to their functions and an opportunity to design therapeutic molecules to target these proteins. Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Extreme sequence divergence but conserved ligand-binding specificity in Streptococcus pyogenes M protein.

Directory of Open Access Journals (Sweden)

2006-05-01

Full Text Available Many pathogenic microorganisms evade host immunity through extensive sequence variability in a protein region targeted by protective antibodies. In spite of the sequence variability, a variable region commonly retains an important ligand-binding function, reflected in the presence of a highly conserved sequence motif. Here, we analyze the limits of sequence divergence in a ligand-binding region by characterizing the hypervariable region (HVR of Streptococcus pyogenes M protein. Our studies were focused on HVRs that bind the human complement regulator C4b-binding protein (C4BP, a ligand that confers phagocytosis resistance. A previous comparison of C4BP-binding HVRs identified residue identities that could be part of a binding motif, but the extended analysis reported here shows that no residue identities remain when additional C4BP-binding HVRs are included. Characterization of the HVR in the M22 protein indicated that two relatively conserved Leu residues are essential for C4BP binding, but these residues are probably core residues in a coiled-coil, implying that they do not directly contribute to binding. In contrast, substitution of either of two relatively conserved Glu residues, predicted to be solvent-exposed, had no effect on C4BP binding, although each of these changes had a major effect on the antigenic properties of the HVR. Together, these findings show that HVRs of M proteins have an extraordinary capacity for sequence divergence and antigenic variability while retaining a specific ligand-binding function.

Intragenic suppressor of Osiaa23 revealed a conserved tryptophan residue crucial for protein-protein interactions.

Directory of Open Access Journals (Sweden)

Jun Ni

Full Text Available The Auxin/Indole-3-Acetic Acid (Aux/IAA and Auxin Response Factor (ARF are two important families that play key roles in auxin signal transduction. Both of the families contain a similar carboxyl-terminal domain (Domain III/IV that facilitates interactions between these two families. In spite of the importance of protein-protein interactions among these transcription factors, the mechanisms involved in these interactions are largely unknown. In this study, we isolated six intragenic suppressors of an auxin insensitive mutant, Osiaa23. Among these suppressors, Osiaa23-R5 successfully rescued all the defects of the mutant. Sequence analysis revealed that an amino acid substitution occurred in the Tryptophan (W residue in Domain IV of Osiaa23. Yeast two-hybrid experiments showed that the mutation in Domain IV prevents the protein-protein interactions between Osiaa23 and OsARFs. Phylogenetic analysis revealed that the W residue is conserved in both OsIAAs and OsARFs. Next, we performed site-specific amino acid substitutions within Domain IV of OsARFs, and the conserved W in Domain IV was exchanged by Serine (S. The mutated OsARF(WSs can be released from the inhibition of Osiaa23 and maintain the transcriptional activities. Expression of OsARF(WSs in Osiaa23 mutant rescued different defects of the mutant. Our results suggest a previously unknown importance of Domain IV in both families and provide an indirect way to investigate functions of OsARFs.

Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites

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Sibley L David

2005-12-01

Full Text Available Abstract Background The phylum Apicomplexa is an early-branching eukaryotic lineage that contains a number of important human and animal pathogens. Their complex life cycles and unique cytoskeletal features distinguish them from other model eukaryotes. Apicomplexans rely on actin-based motility for cell invasion, yet the regulation of this system remains largely unknown. Consequently, we focused our efforts on identifying actin-related proteins in the recently completed genomes of Toxoplasma gondii, Plasmodium spp., Cryptosporidium spp., and Theileria spp. Results Comparative genomic and phylogenetic studies of apicomplexan genomes reveals that most contain only a single conventional actin and yet they each have 8–10 additional actin-related proteins. Among these are a highly conserved Arp1 protein (likely part of a conserved dynactin complex, and Arp4 and Arp6 homologues (subunits of the chromatin-remodeling machinery. In contrast, apicomplexans lack canonical Arp2 or Arp3 proteins, suggesting they lost the Arp2/3 actin polymerization complex on their evolutionary path towards intracellular parasitism. Seven of these actin-like proteins (ALPs are novel to apicomplexans. They show no phylogenetic associations to the known Arp groups and likely serve functions specific to this important group of intracellular parasites. Conclusion The large diversity of actin-like proteins in apicomplexans suggests that the actin protein family has diverged to fulfill various roles in the unique biology of intracellular parasites. Conserved Arps likely participate in vesicular transport and gene expression, while apicomplexan-specific ALPs may control unique biological traits such as actin-based gliding motility.

Conservation and divergence of ADAM family proteins in the Xenopus genome

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Shah Anoop

2010-07-01

Full Text Available Abstract Background Members of the disintegrin metalloproteinase (ADAM family play important roles in cellular and developmental processes through their functions as proteases and/or binding partners for other proteins. The amphibian Xenopus has long been used as a model for early vertebrate development, but genome-wide analyses for large gene families were not possible until the recent completion of the X. tropicalis genome sequence and the availability of large scale expression sequence tag (EST databases. In this study we carried out a systematic analysis of the X. tropicalis genome and uncovered several interesting features of ADAM genes in this species. Results Based on the X. tropicalis genome sequence and EST databases, we identified Xenopus orthologues of mammalian ADAMs and obtained full-length cDNA clones for these genes. The deduced protein sequences, synteny and exon-intron boundaries are conserved between most human and X. tropicalis orthologues. The alternative splicing patterns of certain Xenopus ADAM genes, such as adams 22 and 28, are similar to those of their mammalian orthologues. However, we were unable to identify an orthologue for ADAM7 or 8. The Xenopus orthologue of ADAM15, an active metalloproteinase in mammals, does not contain the conserved zinc-binding motif and is hence considered proteolytically inactive. We also found evidence for gain of ADAM genes in Xenopus as compared to other species. There is a homologue of ADAM10 in Xenopus that is missing in most mammals. Furthermore, a single scaffold of X. tropicalis genome contains four genes encoding ADAM28 homologues, suggesting genome duplication in this region. Conclusions Our genome-wide analysis of ADAM genes in X. tropicalis revealed both conservation and evolutionary divergence of these genes in this amphibian species. On the one hand, all ADAMs implicated in normal development and health in other species are conserved in X. tropicalis. On the other hand, some

The Number, Organization, and Size of Polymorphic Membrane Protein Coding Sequences as well as the Most Conserved Pmp Protein Differ within and across Chlamydia Species.

Science.gov (United States)

Van Lent, Sarah; Creasy, Heather Huot; Myers, Garry S A; Vanrompay, Daisy

2016-01-01

Variation is a central trait of the polymorphic membrane protein (Pmp) family. The number of pmp coding sequences differs between Chlamydia species, but it is unknown whether the number of pmp coding sequences is constant within a Chlamydia species. The level of conservation of the Pmp proteins has previously only been determined for Chlamydia trachomatis. As different Pmp proteins might be indispensible for the pathogenesis of different Chlamydia species, this study investigated the conservation of Pmp proteins both within and across C. trachomatis,C. pneumoniae,C. abortus, and C. psittaci. The pmp coding sequences were annotated in 16 C. trachomatis, 6 C. pneumoniae, 2 C. abortus, and 16 C. psittaci genomes. The number and organization of polymorphic membrane coding sequences differed within and across the analyzed Chlamydia species. The length of coding sequences of pmpA,pmpB, and pmpH was conserved among all analyzed genomes, while the length of pmpE/F and pmpG, and remarkably also of the subtype pmpD, differed among the analyzed genomes. PmpD, PmpA, PmpH, and PmpA were the most conserved Pmp in C. trachomatis,C. pneumoniae,C. abortus, and C. psittaci, respectively. PmpB was the most conserved Pmp across the 4 analyzed Chlamydia species. © 2016 S. Karger AG, Basel.

Conserved RNA-Binding Proteins Required for Dendrite Morphogenesis in Caenorhabditis elegans Sensory Neurons

Science.gov (United States)

Antonacci, Simona; Forand, Daniel; Wolf, Margaret; Tyus, Courtney; Barney, Julia; Kellogg, Leah; Simon, Margo A.; Kerr, Genevieve; Wells, Kristen L.; Younes, Serena; Mortimer, Nathan T.; Olesnicky, Eugenia C.; Killian, Darrell J.

2015-01-01

The regulation of dendritic branching is critical for sensory reception, cell−cell communication within the nervous system, learning, memory, and behavior. Defects in dendrite morphology are associated with several neurologic disorders; thus, an understanding of the molecular mechanisms that govern dendrite morphogenesis is important. Recent investigations of dendrite morphogenesis have highlighted the importance of gene regulation at the posttranscriptional level. Because RNA-binding proteins mediate many posttranscriptional mechanisms, we decided to investigate the extent to which conserved RNA-binding proteins contribute to dendrite morphogenesis across phyla. Here we identify a core set of RNA-binding proteins that are important for dendrite morphogenesis in the PVD multidendritic sensory neuron in Caenorhabditis elegans. Homologs of each of these genes were previously identified as important in the Drosophila melanogaster dendritic arborization sensory neurons. Our results suggest that RNA processing, mRNA localization, mRNA stability, and translational control are all important mechanisms that contribute to dendrite morphogenesis, and we present a conserved set of RNA-binding proteins that regulate these processes in diverse animal species. Furthermore, homologs of these genes are expressed in the human brain, suggesting that these RNA-binding proteins are candidate regulators of dendrite development in humans. PMID:25673135

Modelling of melting and solidification transport phenomena during hypothetical NPP severe accidents

International Nuclear Information System (INIS)

Sarler, B.

1992-01-01

A physical and mathematical framework to deal with the transport phenomena occuring during melting and solidification of the hypothetical NPP severe accidents is presented. It concentrates on the transient temperature, velocity, and species concentration distributions during such events. The framework is based on the Mixture Continuum Formulation of the components and phases, cast in the boundary-domain integral shape structured by the fundamental solution of the Laplace equation. The formulation could cope with various solid-liquid sub-systems through the inclusion of the specific closure relations. The deduced system of boundary-domain integral equations for conservation of mass, energy, momentum, and species could be solved by the boundary element discrete approximative method. (author) [sl

Reducing hypothetical bias in choice experiments

DEFF Research Database (Denmark)

Ladenburg, Jacob; Olsen, Søren Bøye; Nielsen, Rasmus Christian Fejer

eliminate some of the hypothetical bias. The present paper tests an addition to Cheap Talk, an Opt-Out Reminder. The Opt-Out Reminder is an objective short script presented prior to the choice sets, prompting the respondent to choose the opt-out alternative, if he/she finds the proposed policy generated...... alternatives in a choice set too expensive. The results suggest that adding an Opt-Out Reminder to Cheap Talk can in fact reduce hypothetical bias even further and reduces some of the ineffectiveness of CT in relation to the survey bid range and experienced respondents....

An evolutionarily conserved glycine-tyrosine motif forms a folding core in outer membrane proteins.

Directory of Open Access Journals (Sweden)

Marcin Michalik

Full Text Available An intimate interaction between a pair of amino acids, a tyrosine and glycine on neighboring β-strands, has been previously reported to be important for the structural stability of autotransporters. Here, we show that the conservation of this interacting pair extends to nearly all major families of outer membrane β-barrel proteins, which are thought to have originated through duplication events involving an ancestral ββ hairpin. We analyzed the function of this motif using the prototypical outer membrane protein OmpX. Stopped-flow fluorescence shows that two folding processes occur in the millisecond time regime, the rates of which are reduced in the tyrosine mutant. Folding assays further demonstrate a reduction in the yield of folded protein for the mutant compared to the wild-type, as well as a reduction in thermal stability. Taken together, our data support the idea of an evolutionarily conserved 'folding core' that affects the folding, membrane insertion, and thermal stability of outer membrane protein β-barrels.

Membrane Proteins Are Dramatically Less Conserved than Water-Soluble Proteins across the Tree of Life.

Science.gov (United States)

Sojo, Victor; Dessimoz, Christophe; Pomiankowski, Andrew; Lane, Nick

2016-11-01

Membrane proteins are crucial in transport, signaling, bioenergetics, catalysis, and as drug targets. Here, we show that membrane proteins have dramatically fewer detectable orthologs than water-soluble proteins, less than half in most species analyzed. This sparse distribution could reflect rapid divergence or gene loss. We find that both mechanisms operate. First, membrane proteins evolve faster than water-soluble proteins, particularly in their exterior-facing portions. Second, we demonstrate that predicted ancestral membrane proteins are preferentially lost compared with water-soluble proteins in closely related species of archaea and bacteria. These patterns are consistent across the whole tree of life, and in each of the three domains of archaea, bacteria, and eukaryotes. Our findings point to a fundamental evolutionary principle: membrane proteins evolve faster due to stronger adaptive selection in changing environments, whereas cytosolic proteins are under more stringent purifying selection in the homeostatic interior of the cell. This effect should be strongest in prokaryotes, weaker in unicellular eukaryotes (with intracellular membranes), and weakest in multicellular eukaryotes (with extracellular homeostasis). We demonstrate that this is indeed the case. Similarly, we show that extracellular water-soluble proteins exhibit an even stronger pattern of low homology than membrane proteins. These striking differences in conservation of membrane proteins versus water-soluble proteins have important implications for evolution and medicine. © The Author 2016. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

A Xanthomonas citri subsp citri hypothetical protein related to virulence contains a non-functional HD domain and is implicated in flagellar motility.

Science.gov (United States)

Vieira, F C F; Gonçalves, A M; Mendoza, E F R; Ferreira, R M; Costa, M L M; Balbuena, T S; Sebinelli, H G; Ciancaglini, P; Pizauro Junior, J M; Ferro, J A

2017-08-31

Citrus canker, caused by the Gram-negative bacterium Xanthomonas citri subsp citri (Xac), severely affects most economically important citrus varieties worldwide. A previous study showed that disruption of the ORF XAC1201 from the Xac 306 strain by transposon Tn5 decreased bacterium virulence in the Rangpur lime host (Citrus limonia L. Osbeck). However, little is known regarding the possible function of the hypothetical protein XAC1201 and how it affects the virulence of Xac 306. Here, we confirmed that disruption of ORF XAC1201 reduces Xac 306 virulence in two different hosts, delaying the onset of typical symptoms. In silico analysis suggested that XAC1201 interacts with the flagellar proteins FliM and FliL, known to be an important factor for virulence. In fact, motility assays revealed that the XAC1201 mutant has a significant difference in motility compared to the wild-type Xac 306. Also, a 3-D structure model revealed modified cofactor binding sites and suggested that XAC1201 has a non-functional HD domain. This hypothesis was confirmed by enzymatic assays performed in purified, XAC1201 recombinant protein expressed in Escherichia coli, which revealed no significant activities previously associated with HD domains for the tested substrates. Thus, the role of the XAC1201 protein in Xac 306 virulence seems to be related to flagellar motility, although a non-classic role for the HD domain cannot be dismissed.

Serum protein binding displacement: theoretical analysis using a hypothetical radiopharmaceutical and experimental analysis with 123I-N-isopropyl-p-iodoamphetamine

International Nuclear Information System (INIS)

Kawai, Keiichi; Nishii, Ryuichi; Shikano, Naoto; Makino, Nobuo; Kuga, Noriyuki; Yoshimoto, Mitsuyoshi; Jinnouchi, Seishi; Nagamachi, Shigeki; Tamura, Shozo; Takamura, Norito

2009-01-01

Introduction: The binding of radiopharmaceutical to serum proteins is thought to be an important factor that restricts its excretion and accumulation in tissue. We calculated the effect of inhibitors of serum protein binding using a hypothetical radiopharmaceutical. In vitro experiments and protein binding inhibitor-loaded monkey scintigraphy were then conducted using 123 I-N-isopropyl-p-iodoamphetamine (IMP) as the radiopharmaceutical. Methods: Free fraction ratios of radiopharmaceutical were calculated with one radiopharmaceutical, two serum proteins and two specific inhibitors in the steady state at various serum protein concentrations. In vitro protein binding inhibition studies using human, rat and monkey sera were performed with site-selective displacers of specific binding sites: 400 μM 6-methoxy-2-naphthylacetic acid (6MNA; a major nabumeton metabolite) as a serum albumin Site II inhibitor and 400 μM erythromycin (ETC) as an α 1 -acid glycoprotein (AGP) site inhibitor. Scintigraphy with or without 6MNA loading of monkeys was performed. Results: The theoretical findings roughly corresponded to the experimental results. Approximately 75% of IMP bound to serum albumin Site II and AGP in the species examined. The free fraction of IMP (25.0±0.6% for human, 22.8±0.4% for monkey, 23.7±0.3% for rat) increased with loading of specific protein binding inhibitors (6MNA: 28.0±0.3% for human, 24.5±0.7% for monkey, 24.3±0.2% for rat; ETC: 26.3±0.4% for human, 29.5±1.1% for monkey, 26.0±0.7% for rat) and was serum protein concentration dependant based on the results of calculations. Simultaneous administration of 6MNA and ETC produced a higher free fraction ratio of IMP (31.9±1.0% for human, 34.6±0.4% for monkey, 27.0±0.3% for rat) than summation of the single administrations of 6MNA and ETC (domino effect) in human, rat and monkey sera. Rapid cerebral accumulation was observed with 6MNA loading in monkey scintigraphy. Conclusions: 6MNA appears to change

Crystal structure of AFV3-109, a highly conserved protein from crenarchaeal viruses

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Quevillon-Cheruel Sophie

2007-01-01

Full Text Available Abstract The extraordinary morphologies of viruses infecting hyperthermophilic archaea clearly distinguish them from bacterial and eukaryotic viruses. Moreover, their genomes code for proteins that to a large extend have no related sequences in the extent databases. However, a small pool of genes is shared by overlapping subsets of these viruses, and the most conserved gene, exemplified by the ORF109 of the Acidianus Filamentous Virus 3, AFV3, is present on genomes of members of three viral familes, the Lipothrixviridae, Rudiviridae, and "Bicaudaviridae", as well as of the unclassified Sulfolobus Turreted Icosahedral Virus, STIV. We present here the crystal structure of the protein (Mr = 13.1 kD, 109 residues encoded by the AFV3 ORF 109 in two different crystal forms at 1.5 and 1.3 Å resolution. The structure of AFV3-109 is a five stranded β-sheet with loops on one side and three helices on the other. It forms a dimer adopting the shape of a cradle that encompasses the best conserved regions of the sequence. No protein with a related fold could be identified except for the ortholog from STIV1, whose structure was deposited at the Protein Data Bank. We could clearly identify a well bound glycerol inside the cradle, contacting exclusively totally conserved residues. This interaction was confirmed in solution by fluorescence titration. Although the function of AFV3-109 cannot be deduced directly from its structure, structural homology with the STIV1 protein, and the size and charge distribution of the cavity suggested it could interact with nucleic acids. Fluorescence quenching titrations also showed that AFV3-109 interacts with dsDNA. Genomic sequence analysis revealed bacterial homologs of AFV3-109 as a part of a putative previously unidentified prophage sequences in some Firmicutes.

Assessing the structural conservation of protein pockets to study functional and allosteric sites: implications for drug discovery

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Daura Xavier

2010-03-01

Full Text Available Abstract Background With the classical, active-site oriented drug-development approach reaching its limits, protein ligand-binding sites in general and allosteric sites in particular are increasingly attracting the interest of medicinal chemists in the search for new types of targets and strategies to drug development. Given that allostery represents one of the most common and powerful means to regulate protein function, the traditional drug discovery approach of targeting active sites can be extended by targeting allosteric or regulatory protein pockets that may allow the discovery of not only novel drug-like inhibitors, but activators as well. The wealth of available protein structural data can be exploited to further increase our understanding of allosterism, which in turn may have therapeutic applications. A first step in this direction is to identify and characterize putative effector sites that may be present in already available structural data. Results We performed a large-scale study of protein cavities as potential allosteric and functional sites, by integrating publicly available information on protein sequences, structures and active sites for more than a thousand protein families. By identifying common pockets across different structures of the same protein family we developed a method to measure the pocket's structural conservation. The method was first parameterized using known active sites. We characterized the predicted pockets in terms of sequence and structural conservation, backbone flexibility and electrostatic potential. Although these different measures do not tend to correlate, their combination is useful in selecting functional and regulatory sites, as a detailed analysis of a handful of protein families shows. We finally estimated the numbers of potential allosteric or regulatory pockets that may be present in the data set, finding that pockets with putative functional and effector characteristics are widespread across

Ana3 is a conserved protein required for the structural integrity of centrioles and basal bodies.

Science.gov (United States)

Stevens, Naomi R; Dobbelaere, Jeroen; Wainman, Alan; Gergely, Fanni; Raff, Jordan W

2009-11-02

Recent studies have identified a conserved "core" of proteins that are required for centriole duplication. A small number of additional proteins have recently been identified as potential duplication factors, but it is unclear whether any of these proteins are components of the core duplication machinery. In this study, we investigate the function of one of these proteins, Drosophila melanogaster Ana3. We show that Ana3 is present in centrioles and basal bodies, but its behavior is distinct from that of the core duplication proteins. Most importantly, we find that Ana3 is required for the structural integrity of both centrioles and basal bodies and for centriole cohesion, but it is not essential for centriole duplication. We show that Ana3 has a mammalian homologue, Rotatin, that also localizes to centrioles and basal bodies and appears to be essential for cilia function. Thus, Ana3 defines a conserved family of centriolar proteins and plays an important part in ensuring the structural integrity of centrioles and basal bodies.

NCBI nr-aa BLAST: CBRC-TSYR-01-0757 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-TSYR-01-0757 ref|YP_069190.1| hypothetical protein YPTB0648 [Yersinia pseudotuberculosis... IP 32953] ref|YP_001722278.1| type VI secretion system Vgr family protein [Yersinia pseudotuberculosis... YPIII] ref|YP_001871112.1| type VI secretion system Vgr family protein [Yersinia pseudotuberculosis PB...1/+] emb|CAH19888.1| conserved hypothetical protein [Yersinia pseudotuberculosis ...IP 32953] gb|ACA69825.1| type VI secretion system Vgr family protein [Yersinia pseudotuberculosis YPIII] gb|

BOLD responses in reward regions to hypothetical and imaginary monetary rewards.

Science.gov (United States)

Miyapuram, Krishna P; Tobler, Philippe N; Gregorios-Pippas, Lucy; Schultz, Wolfram

2012-01-16

Monetary rewards are uniquely human. Because money is easy to quantify and present visually, it is the reward of choice for most fMRI studies, even though it cannot be handed over to participants inside the scanner. A typical fMRI study requires hundreds of trials and thus small amounts of monetary rewards per trial (e.g. 5p) if all trials are to be treated equally. However, small payoffs can have detrimental effects on performance due to their limited buying power. Hypothetical monetary rewards can overcome the limitations of smaller monetary rewards but it is less well known whether predictors of hypothetical rewards activate reward regions. In two experiments, visual stimuli were associated with hypothetical monetary rewards. In Experiment 1, we used stimuli predicting either visually presented or imagined hypothetical monetary rewards, together with non-rewarding control pictures. Activations to reward predictive stimuli occurred in reward regions, namely the medial orbitofrontal cortex and midbrain. In Experiment 2, we parametrically varied the amount of visually presented hypothetical monetary reward keeping constant the amount of actually received reward. Graded activation in midbrain was observed to stimuli predicting increasing hypothetical rewards. The results demonstrate the efficacy of using hypothetical monetary rewards in fMRI studies. Copyright © 2011 Elsevier Inc. All rights reserved.

Subdominant Outer Membrane Antigens in Anaplasma marginale: Conservation, Antigenicity, and Protective Capacity Using Recombinant Protein.

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Deirdre R Ducken

Full Text Available Anaplasma marginale is a tick-borne rickettsial pathogen of cattle with a worldwide distribution. Currently a safe and efficacious vaccine is unavailable. Outer membrane protein (OMP extracts or a defined surface protein complex reproducibly induce protective immunity. However, there are several knowledge gaps limiting progress in vaccine development. First, are these OMPs conserved among the diversity of A. marginale strains circulating in endemic regions? Second, are the most highly conserved outer membrane proteins in the immunogens recognized by immunized and protected animals? Lastly, can this subset of OMPs recognized by antibody from protected vaccinates and conserved among strains recapitulate the protection of outer membrane vaccines? To address the first goal, genes encoding OMPs AM202, AM368, AM854, AM936, AM1041, and AM1096, major subdominant components of the outer membrane, were cloned and sequenced from geographically diverse strains and isolates. AM202, AM936, AM854, and AM1096 share 99.9 to 100% amino acid identity. AM1041 has 97.1 to 100% and AM368 has 98.3 to 99.9% amino acid identity. While all four of the most highly conserved OMPs were recognized by IgG from animals immunized with outer membranes, linked surface protein complexes, or unlinked surface protein complexes and shown to be protected from challenge, the highest titers and consistent recognition among vaccinates were to AM854 and AM936. Consequently, animals were immunized with recombinant AM854 and AM936 and challenged. Recombinant vaccinates and purified outer membrane vaccinates had similar IgG and IgG2 responses to both proteins. However, the recombinant vaccinates developed higher bacteremia after challenge as compared to adjuvant-only controls and outer membrane vaccinates. These results provide the first evidence that vaccination with specific antigens may exacerbate disease. Progressing from the protective capacity of outer membrane formulations to

Prioritizing orphan proteins for further study using phylogenomics and gene expression profiles in Streptomyces coelicolor

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Takano Eriko

2011-09-01

Full Text Available Abstract Background Streptomyces coelicolor, a model organism of antibiotic producing bacteria, has one of the largest genomes of the bacterial kingdom, including 7825 predicted protein coding genes. A large number of these genes, nearly 34%, are functionally orphan (hypothetical proteins with unknown function. However, in gene expression time course data, many of these functionally orphan genes show interesting expression patterns. Results In this paper, we analyzed all functionally orphan genes of Streptomyces coelicolor and identified a list of "high priority" orphans by combining gene expression analysis and additional phylogenetic information (i.e. the level of evolutionary conservation of each protein. Conclusions The prioritized orphan genes are promising candidates to be examined experimentally in the lab for further characterization of their function.

A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution

DEFF Research Database (Denmark)

Wong, W T; Schumacher, C; Salcini, A E

1995-01-01

In this report we structurally and functionally define a binding domain that is involved in protein association and that we have designated EH (for Eps15 homology domain). This domain was identified in the tyrosine kinase substrate Eps15 on the basis of regional conservation with several heteroge......In this report we structurally and functionally define a binding domain that is involved in protein association and that we have designated EH (for Eps15 homology domain). This domain was identified in the tyrosine kinase substrate Eps15 on the basis of regional conservation with several...... heterogeneous proteins of yeast and nematode. The EH domain spans about 70 amino acids and shows approximately 60% overall amino acid conservation. We demonstrated the ability of the EH domain to specifically bind cytosolic proteins in normal and malignant cells of mesenchymal, epithelial, and hematopoietic...... (for Eps15-related). Structural comparison of Eps15 and Eps15r defines a family of signal transducers possessing extensive networking abilities including EH-mediated binding and association with Src homology 3-containing proteins....

A conserved regulatory mechanism in bifunctional biotin protein ligases.

Science.gov (United States)

Wang, Jingheng; Beckett, Dorothy

2017-08-01

Class II bifunctional biotin protein ligases (BirA), which catalyze post-translational biotinylation and repress transcription initiation, are broadly distributed in eubacteria and archaea. However, it is unclear if these proteins all share the same molecular mechanism of transcription regulation. In Escherichia coli the corepressor biotinoyl-5'-AMP (bio-5'-AMP), which is also the intermediate in biotin transfer, promotes operator binding and resulting transcription repression by enhancing BirA dimerization. Like E. coli BirA (EcBirA), Staphylococcus aureus, and Bacillus subtilis BirA (Sa and BsBirA) repress transcription in vivo in a biotin-dependent manner. In this work, sedimentation equilibrium measurements were performed to investigate the molecular basis of this biotin-responsive transcription regulation. The results reveal that, as observed for EcBirA, Sa, and BsBirA dimerization reactions are significantly enhanced by bio-5'-AMP binding. Thus, the molecular mechanism of the Biotin Regulatory System is conserved in the biotin repressors from these three organisms. © 2017 The Protein Society.

Bound water at protein-protein interfaces: partners, roles and hydrophobic bubbles as a conserved motif.

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Mostafa H Ahmed

Full Text Available There is a great interest in understanding and exploiting protein-protein associations as new routes for treating human disease. However, these associations are difficult to structurally characterize or model although the number of X-ray structures for protein-protein complexes is expanding. One feature of these complexes that has received little attention is the role of water molecules in the interfacial region.A data set of 4741 water molecules abstracted from 179 high-resolution (≤ 2.30 Å X-ray crystal structures of protein-protein complexes was analyzed with a suite of modeling tools based on the HINT forcefield and hydrogen-bonding geometry. A metric termed Relevance was used to classify the general roles of the water molecules.The water molecules were found to be involved in: a (bridging interactions with both proteins (21%, b favorable interactions with only one protein (53%, and c no interactions with either protein (26%. This trend is shown to be independent of the crystallographic resolution. Interactions with residue backbones are consistent for all classes and account for 21.5% of all interactions. Interactions with polar residues are significantly more common for the first group and interactions with non-polar residues dominate the last group. Waters interacting with both proteins stabilize on average the proteins' interaction (-0.46 kcal mol(-1, but the overall average contribution of a single water to the protein-protein interaction energy is unfavorable (+0.03 kcal mol(-1. Analysis of the waters without favorable interactions with either protein suggests that this is a conserved phenomenon: 42% of these waters have SASA ≤ 10 Å(2 and are thus largely buried, and 69% of these are within predominantly hydrophobic environments or "hydrophobic bubbles". Such water molecules may have an important biological purpose in mediating protein-protein interactions.

[Family of ribosomal proteins S1 contains unique conservative domain].

Science.gov (United States)

Deriusheva, E I; Machulin, A V; Selivanova, O M; Serdiuk, I N

2010-01-01

Different representatives of bacteria have different number of amino acid residues in the ribosomal proteins S1. This number varies from 111 (Spiroplasma kunkelii) to 863 a.a. (Treponema pallidum). Traditionally and for lack of this protein three-dimensional structure, its architecture is represented as repeating S1 domains. Number of these domains depends on the protein's length. Domain's quantity and its boundaries data are contained in the specialized databases, such as SMART, Pfam and PROSITE. However, for the same object these data may be very different. For search of domain's quantity and its boundaries, new approach, based on the analysis of dicted secondary structure (PsiPred), was used. This approach allowed us to reveal structural domains in amino acid sequences of S1 proteins and at that number varied from one to six. Alignment of S1 proteins, containing different domain's number, with the S1 RNAbinding domain of Escherichia coli PNPase elicited a fact that in family of ribosomal proteins SI one domain has maximal homology with S1 domain from PNPase. This conservative domain migrates along polypeptide chain and locates in proteins, containing different domain's number, according to specified pattern. In this domain as well in the S1 domain from PNPase, residues Phe-19, Phe-22, His-34, Asp-64 and Arg-68 are clustered on the surface and formed RNA binding site.

Performance assessment for a hypothetical low-level waste disposal facility

International Nuclear Information System (INIS)

Smith, C.S.; Rohe, M.J.; Ritter, P.D.

1997-01-01

Disposing of low-level waste (LLW) is a concern for many states throughout the United States. A common disposal method is below-grade concrete vaults. Performance assessment analyses make predictions of contaminant release, transport, ingestion, inhalation, or other routes of exposure, and the resulting doses for various disposal methods such as the below-grade concrete vaults. Numerous assumptions are required to simplify the processes associated with the disposal facility to make predictions feasible. In general, these assumptions are made conservatively so as to underestimate the performance of the facility. The objective of this report is to describe the methodology used in conducting a performance assessment for a hypothetical waste facility located in the northeastern United States using real data as much as possible. This report consists of the following: (a) a description of the disposal facility and site, (b) methods used to analyze performance of the facility, (c) the results of the analysis, and (d) the conclusions of this study

Performance assessment for a hypothetical low-level waste disposal facility

Energy Technology Data Exchange (ETDEWEB)

Smith, C.S.; Rohe, M.J.; Ritter, P.D. [and others

1997-01-01

Disposing of low-level waste (LLW) is a concern for many states throughout the United States. A common disposal method is below-grade concrete vaults. Performance assessment analyses make predictions of contaminant release, transport, ingestion, inhalation, or other routes of exposure, and the resulting doses for various disposal methods such as the below-grade concrete vaults. Numerous assumptions are required to simplify the processes associated with the disposal facility to make predictions feasible. In general, these assumptions are made conservatively so as to underestimate the performance of the facility. The objective of this report is to describe the methodology used in conducting a performance assessment for a hypothetical waste facility located in the northeastern United States using real data as much as possible. This report consists of the following: (a) a description of the disposal facility and site, (b) methods used to analyze performance of the facility, (c) the results of the analysis, and (d) the conclusions of this study.

Conserved chemosensory proteins in the proboscis and eyes of Lepidoptera.

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Zhu, Jiao; Iovinella, Immacolata; Dani, Francesca Romana; Liu, Yu-Ling; Huang, Ling-Qiao; Liu, Yang; Wang, Chen-Zhu; Pelosi, Paolo; Wang, Guirong

2016-01-01

Odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) are endowed with several different functions besides being carriers for pheromones and odorants. Based on a previous report of a CSP acting as surfactant in the proboscis of the moth Helicoverpa armigera , we revealed the presence of orthologue proteins in two other moths Plutella xylostella and Chilo suppressalis , as well as two butterflies Papilio machaon and Pieris rapae , using immunodetection and proteomic analysis. The unusual conservation of these proteins across large phylogenetic distances indicated a common specific function for these CSPs. This fact prompted us to search for other functions of these proteins and discovered that CSPs are abundantly expressed in the eyes of H. armigera and possibly involved as carriers for carotenoids and visual pigments. This hypothesis is supported by ligand-binding experiments and docking simulations with retinol and β-carotene. This last orange pigment, occurring in many fruits and vegetables, is an antioxidant and the precursor of visual pigments. We propose that structurally related CSPs solubilise nutritionally important carotenoids in the proboscis, while they act as carriers of both β-carotene and its derived products 3-hydroxyretinol and 3-hydroxyretinal in the eye. The use of soluble olfactory proteins, such as CSPs, as carriers for visual pigments in insects, here reported for the first time, parallels the function of retinol-binding protein in vertebrates, a lipocalin structurally related to vertebrate odorant-binding proteins.

Structure-based functional annotation of putative conserved proteins having lyase activity from Haemophilus influenzae.

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Shahbaaz, Mohd; Ahmad, Faizan; Imtaiyaz Hassan, Md

2015-06-01

Haemophilus influenzae is a small pleomorphic Gram-negative bacteria which causes several chronic diseases, including bacteremia, meningitis, cellulitis, epiglottitis, septic arthritis, pneumonia, and empyema. Here we extensively analyzed the sequenced genome of H. influenzae strain Rd KW20 using protein family databases, protein structure prediction, pathways and genome context methods to assign a precise function to proteins whose functions are unknown. These proteins are termed as hypothetical proteins (HPs), for which no experimental information is available. Function prediction of these proteins would surely be supportive to precisely understand the biochemical pathways and mechanism of pathogenesis of Haemophilus influenzae. During the extensive analysis of H. influenzae genome, we found the presence of eight HPs showing lyase activity. Subsequently, we modeled and analyzed three-dimensional structure of all these HPs to determine their functions more precisely. We found these HPs possess cystathionine-β-synthase, cyclase, carboxymuconolactone decarboxylase, pseudouridine synthase A and C, D-tagatose-1,6-bisphosphate aldolase and aminodeoxychorismate lyase-like features, indicating their corresponding functions in the H. influenzae. Lyases are actively involved in the regulation of biosynthesis of various hormones, metabolic pathways, signal transduction, and DNA repair. Lyases are also considered as a key player for various biological processes. These enzymes are critically essential for the survival and pathogenesis of H. influenzae and, therefore, these enzymes may be considered as a potential target for structure-based rational drug design. Our structure-function relationship analysis will be useful to search and design potential lead molecules based on the structure of these lyases, for drug design and discovery.

33 CFR Appendix B to Part 277 - Hypothetical Example of Cost Apportionment

Science.gov (United States)

2010-07-01

... 33 Navigation and Navigable Waters 3 2010-07-01 2010-07-01 false Hypothetical Example of Cost... APPORTIONMENT OF BRIDGE ALTERATIONS Pt. 277, App. B Appendix B to Part 277—Hypothetical Example of Cost... bridge was completed in 1908 and the superstructure completed in 1909. For this hypothetical example it...

Seed storage protein gene promoters contain conserved DNA motifs in Brassicaceae, Fabaceae and Poaceae

Science.gov (United States)

Fauteux, François; Strömvik, Martina V

2009-01-01

Background Accurate computational identification of cis-regulatory motifs is difficult, particularly in eukaryotic promoters, which typically contain multiple short and degenerate DNA sequences bound by several interacting factors. Enrichment in combinations of rare motifs in the promoter sequence of functionally or evolutionarily related genes among several species is an indicator of conserved transcriptional regulatory mechanisms. This provides a basis for the computational identification of cis-regulatory motifs. Results We have used a discriminative seeding DNA motif discovery algorithm for an in-depth analysis of 54 seed storage protein (SSP) gene promoters from three plant families, namely Brassicaceae (mustards), Fabaceae (legumes) and Poaceae (grasses) using backgrounds based on complete sets of promoters from a representative species in each family, namely Arabidopsis (Arabidopsis thaliana (L.) Heynh.), soybean (Glycine max (L.) Merr.) and rice (Oryza sativa L.) respectively. We have identified three conserved motifs (two RY-like and one ACGT-like) in Brassicaceae and Fabaceae SSP gene promoters that are similar to experimentally characterized seed-specific cis-regulatory elements. Fabaceae SSP gene promoter sequences are also enriched in a novel, seed-specific E2Fb-like motif. Conserved motifs identified in Poaceae SSP gene promoters include a GCN4-like motif, two prolamin-box-like motifs and an Skn-1-like motif. Evidence of the presence of a variant of the TATA-box is found in the SSP gene promoters from the three plant families. Motifs discovered in SSP gene promoters were used to score whole-genome sets of promoters from Arabidopsis, soybean and rice. The highest-scoring promoters are associated with genes coding for different subunits or precursors of seed storage proteins. Conclusion Seed storage protein gene promoter motifs are conserved in diverse species, and different plant families are characterized by a distinct combination of conserved motifs

Seed storage protein gene promoters contain conserved DNA motifs in Brassicaceae, Fabaceae and Poaceae

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Fauteux François

2009-10-01

Full Text Available Abstract Background Accurate computational identification of cis-regulatory motifs is difficult, particularly in eukaryotic promoters, which typically contain multiple short and degenerate DNA sequences bound by several interacting factors. Enrichment in combinations of rare motifs in the promoter sequence of functionally or evolutionarily related genes among several species is an indicator of conserved transcriptional regulatory mechanisms. This provides a basis for the computational identification of cis-regulatory motifs. Results We have used a discriminative seeding DNA motif discovery algorithm for an in-depth analysis of 54 seed storage protein (SSP gene promoters from three plant families, namely Brassicaceae (mustards, Fabaceae (legumes and Poaceae (grasses using backgrounds based on complete sets of promoters from a representative species in each family, namely Arabidopsis (Arabidopsis thaliana (L. Heynh., soybean (Glycine max (L. Merr. and rice (Oryza sativa L. respectively. We have identified three conserved motifs (two RY-like and one ACGT-like in Brassicaceae and Fabaceae SSP gene promoters that are similar to experimentally characterized seed-specific cis-regulatory elements. Fabaceae SSP gene promoter sequences are also enriched in a novel, seed-specific E2Fb-like motif. Conserved motifs identified in Poaceae SSP gene promoters include a GCN4-like motif, two prolamin-box-like motifs and an Skn-1-like motif. Evidence of the presence of a variant of the TATA-box is found in the SSP gene promoters from the three plant families. Motifs discovered in SSP gene promoters were used to score whole-genome sets of promoters from Arabidopsis, soybean and rice. The highest-scoring promoters are associated with genes coding for different subunits or precursors of seed storage proteins. Conclusion Seed storage protein gene promoter motifs are conserved in diverse species, and different plant families are characterized by a distinct combination

ORF Sequence: cds [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available KGSWTFYIMLLASFRIFFGLGLSLSPMESWTIMNVVHAGVTFIVFHWIKGNPFHTPWVDMMGKGEKQTWWEQIDGSVQNTPSRKFLICVVVFLYLAAVHSTPFERQFFFVHAVNLIAFLVVFVAKLPFMHGVRIFGINR ... cds gnl|CMER >gnl|CMER|CMQ020C hypothetical protein, conserved MQSGHGETRFDVGVEWLRA

A predicted protein interactome identifies conserved global networks and disease resistance subnetworks in maize.

Directory of Open Access Journals (Sweden)

Matt eGeisler

2015-06-01

Full Text Available Interactomes are genome-wide roadmaps of protein-protein interactions. They have been produced for humans, yeast, the fruit fly, and Arabidopsis thaliana and have become invaluable tools for generating and testing hypotheses. A predicted interactome for Zea mays (PiZeaM is presented here as an aid to the research community for this valuable crop species. PiZeaM was built using a proven method of interologs (interacting orthologs that were identified using both one-to-one and many-to-many orthology between genomes of maize and reference species. Where both maize orthologs occurred for an experimentally determined interaction in the reference species, we predicted a likely interaction in maize. A total of 49,026 unique interactions for 6,004 maize proteins were predicted. These interactions are enriched for processes that are evolutionarily conserved, but include many otherwise poorly annotated proteins in maize. The predicted maize interactions were further analyzed by comparing annotation of interacting proteins, including different layers of ontology. A map of pairwise gene co-expression was also generated and compared to predicted interactions. Two global subnetworks were constructed for highly conserved interactions. These subnetworks showed clear clustering of proteins by function. Another subnetwork was created for disease response using a bait and prey strategy to capture interacting partners for proteins that respond to other organisms. Closer examination of this subnetwork revealed the connectivity between biotic and abiotic hormone stress pathways. We believe PiZeaM will provide a useful tool for the prediction of protein function and analysis of pathways for Z. mays researchers and is presented in this paper as a reference tool for the exploration of protein interactions in maize.

47 CFR 69.608 - Carrier Common Line hypothetical net balance.

Science.gov (United States)

2010-10-01

... 47 Telecommunication 3 2010-10-01 2010-10-01 false Carrier Common Line hypothetical net balance. 69.608 Section 69.608 Telecommunication FEDERAL COMMUNICATIONS COMMISSION (CONTINUED) COMMON CARRIER... net balance. The hypothetical net balance shall be equal to a Carrier Common Line revenue requirement...

Protein (Cyanobacteria): 493685768 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available hypothetical protein Microcoleus vaginatus MSEIPAEQTQTNLTTPEITTESSISGVENVKNSLGNVLNSWKLKVGVAVVVLFAVSLFAFYWQHIIAVVGMKSWSARSGANPIECMVRDTNNDQYVSCSALLDQQIVPLECSSSLFNIGCRVNYGTAAANPRQTNPR

ORF Sequence: Ca19AnnotatedDec2004aaSeq [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available Ca19AnnotatedDec2004aaSeq orf19.1278 >orf19.1278; Contig19-10104; complement(13162...4..>132028); ; conserved hypothetical protein; truncated protein IQNNKCSGCNLKLDFPVIHFKCKHSFHQKCLSTNLIATSTESS

CARNSORE: Hypothetical reactor accident study

International Nuclear Information System (INIS)

Walmod-Larsen, O.; Jensen, N.O.; Kristensen, L.; Meide, A.; Nedergaard, K.L.; Nielsen, F.; Lundtang Petersen, E.; Petersen, T.; Thykier-Nielsen, S.

1984-06-01

Two types of design-basis accident and a series of hypothetical core-melt accidents to a 600 MWe reactor are described and their consequences assessed. The PLUCON 2 model was used to calculate the consequences which are presented in terms of individual and collective doses, as well as early and late health consequences. The site proposed for the nucelar power station is Carnsore Point, County Wexford, south-east Ireland. The release fractions for the accidents described are those given in WASH-1400. The analyses are based on the resident population as given in the 1979 census and on 20 years of data from the meteorological stations at Rosslare Harbour, 8.5 km north of the site. The consequences of one of the hypothetical core-melt accidents are described in detail in a meteorological parametric study. Likewise the consequences of the worst conceivable combination of situations are described. Finally, the release fraction in one accident is varied and the consequences of a proposed, more probable ''Class 9 accident'' are presented. (author)

Protein (Cyanobacteria): 515516403 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available hypothetical protein Anabaena sp. PCC 7108 MTVRFLLDSNIISEPSRPIPNIQVLDQLNRYRSEVAIASVVVHEILYGCWRLPPSKRKDSLWKYIQDSVLNLPVFDYNLNAAKWHAQERARLSKIGKTPAFIDGQIASIAFCNDLILVTNNVADFQDFQDLVIENWFI

Protein (Cyanobacteria): 518320325 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available ... hypothetical protein Calothrix sp. PCC 7103 MDYVHPFQMELHKLESMIVHVQYADIKEVDKTLASNDAVSTQAVGEEGGTKVSTRALGEEGGNILTTYAVGEEGGNILTTYAVGEEGGDKVTTQAVGEEGGTRVTTYAVGEEGGGRVTTKAVGEEGGSIIRR

Evolutionarily conserved regions of the human c-myc protein can be uncoupled from transforming activity

International Nuclear Information System (INIS)

Sarid, J.; Halazonetis, T.D.; Murphy, W.; Leder, P.

1987-01-01

The myc family of oncogenes contains coding sequences that have been preserved in different species for over 400 million years. This conservation (which implies functional selection) is broadly represented throughout the C-terminal portion of the human c-myc protein but is largely restricted to three cluster of amino acid sequences in the N-terminal region. The authors have examined the role that the latter three regions of the c-myc protein might play in the transforming function of the c-myc gene. Several mutations, deletions and frameshifts, were introduced into the c-myc gene, and these mutant genes were tested for their ability to collaborate with the EJ-ras oncogene to transform rat embryo fibroblasts. Complete elimination of the first two N-terminal conserved segments abolished transforming activity. In contrast, genes altered in a portion of the second or the entire third conserved segment retained their transforming activity. Thus, the latter two segments are not required for the transformation process, suggesting that they serve another function related only to the normal expression of the c-myc gene

Protein (Viridiplantae): 159468384 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 3436 hypothetical protein CHLREDRAFT_180911 Chlamydomonas reinhardtii MTTEEPLSCSKIRSWNITVYSFTLKGLPGCLEPSHSFWVKEREGEWGLKCLSETFSHELVENVPGREEVSNLLKKGGSSNKSQKGGWICCERNCFLCQHKKCQVLI ...

Protein (Cyanobacteria): 515895859 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 302 ... hypothetical protein Synechococcus sp. PCC 7336 MADRNESFTPQSCRHILSVEDCDGLRDHALGAPKYFIGRDIANDICLNSQFASRYHALLLRVPAEREGEYFYRLLDGDLEGKPSTNGLTVNGLKVSAHELHEGDEISFGPDAKATYRVECLSADAK

Measuring rural homeowners' willingness to pay for land conservation easements

Science.gov (United States)

Seong-Hoon Cho; David H. Newman; J. Michael Bowker

2005-01-01

Rapid growth of rural communities in the Blue Ridge Mountains of Macon County, North Carolina has been giving rise to concerns over declining environmental quality and increasing need for land-use policy. This paper examines willingness to pay (WTP) for hypothetical conservation easements as an alternative land-use policy for the county. Despite the fact that Macon...

Targeting of nucleotide-binding proteins by HAMLET--a conserved tumor cell death mechanism.

Science.gov (United States)

Ho, J C S; Nadeem, A; Rydström, A; Puthia, M; Svanborg, C

2016-02-18

HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) kills tumor cells broadly suggesting that conserved survival pathways are perturbed. We now identify nucleotide-binding proteins as HAMLET binding partners, accounting for about 35% of all HAMLET targets in a protein microarray comprising 8000 human proteins. Target kinases were present in all branches of the Kinome tree, including 26 tyrosine kinases, 10 tyrosine kinase-like kinases, 13 homologs of yeast sterile kinases, 4 casein kinase 1 kinases, 15 containing PKA, PKG, PKC family kinases, 15 calcium/calmodulin-dependent protein kinase kinases and 13 kinases from CDK, MAPK, GSK3, CLK families. HAMLET acted as a broad kinase inhibitor in vitro, as defined in a screen of 347 wild-type, 93 mutant, 19 atypical and 17 lipid kinases. Inhibition of phosphorylation was also detected in extracts from HAMLET-treated lung carcinoma cells. In addition, HAMLET recognized 24 Ras family proteins and bound to Ras, RasL11B and Rap1B on the cytoplasmic face of the plasma membrane. Direct cellular interactions between HAMLET and activated Ras family members including Braf were confirmed by co-immunoprecipitation. As a consequence, oncogenic Ras and Braf activity was inhibited and HAMLET and Braf inhibitors synergistically increased tumor cell death in response to HAMLET. Unlike most small molecule kinase inhibitors, HAMLET showed selectivity for tumor cells in vitro and in vivo. The results identify nucleotide-binding proteins as HAMLET targets and suggest that dysregulation of the ATPase/kinase/GTPase machinery contributes to cell death, following the initial, selective recognition of HAMLET by tumor cells. The findings thus provide a molecular basis for the conserved tumoricidal effect of HAMLET, through dysregulation of kinases and oncogenic GTPases, to which tumor cells are addicted.

Sequence, structure and function relationships in flaviviruses as assessed by evolutive aspects of its conserved non-structural protein domains.

Science.gov (United States)

da Fonseca, Néli José; Lima Afonso, Marcelo Querino; Pedersolli, Natan Gonçalves; de Oliveira, Lucas Carrijo; Andrade, Dhiego Souto; Bleicher, Lucas

2017-10-28

Flaviviruses are responsible for serious diseases such as dengue, yellow fever, and zika fever. Their genomes encode a polyprotein which, after cleavage, results in three structural and seven non-structural proteins. Homologous proteins can be studied by conservation and coevolution analysis as detected in multiple sequence alignments, usually reporting positions which are strictly necessary for the structure and/or function of all members in a protein family or which are involved in a specific sub-class feature requiring the coevolution of residue sets. This study provides a complete conservation and coevolution analysis on all flaviviruses non-structural proteins, with results mapped on all well-annotated available sequences. A literature review on the residues found in the analysis enabled us to compile available information on their roles and distribution among different flaviviruses. Also, we provide the mapping of conserved and coevolved residues for all sequences currently in SwissProt as a supplementary material, so that particularities in different viruses can be easily analyzed. Copyright © 2017 Elsevier Inc. All rights reserved.

NCBI nr-aa BLAST: CBRC-CREM-01-1364 [SEVENS

Lifescience Database Archive (English)

Full Text Available ted as GTP-binding elongation factor TypA/BipA [Bifidobacterium adolescentis ATCC 15703] ref|ZP_02029709.1| ...hypothetical protein BIFADO_02168 [Bifidobacterium adolescentis L2-32] dbj|BAF39850.1| widely conserved prot...ein similar to those annotated as GTP-binding elongation factor TypA/BipA [Bifidobacterium adolescent...is ATCC 15703] gb|EDN82042.1| hypothetical protein BIFADO_02168 [Bifidobacterium adolescentis L2-32] YP_909932.1 5e-75 60% ...

Protein (Cyanobacteria): 498001483 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 2363:858 ... hypothetical protein Synechococcus sp. CB0205 MQPRLSQQEQRALIRAKRAVRCLPFRRRFYEELEREALSSTQLAARSDWTALSCRRLSANHCEYLLIWLIQLGVLRREVDGQGLTERVRLTPLGRVVLSDWPGEIPSASLPSRLRHWIKQHWPRL

Protein (Cyanobacteria): 516255172 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 7:613 ... hypothetical protein Geitlerinema sp. PCC 7105 MKNKATAALFAFFLGFLGIHKFYLGQNFSGVLYLILSWTGIPAILAIFDFLGLLLMSDATFNVRYNNMVTVVRDNLVVTPSPDRSRSATEITRALADLKKLYEVGAVTAEEYEEKRQKLLSEL

Purification and characterization of a thermostable hypothetical xylanase from Aspergillus oryzae HML366.

Science.gov (United States)

He, Haiyan; Qin, Yongling; Li, Nan; Chen, Guiguang; Liang, Zhiqun

2015-03-01

In the current study, fermentation broth of Aspergillus oryzae HML366 in sugar cane bagasse was subjected to ultrafiltration and ion exchange chromatography, and two xylanases, XynH1 and XynH2, were purified. Time-of-flight mass spectrometry coupled with SDS-PAGE analysis revealed that XynH1 is identical to the hypothetical A. oryzae RIB40 protein XP_001826985.1, with a molecular weight of 33.671 kDa. Likewise, XynH2 was identified as xylanase XynF1 with a molecular weight of 35.402 kDa. Sequence analysis indicated that XynH1 belongs to glycosyl hydrolases family 10. The specific activity of XynH1 was measured at 476.9 U/mg. Optimal xylanase activity was observed at pH 6.0, and enzyme remained active within pH 4.0-10.0 and at a temperature below 70 °C. Mg(2+), Mn(2+), Ca(2+), and K(+) enhanced the XynH1 xylanase activity to 146, 122, 114, and 108%, respectively. XynH1 hydrolyzed Birchwood xylan and Larchwood xylan effectively. The K m and V max of XynH1 values determined were 1.16 mM and 336 μmol/min/mg with Birchwood xylan as the substrate. A. oryzae HML366 xylanase XynH1 showed superior heat and pH tolerance, therefore may have significant applications in paper and biofuel industries. These studies constitute the first investigation of the xylanase activities of the hypothetical protein XP_001826985.1 form A. oryzae.

Combining modularity, conservation, and interactions of proteins significantly increases precision and coverage of protein function prediction

Directory of Open Access Journals (Sweden)

Sers Christine T

2010-12-01

Full Text Available Abstract Background While the number of newly sequenced genomes and genes is constantly increasing, elucidation of their function still is a laborious and time-consuming task. This has led to the development of a wide range of methods for predicting protein functions in silico. We report on a new method that predicts function based on a combination of information about protein interactions, orthology, and the conservation of protein networks in different species. Results We show that aggregation of these independent sources of evidence leads to a drastic increase in number and quality of predictions when compared to baselines and other methods reported in the literature. For instance, our method generates more than 12,000 novel protein functions for human with an estimated precision of ~76%, among which are 7,500 new functional annotations for 1,973 human proteins that previously had zero or only one function annotated. We also verified our predictions on a set of genes that play an important role in colorectal cancer (MLH1, PMS2, EPHB4 and could confirm more than 73% of them based on evidence in the literature. Conclusions The combination of different methods into a single, comprehensive prediction method infers thousands of protein functions for every species included in the analysis at varying, yet always high levels of precision and very good coverage.

Conserved residues and their role in the structure, function, and stability of acyl-coenzyme A binding protein

DEFF Research Database (Denmark)

Kragelund, B B; Poulsen, K; Andersen, K V

1999-01-01

In the family of acyl-coenzyme A binding proteins, a subset of 26 sequence sites are identical in all eukaryotes and conserved throughout evolution of the eukaryotic kingdoms. In the context of the bovine protein, the importance of these 26 sequence positions for structure, function, stability...

Hydra meiosis reveals unexpected conservation of structural synaptonemal complex proteins across metazoans

OpenAIRE

Fraune, Johanna; Alsheimer, Manfred; Volff, Jean-Nicolas; Busch, Karoline; Fraune, Sebastian; Bosch, Thomas C. G.; Benavente, Ricardo

2012-01-01

The synaptonemal complex (SC) is a key structure of meiosis, mediating the stable pairing (synapsis) of homologous chromosomes during prophase I. Its remarkable tripartite structure is evolutionarily well conserved and can be found in almost all sexually reproducing organisms. However, comparison of the different SC protein components in the common meiosis model organisms Saccharomyces cerevisiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, and Mus musculus revealed...

Protein (Cyanobacteria): 516325726 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 8:1201 ... hypothetical protein Oscillatoria sp. PCC 10802 MGHIPSSSFPDNRRAFSLWLWWGGLIEHRHVVAKIWALEIPGMNPTPQPPPRVRGGGERD...GFGGGGLIEHRHVVAKISALEIPGMNPAPQPPPRVRGGGERDGFGGGGFIDIRHVVAKIAGEPAPTNHRHPVSGEAADATHYIYADFEG

Protein (Cyanobacteria): 218248342 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available ... hypothetical protein PCC8801_3595 Cyanothece sp. PCC 8801 MSIQYLLDENLPHLYREQLLRLKSDLTVWIIGDPGVPPKSTLDPEILIWCEQNKFILVTNNRASMPVHLADHLSQNRHIPGIFVLRPKASIGEIIDDLILIDELGNPQDYQDCISHIPFI

Protein (Viridiplantae): 159466610 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 2419 hypothetical protein CHLREDRAFT_123820, partial Chlamydomonas reinhardtii RVQCRLVDMPAPCLPPFLPTCPHKPRRIPMPCTDAH...ELVDMPAPCLPPFLPDNLPARAPQAPHAVTDAHECMQCRLVDMPAPCLPPFLPKCPHKPRRLPMPCTDAHECNMPAPCLPPFLPKCPHKPRRLPMPCTDAHECMQCRLVDMPAPCLPAFLPNCPHKPRRLPMPCTDAHECSAGW ...

Protein (Cyanobacteria): 516258751 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 27:2058 ... hypothetical protein Geitlerinema sp. PCC 7105 MAVWKFALGSIAGVLVGTSPSLALPGQTVEEVQTWIQTNPLLPRGLEGSL...RVSRSDIPGQRFTFTALKTLPTDSNLVVGGRYIRSERLEVLDYENGVTRDRLVSTLRSIYDLDIYRDYRDAEVVYDYVSPAGREMQDVYRGVLLKGDRFGYWIEITEREGIEPVIGHLAIVLAEDVETLETQLRNR

Protein (Cyanobacteria): 516257059 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 7:780 ... hypothetical protein Geitlerinema sp. PCC 7105 MSDKLEDFNGRNLDTKKSEGVERRKENRGKLLIDATVAPADIKYPTDVELLN...QARKTTELILDILYKSLKGQLYKKPRTHRKLARKEYLKFAKKRRPSRKERRNAVKKQLQYLQRNFRNIEKLIEKGASLECLSRRQYRNLLVSSEITRQQQWMWSNQ

Protein (Cyanobacteria): 516255830 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 7:918 ... hypothetical protein Geitlerinema sp. PCC 7105 MLYIYNHKLRRPSPLYIFKNFFESKAVENLLGEGIKAEYLNDDRLGRVLDKI...YRFGLNRIFVAIALATVKKYELTVNSNHLDSSSFHVHGDYPNSGESGTIEITYGYSRDHRPDLKQFLMNLICTGDGDVPLWMKMGSGNDSDSKQFGRSMVEFKKHFSLKV

Protein (Cyanobacteria): 648405821 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 27:2531 ... hypothetical protein Geitlerinema sp. PCC 7105 MLMNIIFLTSAITTAAIATYFITHRLGGFRTVATLLCLGLLAGTGSLPAL...ASTDIAALGAKSNTLEQGQQQLEEDLKLTPTGGQYSGIEYAKGAERGEPMTDRKIRETILSDTSEDLTVNVASGSVILSGTVRDKDRAREIVDEIKGISGVHEITFELGLEEGQSS

Protein (Cyanobacteria): 516258198 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 7:1853 ... hypothetical protein Geitlerinema sp. PCC 7105 MQKKYIVRLTAEERHQLQAVIKKLNGSSQKVRRAQILLKADADGPNWTDQQ...IAEAFDCRTKTVENIRRRLVEQGFEITLNGVKRTRPPTDKRLDGEQEAQVIAMRLGPPPAGYANWSLRLLARKVVELGLVEAVSHETVRQTLKKTG

Comprehensive and consistent interpretation of local fault experiments and application to hypothetical local overpower accident in Monju

International Nuclear Information System (INIS)

Fukano, Yoshitaka

2013-01-01

Experimental studies on local fault (LF) accidents in fast breeder reactors have been performed in many countries because LFs have been historically considered as one of the possible causes of severe accidents. Comprehensive and consistent interpretations of in-pile and out-of-pile experiments related to LF were arrived at in this study based on state-of-the-art review and data analysis techniques. Safety margins for a hypothetical local overpower accident, which was evaluated as a LF accident in the licensing document of the construction permit for a prototype fast breeder reactor called Monju, were also studied. Based on comprehensive interpretations of the latest experimental database, including those performed after the permission of Monju construction, it was clarified that the evaluation of the hypothetical local overpower accident in the Monju licensing was sufficiently conservative. Furthermore, it incorporated adequate safety margins in terms of failure thresholds of the fuel pin, molten fuel ejection, fuel sweep-out behavior after molten fuel ejection, and pin-to-pin failure propagation. Moreover, these comprehensive interpretations are valid and applicable to the safety evaluation of LF accidents of other fast breeder reactors with various fuel and core designs. (author)

DisoMCS: Accurately Predicting Protein Intrinsically Disordered Regions Using a Multi-Class Conservative Score Approach.

Directory of Open Access Journals (Sweden)

Zhiheng Wang

Full Text Available The precise prediction of protein intrinsically disordered regions, which play a crucial role in biological procedures, is a necessary prerequisite to further the understanding of the principles and mechanisms of protein function. Here, we propose a novel predictor, DisoMCS, which is a more accurate predictor of protein intrinsically disordered regions. The DisoMCS bases on an original multi-class conservative score (MCS obtained by sequence-order/disorder alignment. Initially, near-disorder regions are defined on fragments located at both the terminus of an ordered region connecting a disordered region. Then the multi-class conservative score is generated by sequence alignment against a known structure database and represented as order, near-disorder and disorder conservative scores. The MCS of each amino acid has three elements: order, near-disorder and disorder profiles. Finally, the MCS is exploited as features to identify disordered regions in sequences. DisoMCS utilizes a non-redundant data set as the training set, MCS and predicted secondary structure as features, and a conditional random field as the classification algorithm. In predicted near-disorder regions a residue is determined as an order or a disorder according to the optimized decision threshold. DisoMCS was evaluated by cross-validation, large-scale prediction, independent tests and CASP (Critical Assessment of Techniques for Protein Structure Prediction tests. All results confirmed that DisoMCS was very competitive in terms of accuracy of prediction when compared with well-established publicly available disordered region predictors. It also indicated our approach was more accurate when a query has higher homologous with the knowledge database.The DisoMCS is available at http://cal.tongji.edu.cn/disorder/.

Identification of an evolutionary conserved SURF-6 domain in a family of nucleolar proteins extending from human to yeast

International Nuclear Information System (INIS)

Polzikov, Mikhail; Zatsepina, Olga; Magoulas, Charalambos

2005-01-01

The mammalian SURF-6 protein is localized in the nucleolus, yet its function remains elusive in the recently characterized nucleolar proteome. We discovered by searching the Protein families database that a unique evolutionary conserved SURF-6 domain is present in the carboxy-terminal of a novel family of eukaryotic proteins extending from human to yeast. By using the enhanced green fluorescent protein as a fusion protein marker in mammalian cells, we show that proteins from distantly related taxonomic groups containing the SURF-6 domain are localized in the nucleolus. Deletion sequence analysis shows that multiple regions of the SURF-6 protein are capable of nucleolar targeting independently of the evolutionary conserved domain. We identified that the Saccharomyces cerevisiae member of the SURF-6 family, named rrp14 or ykl082c, has been categorized in yeast databases to interact with proteins involved in ribosomal biogenesis and cell polarity. These results classify SURF-6 as a new family of nucleolar proteins in the eukaryotic kingdom and point out that SURF-6 has a distinct domain within the known nucleolar proteome that may mediate complex protein-protein interactions for analogous processes between yeast and mammalian cells

Ribosome-dependent ATPase interacts with conserved membrane protein in Escherichia coli to modulate protein synthesis and oxidative phosphorylation.

Directory of Open Access Journals (Sweden)

Mohan Babu

Full Text Available Elongation factor RbbA is required for ATP-dependent deacyl-tRNA release presumably after each peptide bond formation; however, there is no information about the cellular role. Proteomic analysis in Escherichia coli revealed that RbbA reciprocally co-purified with a conserved inner membrane protein of unknown function, YhjD. Both proteins are also physically associated with the 30S ribosome and with members of the lipopolysaccharide transport machinery. Genome-wide genetic screens of rbbA and yhjD deletion mutants revealed aggravating genetic interactions with mutants deficient in the electron transport chain. Cells lacking both rbbA and yhjD exhibited reduced cell division, respiration and global protein synthesis as well as increased sensitivity to antibiotics targeting the ETC and the accuracy of protein synthesis. Our results suggest that RbbA appears to function together with YhjD as part of a regulatory network that impacts bacterial oxidative phosphorylation and translation efficiency.

Protein (Cyanobacteria): 479132100 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 05 696747:1505 ... hypothetical protein Arthrospira platensis NIES-39 MGGGNGTQQHHLSVMLGFTLVSPNLPRAIAYLSRLGGGNGTQQHHLSVMLGFTLVSPKLPRAIA...YLSRLGGGNGTQQHHLSVMLGFTLVSPNLPRAIAYLSRLGGGNGTQQHHLSVMLGFTLVSPNLQMLGETRATKSDRLFK

Protein (Cyanobacteria): 479132040 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 05 696747:1505 ... hypothetical protein Arthrospira platensis NIES-39 MGGGNGTQQHHLSVMLGFTLVSPNLPRAIAYLSRLGGGNGTQQHHLSVMLGFTLVSPKLPRAIA...YLSRLGGGNGTQQHHLSVMLGFTLVSPNLPRAIAYLSRLGGGNGTQQHHLSVMLGFTLVSPNLQMLGETRATKSDRLFK

Protein (Cyanobacteria): 479132036 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 05 696747:1505 ... hypothetical protein Arthrospira platensis NIES-39 MEVRNPTTPSLNDVGFHGVSPNLQRAIAYLSRLGGGNGTQHHHLSVMFGFTLVSPNLPRAIA...YLSRLGGGNGTQQHHLSVMLGFTLVSPKLPRAIAYLSRLGGGNGTQHHHLSVILGFTLVSPNLQMLGETQATKSDRLFK

Protein (Cyanobacteria): 434405526 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 107:2633 ... hypothetical protein Cylst_3595 Cylindrospermum stagnale PCC 7417 MNKNNIQNYRFVCTLTFGDIYGQIIVWLITITISLASALALMGARRPVYALVTVGLVVLLTLPFLLFAFVTTLINHIELTSIEPGTKMEPIPGNVSQQQPIQASS

Protein (Cyanobacteria): 427719678 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available ... hypothetical protein Cal7507_4468 Calothrix sp. PCC 7507 MYSQQLRTAIYGFFKRSHHLQLNCIDLQLNCIDLQLSCIDLQLSCIDLQLSCIDLQLNCIDLQLSCIDLQLSCI...DLQLSCIDLQLSCIDLQLSCIDLQLSCIDLQLSCIDLQLSCIDLQLSCIDLQSLNYPFLHFTDSFFVVMGTLKI

A Conserved Metal Binding Motif in the Bacillus subtilis Competence Protein ComFA Enhances Transformation.

Science.gov (United States)

Chilton, Scott S; Falbel, Tanya G; Hromada, Susan; Burton, Briana M

2017-08-01

Genetic competence is a process in which cells are able to take up DNA from their environment, resulting in horizontal gene transfer, a major mechanism for generating diversity in bacteria. Many bacteria carry homologs of the central DNA uptake machinery that has been well characterized in Bacillus subtilis It has been postulated that the B. subtilis competence helicase ComFA belongs to the DEAD box family of helicases/translocases. Here, we made a series of mutants to analyze conserved amino acid motifs in several regions of B. subtilis ComFA. First, we confirmed that ComFA activity requires amino acid residues conserved among the DEAD box helicases, and second, we show that a zinc finger-like motif consisting of four cysteines is required for efficient transformation. Each cysteine in the motif is important, and mutation of at least two of the cysteines dramatically reduces transformation efficiency. Further, combining multiple cysteine mutations with the helicase mutations shows an additive phenotype. Our results suggest that the helicase and metal binding functions are two distinct activities important for ComFA function during transformation. IMPORTANCE ComFA is a highly conserved protein that has a role in DNA uptake during natural competence, a mechanism for horizontal gene transfer observed in many bacteria. Investigation of the details of the DNA uptake mechanism is important for understanding the ways in which bacteria gain new traits from their environment, such as drug resistance. To dissect the role of ComFA in the DNA uptake machinery, we introduced point mutations into several motifs in the protein sequence. We demonstrate that several amino acid motifs conserved among ComFA proteins are important for efficient transformation. This report is the first to demonstrate the functional requirement of an amino-terminal cysteine motif in ComFA. Copyright © 2017 American Society for Microbiology.

Computational prediction of protein-protein interactions in Leishmania predicted proteomes.

Directory of Open Access Journals (Sweden)

Antonio M Rezende

Full Text Available The Trypanosomatids parasites Leishmania braziliensis, Leishmania major and Leishmania infantum are important human pathogens. Despite of years of study and genome availability, effective vaccine has not been developed yet, and the chemotherapy is highly toxic. Therefore, it is clear just interdisciplinary integrated studies will have success in trying to search new targets for developing of vaccines and drugs. An essential part of this rationale is related to protein-protein interaction network (PPI study which can provide a better understanding of complex protein interactions in biological system. Thus, we modeled PPIs for Trypanosomatids through computational methods using sequence comparison against public database of protein or domain interaction for interaction prediction (Interolog Mapping and developed a dedicated combined system score to address the predictions robustness. The confidence evaluation of network prediction approach was addressed using gold standard positive and negative datasets and the AUC value obtained was 0.94. As result, 39,420, 43,531 and 45,235 interactions were predicted for L. braziliensis, L. major and L. infantum respectively. For each predicted network the top 20 proteins were ranked by MCC topological index. In addition, information related with immunological potential, degree of protein sequence conservation among orthologs and degree of identity compared to proteins of potential parasite hosts was integrated. This information integration provides a better understanding and usefulness of the predicted networks that can be valuable to select new potential biological targets for drug and vaccine development. Network modularity which is a key when one is interested in destabilizing the PPIs for drug or vaccine purposes along with multiple alignments of the predicted PPIs were performed revealing patterns associated with protein turnover. In addition, around 50% of hypothetical protein present in the networks

Protein (Viridiplantae): 302831798 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 18 3068:3318 hypothetical protein VOLCADRAFT_120454 Volvox carteri f. nagariensis MLVTTRSHRQVSLDGGVLPPEEIKQLASLRRQQQADLAKDSNIVQGALEEAQLITWPTREKALLDTVLVLFIVAGSGAMIFGMNVLLAELSEWWYHLA ...

Protein (Cyanobacteria): 470019 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available hypothetical protein Pro1185 Prochlorococcus marinus subsp. marinus str. CCMP1375 MLNGLNLCTLLEKYCYSKKISDKEVEFLERCWLDSLNSLHYNRYPGIAPAIVCDEAGVARGSYWISCNAAILDKLKPLGTTRSRSARIFDVLFQSGLIAA ...

Protein (Cyanobacteria): 78779802 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 1196 ... hypothetical protein PMT9312_1418 Prochlorococcus marinus str. MIT 9312 MKFLTTLFLKLLLLSNFVIAETIPTKSNILKQSSECIKDSQNQICRELVSKLEKLQYVVFDQNRFKCQSSLLGLQSELIEAYFLKSLSKKRISFMIPYVIKNC

Protein (Cyanobacteria): 428297532 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 0562:1027 ... hypothetical protein Cal6303_0799 Calothrix sp. PCC 6303 MSNLSHGGFDDSKPTIDENSFWQYIRSLHPQTVKQLNKPSSTDVVETINLTVATILDHISDDSSDSQIVTSHDELGMLLGSVMIDGYFLRNAEQRMELDHIFQELGTGGEQE

Protein (Cyanobacteria): 428223918 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available :617 ... hypothetical protein GEI7407_0462 Geitlerinema sp. PCC 7407 MEKIESLPIIGWREWLALPELGISAIKTKVDTGARSSALH...AFDLRRFCQAGQEWVRFTIHPYQHDLQQTVVATARVIDERQVRTSSGHTELRPVIHTPILLGGCQWPIEITLTNRDVMGFRMLLGRQAIRQRFLVDPGHSFLLSSLRLPLRSPTSRSQPL

Protein (Cyanobacteria): 428224977 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available :1268 ... hypothetical protein GEI7407_1530 Geitlerinema sp. PCC 7407 MAQLQRLDIVGDDGQTIEIFVEEKDAPVLATSPNRDGRP...SMGAGSPSVKMQQMQQVIRGYATYALNAFKDFSAAEVEEITLMFGVKLSASAGIPYIANGTTDSNLEVQVKCRFPAKDG

Consequence analyses of hypothetical accidents of high temperature gas-cooled reactors. Pt. 2/3

International Nuclear Information System (INIS)

Mueller, A.; Badur, A.

1978-06-01

With regard to a hypothetical accident which is characterized by the rupture of the primary circuit and by the additional failure of active engineered safeguards, the fission product release resulting from the unlimited core heat-up is analyzed. The applied models are explained and the data base being used is documented. The generally conservative treatment yields pessimistic activity release rates into the containment. The results show in particular that spontaneous massive fission product release does not occur. The time-dependency of the activity release from the fuel elements, the primary circuit and at last from the containment leads to a time delay in the range of at least several hours, before the environmental radiation load is raised. Ultimately the maximum radiation load itself proves relatively favourable. (orig.) 891 HP [de

Important radionuclides and their sensitivity for groundwater pathway of a hypothetical near-surface disposal facility

Energy Technology Data Exchange (ETDEWEB)

Park, J. W.; Chang, K.; Kim, C. L. [Nuclear Enviroment Technology Institute, Taejon (Korea, Republic of)

2001-04-01

A radiological safety assessment was performed for a hypothetical near-surface radioactive waste repository as a simple screening calculation to identify important nuclides and to provide insights on the data needs for a successful demonstration of compliance. Individual effective doses were calculated for a conservative groundwater pathway scenario considering well drilling near the site boundary. Sensitivity of resulting ingestion dose to input parameter values was also analyzed using Monte Carlo sampling. Considering peak dose rate and assessment timescale, C-14 and I-129 were identified as important nuclides and U-235 and U-238 as potentially important nuclides. For C-14, the does was most sensitive to Darcy velocity in aquifer. The distribution coefficient showed high degree of sensitivity for I-129 release.

Important radionuclides and their sensitivity for groundwater pathway of a hypothetical near-surface disposal facility

International Nuclear Information System (INIS)

Park, J. W.; Chang, K.; Kim, C. L.

2001-01-01

A radiological safety assessment was performed for a hypothetical near-surface radioactive waste repository as a simple screening calculation to identify important nuclides and to provide insights on the data needs for a successful demonstration of compliance. Individual effective doses were calculated for a conservative groundwater pathway scenario considering well drilling near the site boundary. Sensitivity of resulting ingestion dose to input parameter values was also analyzed using Monte Carlo sampling. Considering peak dose rate and assessment timescale, C-14 and I-129 were identified as important nuclides and U-235 and U-238 as potentially important nuclides. For C-14, the does was most sensitive to Darcy velocity in aquifer. The distribution coefficient showed high degree of sensitivity for I-129 release

Importance of a Conserved Lys/Arg Residue for Ligand/PDZ Domain Interactions as Examined by Protein Semisynthesis

DEFF Research Database (Denmark)

Pedersen, Søren W; Moran, Griffin E; Sereikaité, Vita

2016-01-01

PDZ domains are ubiquitous small protein domains that are mediators of numerous protein-protein interactions, and play a pivotal role in protein trafficking, synaptic transmission, and the assembly of signaling-transduction complexes. In recent years, PDZ domains have emerged as novel and exciting...... drug targets for diseases (in the brain in particular), so understanding the molecular details of PDZ domain interactions is of fundamental importance. PDZ domains bind to a protein partner at either a C-terminal peptide or internal peptide motifs. Here, we examined the importance of a conserved Lys...

Reactions to Hypothetical, Jealousy Producing Events.

Science.gov (United States)

Hansen, Gary L.

1982-01-01

Asked subjects (N=220) how they would feel about their mates' behavior in eight hypothetical situations designed to measure jealousy. Responses indicated that jealousy is likely to be a major issue. Sex role orientation is most consistently related to jealousy with sex role traditional subjects being the most jealous. (Author)

Adolescents' explicit and implicit evaluations of hypothetical and actual peers with different bullying participant roles.

Science.gov (United States)

Pouwels, J Loes; Lansu, Tessa A M; Cillessen, Antonius H N

2017-07-01

This study examined how adolescents evaluate bullying at three levels of specificity: (a) the general concept of bullying, (b) hypothetical peers in different bullying participant roles, and (c) actual peers in different bullying participant roles. Participants were 163 predominantly ethnic majority adolescents in The Netherlands (58% girls; M age =16.34years, SD=0.79). For the hypothetical peers, we examined adolescents' explicit evaluations as well as their implicit evaluations. Adolescents evaluated the general concept of bullying negatively. Adolescents' explicit evaluations of hypothetical and actual peers in the bullying roles depended on their own role, but adolescents' implicit evaluations of hypothetical peers did not. Adolescents' explicit evaluations of hypothetical peers and actual peers were different. Hypothetical bullies were evaluated negatively by all classmates, whereas hypothetical victims were evaluated relatively positively compared with the other roles. However, when adolescents evaluated their actual classmates, the differences between bullies and the other roles were smaller, whereas victims were evaluated the most negatively of all roles. Further research should take into account that adolescents' evaluations of hypothetical peers differ from their evaluations of actual peers. Copyright © 2017 Elsevier Inc. All rights reserved.

Protein (Cyanobacteria): 647660116 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available :162 ... hypothetical protein, partial Prochlorococcus sp. scB243_496A2 MRILLAAAECAPMIKVGGMGDVVGSLPPSLIKLGHDVRVIIPGYGKLWSLLEVSNEPVFRTNTMGTDFAVYEAKHPIHNYVIYLVGHPTFDSDQIYGGENEDWRFTFFASAT

Protein (Cyanobacteria): 647680444 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available :36 ... hypothetical protein, partial Prochlorococcus sp. scB241_526B22 VYSSHLNNQRELIVTSESTRESINLAKYLTDNGVVKYSAYWCPNCLNQSELFGKQAYRELNVVECARDGINSQTQLCIDKKIKGFPTGEINGALILGVLSLKELSKLTGFKN

Protein (Cyanobacteria): 186682931 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 63737:1993 ... hypothetical protein Npun_R2630 Nostoc punctiforme PCC 73102 MDTLDLQSVSTEDVMLRYGIKSRTTLNKFLENAGVNSFKEGRKTFIRMYQLGVLDRSAH...ELNYPINQSSNQSIQSIHPTDSIKSEQMELAESTGLFPLTTVDLLYITCEYENLPRLAKWLAGYAFLEKMSSGRVILPRDVVLKILDYKRLPTCKDGYFRYGNFVFLMIGDHKKEWLVSKK

Protein (Cyanobacteria): 428225641 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 5:1771 ... hypothetical protein GEI7407_2207 Geitlerinema sp. PCC 7407 MKSLSLCVLLSAGVLSLGALPSQAMAPAELVETPPNHS...VAIHRSEGNCPAQVDLWVQSRYYEGGGEFSALVDTAAIAGRAVFLEAKQDFVEFAAPLKPQYASCYGYVVSSDEPQYNLWFYKGYVYFRFDLQSLPGRPLSEITSQAIIEDRPFMRWAIAD

ORF Alignment: NC_002516 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_002695 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_004337 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_002655 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_002947 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_006513 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_004578 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_005966 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_000913 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_006085 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_003197 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_006905 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_004431 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_004741 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

ORF Alignment: NC_006511 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available etical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1] emb|CAI07855.1| conse...rved ... hypothetical protein, probably involved in cell wall ... turnover [Azoarcus sp. EbN1

Sequence analysis of the L protein of the Ebola 2014 outbreak: Insight into conserved regions and mutations.

Science.gov (United States)

Ayub, Gohar; Waheed, Yasir

2016-06-01

The 2014 Ebola outbreak was one of the largest that have occurred; it started in Guinea and spread to Nigeria, Liberia and Sierra Leone. Phylogenetic analysis of the current virus species indicated that this outbreak is the result of a divergent lineage of the Zaire ebolavirus. The L protein of Ebola virus (EBOV) is the catalytic subunit of the RNA‑dependent RNA polymerase complex, which, with VP35, is key for the replication and transcription of viral RNA. Earlier sequence analysis demonstrated that the L protein of all non‑segmented negative‑sense (NNS) RNA viruses consists of six domains containing conserved functional motifs. The aim of the present study was to analyze the presence of these motifs in 2014 EBOV isolates, highlight their function and how they may contribute to the overall pathogenicity of the isolates. For this purpose, 81 2014 EBOV L protein sequences were aligned with 475 other NNS RNA viruses, including Paramyxoviridae and Rhabdoviridae viruses. Phylogenetic analysis of all EBOV outbreak L protein sequences was also performed. Analysis of the amino acid substitutions in the 2014 EBOV outbreak was conducted using sequence analysis. The alignment demonstrated the presence of previously conserved motifs in the 2014 EBOV isolates and novel residues. Notably, all the mutations identified in the 2014 EBOV isolates were tolerant, they were pathogenic with certain examples occurring within previously determined functional conserved motifs, possibly altering viral pathogenicity, replication and virulence. The phylogenetic analysis demonstrated that all sequences with the exception of the 2014 EBOV sequences were clustered together. The 2014 EBOV outbreak has acquired a great number of mutations, which may explain the reasons behind this unprecedented outbreak. Certain residues critical to the function of the polymerase remain conserved and may be targets for the development of antiviral therapeutic agents.

Protein (Cyanobacteria): 661290558 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available SPYFYASWMPEKEDDYRFTNKKRTPLECSTGTKDARSAALKAISWVKEKQKDCLRKITEYQEVKTKCLEHYWEEHFIDFSSTRASRKSVTKLINDEKLKWCSPTYGIG...6:352 ... hypothetical protein Prochlorococcus sp. scB243_495N4 MTSLSAMDGKLNDRTWINISESRYELELGNRVSFPINLYLKKRVN

Hydra meiosis reveals unexpected conservation of structural synaptonemal complex proteins across metazoans.

Science.gov (United States)

Fraune, Johanna; Alsheimer, Manfred; Volff, Jean-Nicolas; Busch, Karoline; Fraune, Sebastian; Bosch, Thomas C G; Benavente, Ricardo

2012-10-09

The synaptonemal complex (SC) is a key structure of meiosis, mediating the stable pairing (synapsis) of homologous chromosomes during prophase I. Its remarkable tripartite structure is evolutionarily well conserved and can be found in almost all sexually reproducing organisms. However, comparison of the different SC protein components in the common meiosis model organisms Saccharomyces cerevisiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, and Mus musculus revealed no sequence homology. This discrepancy challenged the hypothesis that the SC arose only once in evolution. To pursue this matter we focused on the evolution of SYCP1 and SYCP3, the two major structural SC proteins of mammals. Remarkably, our comparative bioinformatic and expression studies revealed that SYCP1 and SYCP3 are also components of the SC in the basal metazoan Hydra. In contrast to previous assumptions, we therefore conclude that SYCP1 and SYCP3 form monophyletic groups of orthologous proteins across metazoans.

Differences in Behavior and Brain Activity during Hypothetical and Real Choices.

Science.gov (United States)

Camerer, Colin; Mobbs, Dean

2017-01-01

Real behaviors are binding consequential commitments to a course of action, such as harming another person, buying an Apple watch, or fleeing from danger. Cognitive scientists are generally interested in the psychological and neural processes that cause such real behavior. However, for practical reasons, many scientific studies measure behavior using only hypothetical or imagined stimuli. Generalizing from such studies to real behavior implicitly assumes that the processes underlying the two types of behavior are similar. We review evidence of similarity and differences in hypothetical and real mental processes. In many cases, hypothetical choice tasks give an incomplete picture of brain circuitry that is active during real choice. Copyright © 2016. Published by Elsevier Ltd.

Gains of ubiquitylation sites in highly conserved proteins in the human lineage

Directory of Open Access Journals (Sweden)

Kim Dong Seon

2012-11-01

Full Text Available Abstract Background Post-translational modification of lysine residues of specific proteins by ubiquitin modulates the degradation, localization, and activity of these target proteins. Here, we identified gains of ubiquitylation sites in highly conserved regions of human proteins that occurred during human evolution. Results We analyzed human ubiquitylation site data and multiple alignments of orthologous mammalian proteins including those from humans, primates, other placental mammals, opossum, and platypus. In our analysis, we identified 281 ubiquitylation sites in 252 proteins that first appeared along the human lineage during primate evolution: one protein had four novel sites; four proteins had three sites each; 18 proteins had two sites each; and the remaining 229 proteins had one site each. PML, which is involved in neurodevelopment and neurodegeneration, acquired three sites, two of which have been reported to be involved in the degradation of PML. Thirteen human proteins, including ERCC2 (also known as XPD and NBR1, gained human-specific ubiquitylated lysines after the human-chimpanzee divergence. ERCC2 has a Lys/Gln polymorphism, the derived (major allele of which confers enhanced DNA repair capacity and reduced cancer risk compared with the ancestral (minor allele. NBR1 and eight other proteins that are involved in the human autophagy protein interaction network gained a novel ubiquitylation site. Conclusions The gain of novel ubiquitylation sites could be involved in the evolution of protein degradation and other regulatory networks. Although gains of ubiquitylation sites do not necessarily equate to adaptive evolution, they are useful candidates for molecular functional analyses to identify novel advantageous genetic modifications and innovative phenotypes acquired during human evolution.

Protein (Viridiplantae): 232868 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 3051:4703 ... 3052:4703 ... 3055:4703 ... hypothetical protein CHLREDRAFT_120274, partial Chlamydomonas reinhardtii PPGCRCSSAPPGCRC...SSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCSSAPPGCRCS

Protein (Viridiplantae): 302830920 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 058 3068:3058 hypothetical protein VOLCADRAFT_87241 Volvox carteri f. nagariensis MPNPLAEMELLGFWGLKLVATVTDCHMSDSGRVMTAFVFKVVSYRNEAAST...LAEMELLGFWGLKLVATVTDCHMSDSGRVMTAFVFKVVSYRNEAASTMLTPEPLPESLEYLQAQVERALDERRELERVMWA...AREGRGGPSMLSCKQLETIELSTMGEAAELEVKRALEAITVVQYSMPNPLAEMELLGFWGLKLVATVTDCHMSDSGRVMTAFVFKVVSYRNEAASTMLTPEPLPESLEYLQAQVERALDERRELERVMWAAREGRGGPSMLSCKQLETIELSTMGEAAELEVKRALEEMFH ...

Protein (Cyanobacteria): 661286037 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 0:477 ... hypothetical protein, partial Prochlorococcus sp. scB243_498P3 MSTKSDSLKEKLIENFSDFSKLSDYSFMNYLRADPQ...STKDGNDHKPRSVYSGHYVPVLPTAIPEPEYISHSKKLFKELRLSSDLTKDKNFCLFFSGDISVANYPMSPVGWATGYALSIYGTEYTQQCPFGTGNGYGDGIAISVFEGLFNGKRMEMQLKGGGPTPYCRGA

Conservation, diversification and expansion of C2H2 zinc finger proteins in the Arabidopsis thaliana genome

Directory of Open Access Journals (Sweden)

Böhm Siegfried

2004-07-01

Full Text Available Background The classical C2H2 zinc finger domain is involved in a wide range of functions and can bind to DNA, RNA and proteins. The comparison of zinc finger proteins in several eukaryotes has shown that there is a lot of lineage specific diversification and expansion. Although the number of characterized plant proteins that carry the classical C2H2 zinc finger motifs is growing, a systematic classification and analysis of a plant genome zinc finger gene set is lacking. Results We found through in silico analysis 176 zinc finger proteins in Arabidopsis thaliana that hence constitute the most abundant family of putative transcriptional regulators in this plant. Only a minority of 33 A. thaliana zinc finger proteins are conserved in other eukaryotes. In contrast, the majority of these proteins (81% are plant specific. They are derived from extensive duplication events and form expanded families. We assigned the proteins to different subgroups and families and focused specifically on the two largest and evolutionarily youngest families (A1 and C1 that are suggested to be primarily involved in transcriptional regulation. The newly defined family A1 (24 members comprises proteins with tandemly arranged zinc finger domains. Family C1 (64 members, earlier described as the EPF-family in Petunia, comprises proteins with one isolated or two to five dispersed fingers and a mostly invariant QALGGH motif in the zinc finger helices. Based on the amino acid pattern in these helices we could describe five different signature sequences prevalent in C1 zinc finger domains. We also found a number of non-finger domains that are conserved in these families. Conclusions Our analysis of the few evolutionarily conserved zinc finger proteins of A. thaliana suggests that most of them could be involved in ancient biological processes like RNA metabolism and chromatin-remodeling. In contrast, the majority of the unique A. thaliana zinc finger proteins are known or

NCBI nr-aa BLAST: CBRC-CREM-01-1365 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CREM-01-1365 ref|YP_056345.1| hypothetical protein PPA1652 [Propionibacterium acne...s KPA171202] gb|AAT83387.1| conserved protein [Propionibacterium acnes KPA171202] YP_056345.1 5e-19 40% ...

Annotation and Curation of Uncharacterized proteins- Challenges

Directory of Open Access Journals (Sweden)

Johny eIjaq

2015-03-01

Full Text Available Hypothetical Proteins are the proteins that are predicted to be expressed from an open reading frame (ORF, constituting a substantial fraction of proteomes in both prokaryotes and eukaryotes. Genome projects have led to the identification of many therapeutic targets, the putative function of the protein and their interactions. In this review we have enlisted various methods. Annotation linked to structural and functional prediction of hypothetical proteins assist in the discovery of new structures and functions serving as markers and pharmacological targets for drug designing, discovery and screening. Mass spectrometry is an analytical technique for validating protein characterisation. Matrix-assisted laser desorption ionization–mass spectrometry (MALDI-MS is an efficient analytical method. Microarrays and Protein expression profiles help understanding the biological systems through a systems-wide study of proteins and their interactions with other proteins and non-proteinaceous molecules to control complex processes in cells and tissues and even whole organism. Next generation sequencing technology accelerates multiple areas of genomics research.

ProClaT, a new bioinformatics tool for in silico protein reclassification: case study of DraB, a protein coded from the draTGB operon in Azospirillum brasilense.

Science.gov (United States)

Rubel, Elisa Terumi; Raittz, Roberto Tadeu; Coimbra, Nilson Antonio da Rocha; Gehlen, Michelly Alves Coutinho; Pedrosa, Fábio de Oliveira

2016-12-15

Azopirillum brasilense is a plant-growth promoting nitrogen-fixing bacteria that is used as bio-fertilizer in agriculture. Since nitrogen fixation has a high-energy demand, the reduction of N 2 to NH 4 + by nitrogenase occurs only under limiting conditions of NH 4 + and O 2 . Moreover, the synthesis and activity of nitrogenase is highly regulated to prevent energy waste. In A. brasilense nitrogenase activity is regulated by the products of draG and draT. The product of the draB gene, located downstream in the draTGB operon, may be involved in the regulation of nitrogenase activity by an, as yet, unknown mechanism. A deep in silico analysis of the product of draB was undertaken aiming at suggesting its possible function and involvement with DraT and DraG in the regulation of nitrogenase activity in A. brasilense. In this work, we present a new artificial intelligence strategy for protein classification, named ProClaT. The features used by the pattern recognition model were derived from the primary structure of the DraB homologous proteins, calculated by a ProClaT internal algorithm. ProClaT was applied to this case study and the results revealed that the A. brasilense draB gene codes for a protein highly similar to the nitrogenase associated NifO protein of Azotobacter vinelandii. This tool allowed the reclassification of DraB/NifO homologous proteins, hypothetical, conserved hypothetical and those annotated as putative arsenate reductase, ArsC, as NifO-like. An analysis of co-occurrence of draB, draT, draG and of other nif genes was performed, suggesting the involvement of draB (nifO) in nitrogen fixation, however, without the definition of a specific function.

Evaluation of hypothetical (153)Gd source for use in brachytherapy.

Science.gov (United States)

Ghorbani, Mahdi; Behmadi, Marziyeh

2016-01-01

The purpose of this work is to evaluate the dosimetric parameters of a hypothetical (153)Gd source for use in brachytherapy and comparison of the dosimetric parameters with those of (192)Ir and (125)I sources. Dose rate constant, the radial dose function and the two dimensional (2D) anisotropy function data for the hypothetical (153)Gd source were obtained by simulation of the source using MCNPX code and then were compared with the corresponding data reported by Enger et al. A comprehensive comparison between this hypothetical source and a (192)Ir source with similar geometry and a (125)I source was performed as well. Excellent agreement was shown between the results of the two studies. Dose rate constant values for the hypothetical (153)Gd, (192)Ir, (125)I sources are 1.173 cGyh(-1) U(-1), 1.044 cGyh(-1) U(-1), 0.925 cGyh(-1) U(-1), respectively. Radial dose function for the hypothetical (153)Gd source has an increasing trend, while (192)Ir has more uniform and (125)I has more rapidly falling off radial dose functions. 2D anisotropy functions for these three sources indicate that, except at 0.5 cm distance, (192)Ir and (125)I have more isotropic trends as compared to the (153)Gd source. A more uniform radial dose function, and 2D anisotropy functions with more isotropy, a much higher specific activity are advantages of (192)Ir source over (153)Gd. However, a longer half-life of (153)Gd source compared to the other two sources, and lower energy of the source with respect to (192)Ir are advantages of using (153)Gd in brachytherapy versus (192)Ir source.

FuncPatch: a web server for the fast Bayesian inference of conserved functional patches in protein 3D structures.

Science.gov (United States)

Huang, Yi-Fei; Golding, G Brian

2015-02-15

A number of statistical phylogenetic methods have been developed to infer conserved functional sites or regions in proteins. Many methods, e.g. Rate4Site, apply the standard phylogenetic models to infer site-specific substitution rates and totally ignore the spatial correlation of substitution rates in protein tertiary structures, which may reduce their power to identify conserved functional patches in protein tertiary structures when the sequences used in the analysis are highly similar. The 3D sliding window method has been proposed to infer conserved functional patches in protein tertiary structures, but the window size, which reflects the strength of the spatial correlation, must be predefined and is not inferred from data. We recently developed GP4Rate to solve these problems under the Bayesian framework. Unfortunately, GP4Rate is computationally slow. Here, we present an intuitive web server, FuncPatch, to perform a fast approximate Bayesian inference of conserved functional patches in protein tertiary structures. Both simulations and four case studies based on empirical data suggest that FuncPatch is a good approximation to GP4Rate. However, FuncPatch is orders of magnitudes faster than GP4Rate. In addition, simulations suggest that FuncPatch is potentially a useful tool complementary to Rate4Site, but the 3D sliding window method is less powerful than FuncPatch and Rate4Site. The functional patches predicted by FuncPatch in the four case studies are supported by experimental evidence, which corroborates the usefulness of FuncPatch. The software FuncPatch is freely available at the web site, http://info.mcmaster.ca/yifei/FuncPatch golding@mcmaster.ca Supplementary data are available at Bioinformatics online. © The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.

Assessing Hypothetical Gravity Control Propulsion

OpenAIRE

Millis, Marc G.

2006-01-01

Gauging the benefits of hypothetical gravity control propulsion is difficult, but addressable. The major challenge is that such breakthroughs are still only notional concepts rather than being specific methods from which performance can be rigorously quantified. A recent assessment by Tajmar and Bertolami used the rocket equation to correct naive misconceptions, but a more fundamental analysis requires the use of energy as the basis for comparison. The energy of a rocket is compared to an ide...

Protein (Cyanobacteria): 652400785 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796581.1 ... 1117:7580 ... 1150:51181 1301283:72257 ... 54304:1131 54307:211 ... hypothetical protein Plankt...NDVINTIEHLLETEFQQSCIHKRLKLPGLASEIALVVDGTLQTIGFYHQKIHVLSEMNKTIACSIAKAQRELGYNPTIALEEGMRRSLKWIFENYGGLD

Protein (Cyanobacteria): 653002349 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254540.1 ... 1117:3646 ... 1150:52865 1301283:74127 ... 54304:528 1160:1354 ... hypothetical protein Plankt...FCQRYKPKEKKTPTRCHWGSKLLAGVHLSNKTLTTNPKKSKSRLVQTPCQVSKSPELTRVVSQFIEANRAPWQAEKDF

Protein (Cyanobacteria): 652400958 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796754.1 ... 1117:7970 ... 1150:52478 1301283:73697 ... 54304:23 54307:536 ... hypothetical protein Plankt...LAKLKQDIAQTEALNPMEKAMVEVPIKMIESELQKPEANKTLINQAVVALKKGLEGVETLAEPVIKVAAILAKVWI

Protein (Cyanobacteria): 652997006 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249473.1 ... 1117:5662 ... 1150:51230 1301283:72312 ... 54304:1176 1160:459 ... hypothetical protein Plankt...RQISFRDQNNTVQWVIHRPDETPTESQWTILDQGVQIDTEETTLYQNKTTKIWRMQFDHKGRANGQLGRMTVSLRNGSPAKRCTFVSTLLGTLRTSQNNPKPKDGKYCY

Protein (Cyanobacteria): 652400689 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796485.1 ... 1117:7766 ... 1150:53377 1301283:74696 ... 54304:99 54307:105 ... hypothetical protein Plankt...GNYADSEAIFRQLVENQPKEAKYHFYLGNSLFYQRKIEEATQVYQEAISLNPQYGLAYNALGFLHASQGQWDEAIAQYQKALEINPDYAEALKNLGESLWKKGNTAEANNAWKKALELYTQQGNNKAVLQLQEMLNKTSQ

Protein (Cyanobacteria): 652392302 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026788149.1 ... 1117:1255 ... 1150:52201 1301283:73391 ... 54304:205 59512:888 ... hypothetical protein Plankt...ARTEQLPEPVYTQGLIRTYADALGLNGVELANFFLPEPQKVGMKSKLNFLTLPQLRPTHLYLTYILLIICAINGVSYLNKTANFASVSGEPVATTNPPEVNPQLRQAV

Protein (Cyanobacteria): 652390785 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026786633.1 ... 1117:7276 ... 1150:53339 1301283:74654 ... 54304:955 59512:541 ... hypothetical protein Plankt...HEAQPDKFPHIPASMWWAVITLTTVGYGDVYPITPLGRLLGGILALLGIGLIALPAGIIASGFTEVIALNQRKNKTIYPKICPHCGKNIDQPLEDSTDLDH

Protein (Cyanobacteria): 652389677 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026785525.1 ... 1117:5888 ... 1150:52976 1301283:74250 ... 54304:628 59512:189 ... hypothetical protein Plankt...GVALLGMAYPIFSKMLSNDTLTKEPFRVFFALAIFLLSIASFTLLFKARVKLWKGIFATFTGMGLIILGSQPEIYRRDNEWFVSHYYYGITAALLMIFSVAIVQDIYQDKQNRWRTAHIILNCFALLLFIGQGMTGARDLLEIPLHWQEHYIYQCDFTNKTCSQPK

Protein (Cyanobacteria): 653003380 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027255564.1 ... 1117:4943 ... 1150:53097 1301283:74385 ... 54304:737 1160:1650 ... hypothetical protein Plankt...TSGRKQAKSGKGFSPVMVGQKWMLSQLEKLVPVVKIEGYRTASTRKYLGLKKNKTDKSKPEFNTHAVDGVAIAATAFVEYR

Protein (Cyanobacteria): 652996507 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027248974.1 ... 1117:6200 ... 1150:51081 1301283:72146 ... 54304:1041 1160:304 ... hypothetical protein Plankt...NGENVLIEMQAFNVPAFGKRILYNTAKMYVNQLKLGEVYPELRAAIGVAVTDFIMFNEHNKVISQFTLKEDELQVNYQHSPLKLVFVELPKFNKTLEELTTITDKWLY

Protein (Cyanobacteria): 653003025 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027255213.1 ... 1117:7881 ... 1150:51355 1301283:72450 ... 54304:1289 1160:584 ... hypothetical protein Plankt...SPPDGVSPLSETPTPAITTPISPTPQVKQPESAILGLVFVTPAQKPIQPALKPQIIPGTQSQNKTSTKTACSVQPTTGNICTTPLPSAVVPSSTTTESYWATPFILYF

Protein (Cyanobacteria): 652402235 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026798031.1 ... 1117:6249 ... 1150:53365 1301283:74683 ... 54304:979 54307:314 ... hypothetical protein Plankt...LCEEISSQLLLPVETDYVDSDFNYSSLWQNKTVETSWFSKILYTAQKPNSQPIFSPSLVSFLVGCTDSEATAKKSKKIRIYLNPEQKKLLKQWFGVSRFVYNETIKYLQQPDTKANWMAIKTGILNGLPEWAKPWVD

Protein (Cyanobacteria): 652996481 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027248948.1 ... 1117:44906 ... 1150:51132 1301283:72203 ... 54304:1088 1160:350 ... hypothetical protein Plankt...IFVEEGSVLNEKIEKAYSELKIEVKKKESTSDQQEKARNWMIENFYDIRMFGAVLSTGLNAGQVWGPLQISWGRSYDPVLPISATITRCAATEAKEKKDNKTMGRKEL

Protein (Cyanobacteria): 652391798 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026787645.1 ... 1117:7766 ... 1150:53377 1301283:74696 ... 54304:99 59512:39 ... hypothetical protein Plankt...NYAASEAIFRQLVENQPKEAKYHFYLGNSLFYQRKIEEATQVYQEAISLNPQYGLAYNALGFLHASQGQWDEAIAQYQKALEINPDYAEALKNLGESLWKKGNTAEANNAWKKALELYTQQGNNKAVLQLQEMLNKTSQ

Protein (Cyanobacteria): 652402868 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026798653.1 ... 1117:6200 ... 1150:51081 1301283:72146 ... 54304:1041 54307:1121 ... hypothetical protein Plankt...QLNNGENVLIEMQAFNVPAFGKKILYNTAKMYVNQLKLGEVYPELRAAIGVAVTDFIMFNEHNKVISQFTLKEDELQVNYQHSPLKLVFVELPKFNKTLEELTTITDK

Protein (Cyanobacteria): 652997420 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249886.1 ... 1117:7580 ... 1150:51181 1301283:72257 ... 54304:1131 1160:409 ... hypothetical protein Plankt...VINTIEHLLETEFQQSCIHKRLKLPGLASEIALVVDGTLQTLGFYHQKIHVLSEMNKTIACSIAKAQRELGYNPTIALEEGMRRSLKWIFENYGGLD

Protein (Cyanobacteria): 652390511 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026786359.1 ... 1117:2598 ... 1150:51863 1301283:73014 ... 54304:1746 59512:466 ... hypothetical protein Plankt...INCYRVIKDNVEELIEVLKVHKAKNSKEYFDYLRERDRLKQYNKFSDIQKAARIIYLNKTCYNGLFRVNSKGQFNVPFGSYKNPNILDEAVLRGVNDYLNQKSVTFLN

Protein (Cyanobacteria): 652997790 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027250244.1 ... 1117:4728 ... 1150:51209 1301283:72288 ... 54304:1157 1160:435 ... hypothetical protein Plankt...DKVMTIVESLSGYKLYKTASENFGLIFETAQKIINLPEPARKDIAKWLKLSNPCSVNKIGDIQENLYFLGDFSEAIIQAGLSQNKTFFSRN

Protein (Cyanobacteria): 652996974 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249441.1 ... 1117:5593 ... 1150:51293 1301283:72381 ... 54304:1232 1160:703 ... hypothetical protein Plankt...KWIREDRMSSGMWRTIIHIGEIFLSSEGSVILIDEFENSLGINCIDILTEDLIHENKTLQFIATSHHPYIINNIPYEYWKIVTRQGGHISIGNASDYHLGKSKQDAFIQLTKILEKQS

Protein (Cyanobacteria): 652391987 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026787834.1 ... 1117:7580 ... 1150:51181 1301283:72257 ... 54304:1131 59512:170 ... hypothetical protein Plankt...NDIINTIEHLLETEFQQSCTHKRLKLPGLASEIALVVDGTLQTLGFYHQKIHVLSEMNKTIACSIAKSQRELGYNPTITLEEGMRRSLKWIFENYGGLD

Protein (Cyanobacteria): 652400636 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796432.1 ... 1117:6249 ... 1150:53365 1301283:74683 ... 54304:979 54307:314 ... hypothetical protein Plankt...LCEEISSQLLLPVETDYVDSDFNYSSLWQNKTVETSWFSKILYTAQKPNSQPIFSPSLVSFLVGCTDSEATAKKSKKIRIYLNPEQKKLLKQWFGVSRFVYNETIKYLQQPDTKANWMAIKTGILNGLPEWAKPGID

Protein (Cyanobacteria): 652390179 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026786027.1 ... 1117:3646 ... 1150:52865 1301283:74127 ... 54304:528 59512:364 ... hypothetical protein Plankt...GFCQRYKPKEKKTPTRCHWGSKLLAGVHLSNKTLTTNPKKSKSRLVQTPCQVSKRPELTRIVSQFIEANRAPWQAEKDF

Protein (Cyanobacteria): 652997530 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249996.1 ... 1117:1255 ... 1150:52201 1301283:73391 ... 54304:205 1160:1045 ... hypothetical protein Plankt...RTEQLPEPVYTQGLIRTYADALGLNGVELANFFLPEPQKVGMKSKLNFLTLPQLRPTHLYLTYILLIICAINGVSYLNKTANFASVSGEPVATTNPPEVNAQLRQAVV

Protein (Cyanobacteria): 652402139 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026797935.1 ... 1117:2598 ... 1150:51863 1301283:73014 ... 54304:1746 54307:1182 ... hypothetical protein Plankt...LINCYRVIKDNVEELIEVLKVHKAKNSKEYFDYLRERDRLKQYNKFSDIQKAARIIYLNKTCYNGLFRVNSKGQFNVPFGSYKNPNILDEAVLRGVNDYLNQKSVTFL

Protein (Cyanobacteria): 653002222 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254413.1 ... 1117:3316 ... 1150:51705 1301283:72839 ... 54304:1603 1160:934 ... hypothetical protein Plankt...NLNSDWFCYHDRNFGRFRWGEDIGWEWFVIFAQTETKIPLTLILDWRTNKTHSQGGLPYIFIYQNHQLRKIFLGETLRLNW

Protein (Cyanobacteria): 652401612 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026797408.1 ... 1117:6743 ... 1150:53326 1301283:74640 ... 54304:943 54307:169 ... hypothetical protein Plankt...WLWNRQNQLGIAFDSSTGFHLPNGADRSPDASWIRQERWDLLTQEEREIFAPICPDFVLELRSKNDAIEKLQAKMIEYIENGASLGWLIDRKNKTVEIYRQNQDIELLNHPLILSGEDILPGFMLNLTEVWN

Protein (Cyanobacteria): 652997358 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249824.1 ... 1117:3316 ... 1150:51705 1301283:72839 ... 54304:1603 1160:934 ... hypothetical protein Plankt...NLNSDWFCYHDRNFGRFRWGEDIGWEWFVIFAQTETKIPLTLILDWRTNKTHSQGGLPYIFIYQNHQLRKIFLGETLRLNW

Protein (Cyanobacteria): 653002178 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254369.1 ... 1117:7580 ... 1150:51181 1301283:72257 ... 54304:1131 1160:409 ... hypothetical protein Plankt...VINTIEHLLETEFQQSCIHKRLKLPGLASEIALVVDGTLQTIGFYHQKIHVLSEMNKTIACSIAKAQRELGYNPTIALEAGMRKSLKWIFENYGGLD

Protein (Cyanobacteria): 653002395 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254586.1 ... 1117:6743 ... 1150:53326 1301283:74640 ... 54304:943 1160:197 ... hypothetical protein Plankt...WNRQNQLGIAFDSSTGFHLPNGADRSPDASWIRQERWDLLTQEEREIFAPICPDFVLELRSKNDALEKLQAKMIEYIENGASLGWLIDRKNKTVEIYRQNQDIELLNHPLILSGEDILPGFMLDLTEVWN

Protein (Cyanobacteria): 652997575 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027250041.1 ... 1117:7881 ... 1150:51355 1301283:72450 ... 54304:1289 1160:584 ... hypothetical protein Plankt...SPPDGVSPLWETPTPAITTPISPTPQVKQPQSAILGLVFVTPAQKPIQPALKPQIIPGTQSQNKTSTKTACSVQPTTGNICTTPLPSAVVPSSTTTESYWATPFILYF

Protein (Cyanobacteria): 653002660 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254850.1 ... 1117:5593 ... 1150:51293 1301283:72381 ... 54304:1232 1160:703 ... hypothetical protein Plankt...WIREDRMSSGMWRTIIHIGEIFLSSEGSVILIDEFENSLGINCIDILTEDLIHENKTLQFIATSHHPYIINNIPYEYWKIVTRQGGHISIGNASDYHLGKSKQDAFIQLTKILEKQS

Protein (Cyanobacteria): 653002681 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254871.1 ... 1117:17730 ... 1150:52975 1301283:74249 ... 54304:627 1160:1450 ... hypothetical protein Plankt...DCCAWSMQTVYSELQKHGAEFRFVPWDTFRDGARERNKTVPSELGGFSRSNDAAFLQEAADFINNQLDPNRPLVLIGHSFGGDSLLSLVPRINRRIQFLGVIDPTAAG

Protein (Cyanobacteria): 504983429 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170531.1 ... 1117:3357 ... 1150:56771 1301283:78467 ... 63132:1699 1173025:617 ... hypothetical protein Geit...QHDLQQTVVATARVIDERQVRTSSGHTELRPVIHTPILLGGCQWPIEITLTNRDVMGFRMLLGRQAIRQRFLVDPGHSFLLSSLRLPLRSPTSRSQPL

Protein (Cyanobacteria): 504984105 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015171207.1 ... 1117:173 ... 1150:57133 1301283:78870 ... 63132:2023 1173025:1133 ... hypothetical protein Geit...RTSIPGAVRYTVVYDNGANQAVVAVAPEITETELEATLRQAAGDLFSLGRYGGQDNQFMIRARTIIHPSEGLSKPLFLGQVKRSLAVREDENMQVELFRQNFAELPSDRA

Structural and Sequence Similarities of Hydra Xeroderma Pigmentosum A Protein to Human Homolog Suggest Early Evolution and Conservation

Directory of Open Access Journals (Sweden)

Apurva Barve

2013-01-01

Full Text Available Xeroderma pigmentosum group A (XPA is a protein that binds to damaged DNA, verifies presence of a lesion, and recruits other proteins of the nucleotide excision repair (NER pathway to the site. Though its homologs from yeast, Drosophila, humans, and so forth are well studied, XPA has not so far been reported from protozoa and lower animal phyla. Hydra is a fresh-water cnidarian with a remarkable capacity for regeneration and apparent lack of organismal ageing. Cnidarians are among the first metazoa with a defined body axis, tissue grade organisation, and nervous system. We report here for the first time presence of XPA gene in hydra. Putative protein sequence of hydra XPA contains nuclear localization signal and bears the zinc-finger motif. It contains two conserved Pfam domains and various characterized features of XPA proteins like regions for binding to excision repair cross-complementing protein-1 (ERCC1 and replication protein A 70 kDa subunit (RPA70 proteins. Hydra XPA shows a high degree of similarity with vertebrate homologs and clusters with deuterostomes in phylogenetic analysis. Homology modelling corroborates the very close similarity between hydra and human XPA. The protein thus most likely functions in hydra in the same manner as in other animals, indicating that it arose early in evolution and has been conserved across animal phyla.

Protein (Viridiplantae): 108124 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 065:363 ... 3066:363 ... 3067:363 ... 3068:363 ... hypothetical protein VOLCADRAFT_99209 Volvox carteri f. nagariensis MQMHAHTYNISHIVYCISH...IAYCISHIAYRISHIAYRISHIVYRVSHIAYRILHIAYCILHIAYCILHIAYCILHIAYCILHIAYCILHIAYRISHIAAYMAYRISHTAYRISQIAYRCISHIAAYRCILHITYMHIIYAHI

Protein (Viridiplantae): 108120 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 065:363 ... 3066:363 ... 3067:363 ... 3068:363 ... hypothetical protein VOLCADRAFT_100737 Volvox carteri f. nagariensis MYNISHIVYCISHIAYCISH...IAYRISHIAYRILHIAYCISHIAYCISHIAYCISHIAYRISHIPYRCTISLHMAYRISHTARISHIANCISLHIAYCILHIAYCISHIAYPISLHHIAAYGISHITYRTHIAYRKLHIAAYRISLHIAAYCISHIHICIYAHI

Protein (Viridiplantae): 108121 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 065:363 ... 3066:363 ... 3067:363 ... 3068:363 ... hypothetical protein VOLCADRAFT_90903 Volvox carteri f. nagariensis MQMHIVYCISH...IAYCILHIAYRILHIAYCISHIAYRILHIAYCILHIAYCISHVAYCISHIPYRCIWHIARISHTAYRIPQITYRCISHIAAYRCILHITYTYMYIYAHI

Protein (Viridiplantae): 108123 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 065:363 ... 3066:363 ... 3067:363 ... 3068:363 ... hypothetical protein VOLCADRAFT_71945 Volvox carteri f. nagariensis MRICLHIAYVCISH...IAYRICACLHIAISHIIHIAYRILPIAYCISHIAYCISHIAYCILHIAYCISHIAYRISHIAYCISHIAYCISHIAYCILHIAYCILHIAYCILHIAYCILHIAYCILHIAYCILHIAYCILHIAAYGILHIAYAYRSQHSIA

Protein (Viridiplantae): 875613 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 35472:181 ... 41891:181 ... 248742:181 ... 574566:181 hypothetical protein COCSUDRAFT_37270 Coccomyxa subellipso...idea C-169 MAAAVLSLLATSCTPATGAMPAFARMSIDIAEASEVESSAEASTSKAPMPVYFGNGCFWGRQKDFVDAEKALGRSPEQISSVVGYAGGREQGPKGRV

Protein (Cyanobacteria): 354631 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007110277.1 1117:15352 1150:9068 63132:1761 1173025:1761 hypothetical protein GEI7407_2752 Geit...GGTEYTVIPDTLTIGGPATLVGASDRGIEYTAPLQSRYASCVGETLEQPERYYHARFQNGQVTFRVDFTALPSGLYSEITHLNVVNARPYVRWAVVD ...

Protein (Cyanobacteria): 354630 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109738.1 1117:15352 1150:9068 63132:1761 1173025:1761 hypothetical protein GEI7407_2207 Geit...DTAAIAGRAVFLEAKQDFVEFAAPLKPQYASCYGYVVSSDEPQYNLWFYKGYVYFRFDLQSLPGRPLSEITSQAIIEDRPFMRWAIAD ...

Protein (Cyanobacteria): 345550 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007110830.1 1117:12257 1150:7214 63132:1987 1173025:1987 hypothetical protein GEI7407_3311 Geit...TAKGYVLWVLEPDAYLDGAEAIAPQAETPAQPTQTSTPCKILDSKSQYRTCHIRVPDLQQRLAALWVDGKYYALFKVVPTVDKAMEITARFGRRGDETVIAKTKKGYSVWVLEPEAYPAPTP ...

Protein (Cyanobacteria): 314283 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109292.1 1117:7227 1150:63 63132:1506 1173025:1506 hypothetical protein GEI7407_1753 Geit...IGLIALLLLGVTVFTQSQQQLLTRVTAERDRITLVQDDGGDLSTVLRQTSGEVVYRVTLSDAPVGQKLSLSCNWMDPNGQIVHQNRYQTKEITTPVWNTICRHTIGSAAPVGTWKVQMLLGDRLLSDTTFVVK ...

Protein (Cyanobacteria): 248585 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007111118.1 1117:4619 1150:1758 63132:2521 1173025:2521 hypothetical protein GEI7407_3599 Geit...VTLADSLKRQRPAILFFYLDDSRDSKQYASVVSQLQAFYGRAADFLPLSIDTLPLEGSPDLKDPAHYYKGFVPQTVIIDQSGKVVFDQSGVLALESVDDVLRKVFDLLPRSESVELKRRPLNEINIEITSEPQ ...

Genes encoding calmodulin-binding proteins in the Arabidopsis genome

Science.gov (United States)

Reddy, Vaka S.; Ali, Gul S.; Reddy, Anireddy S N.

2002-01-01

Analysis of the recently completed Arabidopsis genome sequence indicates that approximately 31% of the predicted genes could not be assigned to functional categories, as they do not show any sequence similarity with proteins of known function from other organisms. Calmodulin (CaM), a ubiquitous and multifunctional Ca(2+) sensor, interacts with a wide variety of cellular proteins and modulates their activity/function in regulating diverse cellular processes. However, the primary amino acid sequence of the CaM-binding domain in different CaM-binding proteins (CBPs) is not conserved. One way to identify most of the CBPs in the Arabidopsis genome is by protein-protein interaction-based screening of expression libraries with CaM. Here, using a mixture of radiolabeled CaM isoforms from Arabidopsis, we screened several expression libraries prepared from flower meristem, seedlings, or tissues treated with hormones, an elicitor, or a pathogen. Sequence analysis of 77 positive clones that interact with CaM in a Ca(2+)-dependent manner revealed 20 CBPs, including 14 previously unknown CBPs. In addition, by searching the Arabidopsis genome sequence with the newly identified and known plant or animal CBPs, we identified a total of 27 CBPs. Among these, 16 CBPs are represented by families with 2-20 members in each family. Gene expression analysis revealed that CBPs and CBP paralogs are expressed differentially. Our data suggest that Arabidopsis has a large number of CBPs including several plant-specific ones. Although CaM is highly conserved between plants and animals, only a few CBPs are common to both plants and animals. Analysis of Arabidopsis CBPs revealed the presence of a variety of interesting domains. Our analyses identified several hypothetical proteins in the Arabidopsis genome as CaM targets, suggesting their involvement in Ca(2+)-mediated signaling networks.

ORF Alignment: NC_002162 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available [imported] - ... Ureaplasma urealyticum ... Length = 313 ... Query: 8... NC_002162 gi|13357852 >1esc0 2 302 87 399 2e-29 ... ref|NP_078126.1| hypothetical protein UU292 [Ureap...lasma parvum serovar 3 str. ATCC ... 700970] gb|AAF30701.1| conserved hypothetical ... [Ureap...7 ... KINYLAIGDSITAGFNSELGWEAPGRYDPITNKISGLSFPSFIAQYINKVEPNRLASYEN 146 ... KINYLAIGDSITAGFNSELGWEAPGRYDP...ITNKISGLSFPSFIAQYINKVEPNRLASYEN Sbjct: 1 ... KINYLAIGDSITAGFNSELGWEAPGRYDPITNKISGLSFPSFIAQYINKVEPNRLASYEN 60 ...

ORF Alignment: NC_002162 [GENIUS II[Archive

Lifescience Database Archive (English)

Full Text Available NC_002162 gi|13358063 >1t71A 5 267 1 262 2e-78 ... ref|NP_078337.1| hypothetical protein UU500 [Ureap...lasma parvum serovar 3 str. ATCC ... 700970] gb|AAF30912.1| conserved hypothetical ... [Ureap...[imported] - ... Ureaplasma urealyticum ... Length = 262 ... Query: 1 ...ery: 121 GNSIDMKGLQTNPFESLDKIIAFNEAPIHIVDFHAETTSEKNALFLDFKSKLSLVYGTHT 180 ... ... ... GNSIDMKGLQTNPFESLDKIIAFNEAPIHIVDFHAETTSEKNALFLDFKSKLSLVYGTHT Sbjct: 121 GNSIDMKGLQTNPFESLDKIIAFNEAPIHIVD

Bactericidal activity of M protein conserved region antibodies against group A streptococcal isolates from the Northern Thai population

Directory of Open Access Journals (Sweden)

Pruksachatkunakorn Chulabhorn

2006-08-01

Full Text Available Abstract Background Most group A streptococcal (GAS vaccine strategies have focused on the surface M protein, a major virulence factor of GAS. The amino-terminus of the M protein elicits antibodies, that are both opsonic and protective, but which are type specific. J14, a chimeric peptide that contains 14 amino acids from the M protein conserved C-region at the carboxy-terminus, offers the possibility of a vaccine which will elicit protective opsonic antibodies against multiple different GAS strains. In this study, we searched for J14 and J14-like sequences and the number of their repeats in the C-region of the M protein from GAS strains isolated from the Northern Thai population. Then, we examined the bactericidal activity of J14, J14.1, J14-R1 and J14-R2 antisera against multiple Thai GAS strains. Results The emm genes of GAS isolates were sequenced and grouped as 14 different J14-types. The most diversity of J14-types was found in the C1-repeat. The J14.1 type was the major sequence in the C2 and C3-repeats. We have shown that antisera raised against the M protein conserved C-repeat region peptides, J14, J14.1, J14-R1 and J14-R2, commonly found in GAS isolates from the Northern Thai population, are able to kill GAS of multiple different emm types derived from an endemic area. The mean percent of bactericidal activities for all J14 and J14-like peptide antisera against GAS isolates were more than 70%. The mean percent of bactericidal activity was highest for J14 antisera followed by J14-R2, J14.1 and J14-R1 antisera. Conclusion Our study demonstrated that antisera raised against the M protein conserved C-repeat region are able to kill multiple different strains of GAS isolated from the Northern Thai population. Therefore, the four conserved "J14" peptides have the potential to be used as GAS vaccine candidates to prevent streptococcal infections in an endemic area.

NCBI nr-aa BLAST: CBRC-CREM-01-1348 [SEVENS

Lifescience Database Archive (English)

Full Text Available CBRC-CREM-01-1348 ref|YP_056275.1| hypothetical protein PPA1574 [Propionibacterium acne...s KPA171202] gb|AAT83317.1| conserved membrane protein, UPF0118 [Propionibacterium acnes KPA171202] YP_056275.1 4e-55 35% ...

On the interconnection of stable protein complexes: inter-complex hubs and their conservation in Saccharomyces cerevisiae and Homo sapiens networks.

Science.gov (United States)

Guerra, Concettina

2015-01-01

Protein complexes are key molecular entities that perform a variety of essential cellular functions. The connectivity of proteins within a complex has been widely investigated with both experimental and computational techniques. We developed a computational approach to identify and characterise proteins that play a role in interconnecting complexes. We computed a measure of inter-complex centrality, the crossroad index, based on disjoint paths connecting proteins in distinct complexes and identified inter-complex hubs as proteins with a high value of the crossroad index. We applied the approach to a set of stable complexes in Saccharomyces cerevisiae and in Homo sapiens. Just as done for hubs, we evaluated the topological and biological properties of inter-complex hubs addressing the following questions. Do inter-complex hubs tend to be evolutionary conserved? What is the relation between crossroad index and essentiality? We found a good correlation between inter-complex hubs and both evolutionary conservation and essentiality.

Protein (Viridiplantae): 653014 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 3065:1239 ... 3066:1239 ... 3067:1239 ... 3068:1239 ... hypothetical protein VOLCADRAFT_66785 Volvox carteri f. nagariensis MRVGERDCPRVGERD...CPGVGERDCPGVGERDCPRVGERDCPGVGERDCPGVGERDCPRVGERDCPGVGERDCPRVGERDCPGVGERDCPGVGERDCPGVGERDCWPNVDSWTNLSNGRLMRVGER...DCPRVGERDCPGVGERDCPGVGERDCPRVGERDCPGVGERDCPGVGERDCPRVGERDCPGVGERDCPRVGERDCPGVGERDCPGVGERDCPGVGERDCWPNVDSWTNVCVVFRFLNLGPN

Protein (Viridiplantae): 108125 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 065:363 ... 3066:363 ... 3067:363 ... 3068:363 ... hypothetical protein VOLCADRAFT_35996, partial Volvox carteri f. nagariensis HIAYCISH...IAYCISHIAYCISHIAYCILHIAYCISHIAYCVSHIAYRILHIAYRILHIAYRILHIAYCILHIAYCILHIAYRISHIAYCISHPYRCIWHIAY

Protein (Cyanobacteria): 652402487 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026798282.1 ... 1117:5648 ... 1150:51942 1301283:73102 ... 54304:1817 54307:1346 ... hypothetical protein Plankt...othrix prolifica MNKTKLKFSTELRKLTTVQNPEALRAYCQSLKSQLVADPSNYAKGRYRLWLFHEVDFRDGTLSKGY

Protein (Cyanobacteria): 652389878 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026785726.1 ... 1117:3298 ... 1150:52043 1301283:73215 ... 54304:1908 59512:262 ... hypothetical protein Plankt...othrix rubescens MPTFFPEGKTININGEVELLAFQCQDTVVQLAAIAPGAIFPLHQHTESQIGMIFNGNLEMNLNGNKT

Protein (Cyanobacteria): 652391756 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026787603.1 ... 1117:6086 ... 1150:52096 1301283:73273 ... 54304:1956 59512:755 ... hypothetical protein Plankt...othrix rubescens MKNAMLEAADIKILEAAAAEDLARDRQFILEEDSNKTLAQQSYKAQQRDQRLVKAALIPRTGEAASP

Protein (Cyanobacteria): 652402508 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026798303.1 ... 1117:6692 ... 1150:51953 1301283:73114 ... 54304:1827 54307:1360 ... hypothetical protein Plankt...othrix prolifica MKRWKILSFQIILAALESCFLPAYSDLITNPAYINKMCQRQQDLPQIERFTVFYQQEFSSQNKTYW

Protein (Cyanobacteria): 652400769 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796565.1 ... 1117:6622 ... 1150:52114 1301283:73294 ... 54304:1972 54307:411 ... hypothetical protein Plankt...othrix prolifica MFPLKSYLISKRISSQAFLISVLAVFTVILTVTLDSVSLAMTHPDAARNQTVYGQELIAQSRIPTSDQPSPSSLSDIPTADTASLFQNNRYAVRVFRQENKAYVNIYDKENKTLTLNNE

Protein (Cyanobacteria): 653002693 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254883.1 ... 1117:2965 ... 1150:52982 1301283:74257 ... 54304:633 1160:1456 ... hypothetical protein Plankt...othrix agardhii MKTSLLILCQNRLKQKSLLQHQKTSGFTMIELLIGMIMAAVIITPILAFVVDVLQSDRKEGVKAATDQELEAATDFIKRDLSQAIYIYNKT

Protein (Cyanobacteria): 652390640 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026786488.1 ... 1117:44775 ... 1150:52433 1301283:73648 ... 54304:2259 59512:501 ... hypothetical protein Plankt...othrix rubescens MKIIQGYNPSKTISPMKIRKVKGVTIVEKYGDNLYVLPDENNNKTVPEFNKTDSFDINNWAEQATDLDGFYFINAITMTGNYLGSEWNDIILGLKFRGLATYISNH

Protein (Cyanobacteria): 652392751 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026788598.1 ... 1117:7257 ... 1150:51123 1301283:72193 ... 54304:108 59512:73 ... hypothetical protein Plankt...othrix rubescens MNSVEELARLQKRFQEAAKVIDDLSRIKQELDQLSKSYKDKLSNNSFELSQTKQEIESLSINHKEYKKYWHETFNAIHNKT

Protein (Cyanobacteria): 653003511 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027255690.1 ... 1117:21960 ... 1150:53273 1301283:74581 ... 54304:896 1160:1705 ... hypothetical protein Plankt...othrix agardhii MIPNKTQFLSELQVDSELDLELSTDPNQSIRKFVEHKQVIKFLSEQLSEIEPDAIVEALAIHQDNMNN

Protein (Cyanobacteria): 652400912 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796708.1 ... 1117:53359 ... 1150:52148 1301283:73331 ... 54304:2001 54307:507 ... hypothetical protein Plankt...othrix prolifica MKTTFSWLSSYFLLTGLAISGITFLGEVRPASACTGFWGRMDPTCDHGGITNPVHMTTQDFKICNKTENSISFTLNGSLEAPLRVGYCRTYTNVILPGNVAFDASYADGYQESSYGLDDEKNYSFKLNNQGSGIDLFAD

Protein (Cyanobacteria): 652400898 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796694.1 ... 1117:5991 ... 1150:52142 1301283:73325 ... 54304:1998 54307:498 ... hypothetical protein Plankt...othrix prolifica MLKITLTPEQEQFLQAQLKTGKYNNPQEVISKAFKLLEKENKTELLANIPASASAKKILTEKIKEFRDNLENTQNQPLNPEREKLSREVKELFDKTQSIPGIGDITEEEIAAEIEA

Protein (Cyanobacteria): 653002319 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254510.1 ... 1117:7257 ... 1150:51123 1301283:72193 ... 54304:108 1160:168 ... hypothetical protein Plankt...othrix agardhii MNSVEELARLQKRFQEAAKVIDDLSRIKQELDQLSKSYKDKLSNNSFELSQTKQEIDSLSINHKEYKKYWHETFNAIHNKTENILTQISQIENKT

Protein (Cyanobacteria): 652998182 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027250437.1 ... 1117:53495 ... 1150:52763 1301283:74014 ... 54304:436 1160:1265 ... hypothetical protein Plankt...othrix agardhii MIVMPPPPPAIVSQVPHQAIFRDDFSRGCPGYSQAENQQIGNTAANHLAGITKNKTDSLVIFFTREFT

Protein (Cyanobacteria): 653002604 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027254794.1 ... 1117:7880 ... 1150:53167 1301283:74463 ... 54304:80 1160:53 ... hypothetical protein Plankt...othrix agardhii MEFEQALEVVNNAIAPKIARTLTEVEVALLFGAWNNLTYDRIAERSGYSINYLQRDIGPKFWKFLSEALGRKVNKT

Protein (Cyanobacteria): 652401088 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796884.1 ... 1117:41752 ... 1150:52182 1301283:73369 ... 54304:2032 54307:622 ... hypothetical protein Plankt...othrix prolifica MNTNDEDQSISNIKRKLLEQINTLKCEDERMYNILAIDVWALAKTMDEFQPGFWGAFMKNREKALKRFLAESAKNKTDTDSKRPPFLR

Protein (Cyanobacteria): 652402883 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026798668.1 ... 1117:7321 ... 1150:52735 1301283:73983 ... 54304:410 54307:1082 ... hypothetical protein Plankt...othrix prolifica MHGGFYCTDETTQATYIQLHTSQGLEVLFFDSFIDSHFISFLEREHTDVKFARVDAELDDNLIAKDNSPEIVDPKTNKT

Protein (Cyanobacteria): 653003418 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027255601.1 ... 1117:6743 ... 1150:53326 1301283:74640 ... 54304:943 1160:195 ... hypothetical protein Plankt...othrix agardhii MVQILNKTLSLEDFLNLPETKPANEYINGQIIQKPMPQGKHSKLQGKLVTVINNMAEEQAIALALPELRC

Protein (Cyanobacteria): 652400421 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796217.1 ... 1117:3298 ... 1150:52043 1301283:73215 ... 54304:1908 54307:20 ... hypothetical protein Plankt...othrix prolifica MPTFFPEGKTININGEVELLAFQCQDTVVQLAAIAPGAIFPLHQHTESQIGMIFNGNLEMNLNGNKTV

Protein (Cyanobacteria): 652400810 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026796606.1 ... 1117:6743 ... 1150:53326 1301283:74640 ... 54304:943 54307:170 ... hypothetical protein Plankt...othrix prolifica MVQILNKTLSLEDFLNLPETKPANEYINGQIIQKPMPQGKHSKLQGKLVTVINNMAEEQAIALALPEL

Protein (Cyanobacteria): 652391725 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026787573.1 ... 1117:6169 ... 1150:52274 1301283:73471 ... 54304:2115 59512:749 ... hypothetical protein Plankt...othrix rubescens MGNVSFASENKTLAQSSNISGWVDSFGFASTKQGAGQAGIDQGEKLGILFDGNFDNVINSLKANQLK

Protein (Cyanobacteria): 652390481 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_026786329.1 ... 1117:7618 ... 1150:52216 1301283:73407 ... 54304:2063 59512:458 ... hypothetical protein Plankt...othrix rubescens MIPFQDSRLLLRALTYRSYMFENPNKTQGDNEQLEFLGDSVLQFLAGDYVYEKYFGEQEGQLTQKRE

Protein (Viridiplantae): 688657 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 65:2039 ... 3066:2039 ... 3067:2039 ... 3068:2039 ... hypothetical protein VOLCADRAFT_35179, partial Volvox carteri f. nagariensis EDRG...PRTEDRGPRTEDRGPRTEDRGPRTEDRGPRTEDRGPRTEDRGPRTEDRGPRTEDRGPRTEDRG

Hypothetical Scenario Generator for Fault-Tolerant Diagnosis

Science.gov (United States)

James, Mark

2007-01-01

The Hypothetical Scenario Generator for Fault-tolerant Diagnostics (HSG) is an algorithm being developed in conjunction with other components of artificial- intelligence systems for automated diagnosis and prognosis of faults in spacecraft, aircraft, and other complex engineering systems. By incorporating prognostic capabilities along with advanced diagnostic capabilities, these developments hold promise to increase the safety and affordability of the affected engineering systems by making it possible to obtain timely and accurate information on the statuses of the systems and predicting impending failures well in advance. The HSG is a specific instance of a hypothetical- scenario generator that implements an innovative approach for performing diagnostic reasoning when data are missing. The special purpose served by the HSG is to (1) look for all possible ways in which the present state of the engineering system can be mapped with respect to a given model and (2) generate a prioritized set of future possible states and the scenarios of which they are parts.

Mutation of a Broadly Conserved Operon (RL3499-RL3502) from Rhizobium leguminosarum Biovar viciae Causes Defects in Cell Morphology and Envelope Integrity▿†

Science.gov (United States)

Vanderlinde, Elizabeth M.; Magnus, Samantha A.; Tambalo, Dinah D.; Koval, Susan F.; Yost, Christopher K.

2011-01-01

The bacterial cell envelope is of critical importance to the function and survival of the cell; it acts as a barrier against harmful toxins while allowing the flow of nutrients into the cell. It also serves as a point of physical contact between a bacterial cell and its host. Hence, the cell envelope of Rhizobium leguminosarum is critical to cell survival under both free-living and symbiotic conditions. Transposon mutagenesis of R. leguminosarum strain 3841 followed by a screen to isolate mutants with defective cell envelopes led to the identification of a novel conserved operon (RL3499-RL3502) consisting of a putative moxR-like AAA+ ATPase, a hypothetical protein with a domain of unknown function (designated domain of unknown function 58), and two hypothetical transmembrane proteins. Mutation of genes within this operon resulted in increased sensitivity to membrane-disruptive agents such as detergents, hydrophobic antibiotics, and alkaline pH. On minimal media, the mutants retain their rod shape but are roughly 3 times larger than the wild type. On media containing glycine or peptides such as yeast extract, the mutants form large, distorted spheres and are incapable of sustained growth under these culture conditions. Expression of the operon is maximal during the stationary phase of growth and is reduced in a chvG mutant, indicating a role for this sensor kinase in regulation of the operon. Our findings provide the first functional insight into these genes of unknown function, suggesting a possible role in cell envelope development in Rhizobium leguminosarum. Given the broad conservation of these genes among the Alphaproteobacteria, the results of this study may also provide insight into the physiological role of these genes in other Alphaproteobacteria, including the animal pathogen Brucella. PMID:21357485

Conserved CPEs in the p53 3' untranslated region influence mRNA stability and protein synthesis

DEFF Research Database (Denmark)

Rosenstierne, Maiken W; Vinther, Jeppe; Mittler, Gerhard

2008-01-01

CaT skin and MCF-7 breast cancer cell lines were established. Quantitative PCR and an enzymatic assay were used to quantify the reporter mRNA and protein levels, respectively. Proteins binding to the CPEs were identified by RNA-immunoprecipitation (IP) and quantitative mass spectroscopy. RESULTS: The wild...... irradiation. Several proteins (including GAPDH, heterogeneous nuclear ribonucleoprotein (hnRNP) D and A/B) were identified from the MCF-7 cytoplasmic extracts that bound specifically to the CPEs. CONCLUSION: Two conserved CPEs in the p53 3'UTR regulate stability and translation of a reporter mRNA in non...

To what extent do potential conservation donors value community-aspects of conservation projects in low income countries?

Science.gov (United States)

Young, Richard P.; Gibbons, James M.; Jones, Julia P. G.

2018-01-01

There is a major gap in funding required for conservation, especially in low income countries. Given the significant contribution of taxpayers in industrialized countries to funding conservation overseas, and donations from membership organisation, understanding the preferences of ordinary people in a high income country for different attributes of conservation projects is valuable for future marketing of conservation. We conducted a discrete choice experiment with visitors to a UK zoo, while simultaneously conducting a revealed preference study through a real donation campaign on the same sample. Respondents showed the highest willingness to pay for projects that have local community involvement in management (95% confidence interval £9.82 to £15.83), and for improvement in threatened species populations (£2.97 - £13.87). Both of these were significantly larger than the willingness to pay for projects involving provision of alternative livelihoods, or improving the condition of conservation sites. Results of the simultaneous donation campaign showed that respondents were very willing to donate the suggested £1 or above donation (88% made a donation, n = 1798); there was no effect of which of the two campaigns they were exposed to (threatened species management or community involvement in management). The small number of people who did not make a donation had a higher stated willingness to pay within the choice experiment, which may suggest hypothetical bias. Conservationists increasingly argue that conservation should include local communities in management (for both pragmatic and moral reasons). It is heartening that potential conservation donors seem to agree. PMID:29451923

Protein (Cyanobacteria): 652997312 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_027249778.1 ... 1117:3511 ... 1150:51681 1301283:72812 ... 54304:1582 1160:909 ... hypothetical protein Plankt...othrix agardhii MATSLKKLLIGTSVAVGISAVGITPALAGSLTNATIGGTASTDYLIYGKEGNKTVVIPNSVANLQSVLD...ATKWFGETLSKYGMTSSQTLFSNFLLAGGFQRFSDPNISYVNQDNKTGKITIGLAGHYDAASLLGLPSNPNNPIPNPNNPI

Protein (Cyanobacteria): 504985318 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015172420.1 ... 1117:22013 ... 1150:56822 1301283:78524 ... 63132:1744 1173025:1864 ... ... hypothetical protein Geitlerinema sp. PCC 7407 MTTANFSHKDVAEITEAEVAALANRLEDDDYSSVFEGLEDWHLLRAIAFQRPELVEPYIHLLDLEAYDEA

Protein (Cyanobacteria): 504985975 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015173077.1 ... 1117:22894 ... 1150:58400 1301283:80278 ... 63132:3164 1173025:2236 ... ... hypothetical protein Geitlerinema sp. PCC 7407 MAKPWQKVLLAVALVGGVWGVSPAIAGTCASNCGPKPLQFIPGQQVKLQIINRTASIIEIQKVYGTDPVALRPGQEIT

Protein (Cyanobacteria): 504984488 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015171590.1 ... 1117:23095 ... 1150:57940 1301283:79766 ... 63132:2750 1173025:1386 ... ... hypothetical protein Geitlerinema sp. PCC 7407 MTQSSDSSTSQAKHQRSFAEWVSFAIAAAIIASVLGLVAYTWATGDTQPPVLETEITPEV

Cross-serotype immunity induced by immunization with a conserved rhinovirus capsid protein.

Directory of Open Access Journals (Sweden)

Nicholas Glanville

Full Text Available Human rhinovirus (RV infections are the principle cause of common colds and precipitate asthma and COPD exacerbations. There is currently no RV vaccine, largely due to the existence of ∼150 strains. We aimed to define highly conserved areas of the RV proteome and test their usefulness as candidate antigens for a broadly cross-reactive vaccine, using a mouse infection model. Regions of the VP0 (VP4+VP2 capsid protein were identified as having high homology across RVs. Immunization with a recombinant VP0 combined with a Th1 promoting adjuvant induced systemic, antigen specific, cross-serotype, cellular and humoral immune responses. Similar cross-reactive responses were observed in the lungs of immunized mice after infection with heterologous RV strains. Immunization enhanced the generation of heterosubtypic neutralizing antibodies and lung memory T cells, and caused more rapid virus clearance. Conserved domains of the RV capsid therefore induce cross-reactive immune responses and represent candidates for a subunit RV vaccine.

Conservation and divergence of C-terminal domain structure in the retinoblastoma protein family

Energy Technology Data Exchange (ETDEWEB)

Liban, Tyler J.; Medina, Edgar M.; Tripathi, Sarvind; Sengupta, Satyaki; Henry, R. William; Buchler, Nicolas E.; Rubin, Seth M. (UCSC); (Duke); (MSU)

2017-04-24

The retinoblastoma protein (Rb) and the homologous pocket proteins p107 and p130 negatively regulate cell proliferation by binding and inhibiting members of the E2F transcription factor family. The structural features that distinguish Rb from other pocket proteins have been unclear but are critical for understanding their functional diversity and determining why Rb has unique tumor suppressor activities. We describe here important differences in how the Rb and p107 C-terminal domains (CTDs) associate with the coiled-coil and marked-box domains (CMs) of E2Fs. We find that although CTD–CM binding is conserved across protein families, Rb and p107 CTDs show clear preferences for different E2Fs. A crystal structure of the p107 CTD bound to E2F5 and its dimer partner DP1 reveals the molecular basis for pocket protein–E2F binding specificity and how cyclin-dependent kinases differentially regulate pocket proteins through CTD phosphorylation. Our structural and biochemical data together with phylogenetic analyses of Rb and E2F proteins support the conclusion that Rb evolved specific structural motifs that confer its unique capacity to bind with high affinity those E2Fs that are the most potent activators of the cell cycle.

Protein (Cyanobacteria): 504983711 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170813.1 ... 1117:4710 ... 1150:56664 1301283:78348 ... 63132:1601 1173025:861 ... hypothetical protein Geit...lerinema sp. PCC 7407 MGIKRQIEITPLHCIHPGKGLEICPLDQAATATHTNAEQPTWGHETTLVTLAPGTIEDLFVH

Protein (Cyanobacteria): 504983895 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170997.1 ... 1117:21655 ... 1150:57681 1301283:79478 ... 63132:2517 1173025:996 ... hypothetical protein Geit...lerinema sp. PCC 7407 MFSSDLPEPDLLKTVLLPLLEDFQYWFGRSRSLLESEEITFLSQDQQADLLARVCQAQQEVMAAQALFNATDGQVGVETAALMPWHQLVTECWQVGMRLRTEKSRS

Protein (Cyanobacteria): 504983646 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170748.1 ... 1117:22225 ... 1150:58729 1301283:80642 ... 63132:3460 1173025:812 ... hypothetical protein Geit...lerinema sp. PCC 7407 MASTYSFDIVSDFDRQELVNAIDQTTREIGTRYDLKDTKTTLELGEDEITVNTDSEFTLTA

Protein (Cyanobacteria): 504984487 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015171589.1 ... 1117:22124 ... 1150:57295 1301283:79049 ... 63132:217 1173025:1268 ... hypothetical protein Geit...lerinema sp. PCC 7407 MAQLQRLDIVGDDGQTIEIFVEEKDAPVLATSPNRDGRPSMGAGSPSVKMQQMQQVIRGYATYALNAFKDFSAAEVEEITLMFGVKLSASAGIPYIANGTTDSNLEVQVKCRFPAKDG

Protein (Cyanobacteria): 504985936 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015173038.1 ... 1117:4673 ... 1150:58391 1301283:80267 ... 63132:3156 1173025:2219 ... hypothetical protein Geit...lerinema sp. PCC 7407 MNKLLTLTVLGCVLSAAPAAIAAEWREITRNDVGDRFMIDTSSLDRRGSSVWFWEYRDFPQ

Protein (Cyanobacteria): 504983317 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170419.1 ... 1117:23009 ... 1150:58655 1301283:80560 ... 63132:3394 1173025:527 ... hypothetical protein Geit...lerinema sp. PCC 7407 MAASDDFKQQIRDGNLSDALKLALSEAIHLEITTWVSSPEQGDRAAMPGSRMRTRINVVDG

Protein (Cyanobacteria): 504983362 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available WP_015170464.1 ... 1117:946 ... 1150:58664 1301283:80570 ... 63132:3401 1173025:562 ... hypothetical protein Geit...lerinema sp. PCC 7407 MTGFGAGESGQAPERSGFEPELGGFLRDAAQRSGLEPELGGVLRQRGVYVDEITCIGCKHCAH

Using respondent uncertainty to mitigate hypothetical bias in a stated choice experiment

Science.gov (United States)

Richard C. Ready; Patricia A. Champ; Jennifer L. Lawton

2010-01-01

In a choice experiment study, willingness to pay for a public good estimated from hypothetical choices was three times as large as willingness to pay estimated from choices requiring actual payment. This hypothetical bias was related to the stated level of certainty of respondents. We develop protocols to measure respondent certainty in the context of a choice...

Can a Repeated Opt-Out Reminder remove hypothetical bias in discrete choice experiments?

DEFF Research Database (Denmark)

Alemu, Mohammed Hussen; Olsen, Søren Bøye

hypothetical bias in stated DCE. The data originates from a field experiment concerning consumer preferences for a novel food product made from cricket flour. Utilizing a between-subject design with three treatments, we find significantly higher marginal willingness to pay values in hypothetical than...

Protein (Viridiplantae): 888289 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available 0727 3803:10727 ... 3814:10727 ... 163735:2506 ... 3883:1736 ... 3885:1736 ... hypothetical protein PHAVU_009G116600g Phaseolus vulgaris MKKNRMMIM...ICSVGVVWMLLVGGSYGEQCGRQAGGALCPGGNCCSQFGWCGSTTDYCGKDCQSQC

Protein (Cyanobacteria): 118891 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007110526.1 1117:2337 1150:9795 63132:2205 1173025:2205 hypothetical protein GEI7407_3004 Geit...lerinema sp. PCC 7407 MNKLLTLTVLGCVLSAAPAAIAAEWREITRNDVGDRFMIDTSSLDRRGSSVWFWEYRDFPQPNNAFLEETVD

Protein (Cyanobacteria): 444358 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109074.1 1117:25729 1150:9238 63132:1257 1173025:1257 hypothetical protein GEI7407_1530 Geit...lerinema sp. PCC 7407 MAQLQRLDIVGDDGQTIEIFVEEKDAPVLATSPNRDGRPSMGAGSPSVKMQQMQQVIRGYATYALNAFKDFSAAEVEEITLMFGVKLSASAGIPYIANGTTDSNLEVQVKCRFPAKDG ...

Protein (Cyanobacteria): 462887 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109749.1 1117:35991 1150:9729 63132:1766 1173025:1766 hypothetical protein GEI7407_2218 Geit...lerinema sp. PCC 7407 MAEITDPEGEHRRIHWAAEQTDVATLINAYRGWYHWADAKEWASGAAFLRRLSQVGAGSPEAIALFIEQMNFHAQSRTKSGKYIYSAAKDALKALAEQGDPSAIAAWEEMQSSSEKP ...

Protein (Cyanobacteria): 334532 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109075.1 1117:10916 1150:5016 63132:1375 1173025:1375 hypothetical protein GEI7407_1531 Geit...lerinema sp. PCC 7407 MTQSSDSSTSQAKHQRSFAEWVSFAIAAAIIASVLGLVAYTWATGDTQPPVLETEITPEVRQAGSQFYIPFSVTNTGGGTAESVQVIAELRVNGEVIETGEQQFDFLSGGEKAEGAFVFQRDPAQGDLSLRVASYSLP ...

Protein (Cyanobacteria): 134448 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007108952.1 1117:2626 1150:6080 63132:1307 1173025:1307 hypothetical protein GEI7407_1406 Geit...lerinema sp. PCC 7407 MFQPSTVLPSSDRPVSHEIRYERSFLLDLKNLEPAVYQRVFQFVFQDKLTLTQIQEMPGFRQIYASPIFYRFELSDCLIGVEITGQIVKFLRVIPKPDI ...

Protein (Cyanobacteria): 345257 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007108297.1 1117:12245 1150:7393 63132:850 1173025:850 hypothetical protein GEI7407_0747 Geit...lerinema sp. PCC 7407 MGIKRQIEITPLHCIHPGKGLEICPLDQAATATHTNAEQPTWGHETTLVTLAPGTIEDLFVHHFQTDQLLVVQ

Protein (Cyanobacteria): 40520 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007107948.1 1117:753 1150:5622 63132:560 1173025:560 hypothetical protein GEI7407_0395 Geit...lerinema sp. PCC 7407 MTGFGAGESGQAPERSGFEPELGGFLRDAAQRSGLEPELGGVLRQRGVYVDEITCIGCKHCAHVARNTFYIEPDY

Protein (Cyanobacteria): 4022 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007110171.1 1117:85 1150:6948 63132:2007 1173025:2007 hypothetical protein GEI7407_2646 Geit...lerinema sp. PCC 7407 MDPLFWLGLSILLVAVSLTALLFVAIPAFQELGRAARSAEKLFDTLNRELPPTLESIRLTGLEITELTEDVSDG

Protein (Cyanobacteria): 207028 [PGDBj - Ortholog DB

Lifescience Database Archive (English)

Full Text Available YP_007109341.1 1117:3927 1150:1735 63132:1535 1173025:1535 hypothetical protein GEI7407_1805 Geit...lerinema sp. PCC 7407 MKIETRRFLLRDFIPADDAAFLAYHVEPRFAEFCSPAEITPSFNRNLLQQFNQWANEYPRHNYQLAIVSRRD

Gα and regulator of G-protein signaling (RGS) protein pairs maintain functional compatibility and conserved interaction interfaces throughout evolution despite frequent loss of RGS proteins in plants.

Science.gov (United States)

Hackenberg, Dieter; McKain, Michael R; Lee, Soon Goo; Roy Choudhury, Swarup; McCann, Tyler; Schreier, Spencer; Harkess, Alex; Pires, J Chris; Wong, Gane Ka-Shu; Jez, Joseph M; Kellogg, Elizabeth A; Pandey, Sona

2017-10-01

Signaling pathways regulated by heterotrimeric G-proteins exist in all eukaryotes. The regulator of G-protein signaling (RGS) proteins are key interactors and critical modulators of the Gα protein of the heterotrimer. However, while G-proteins are widespread in plants, RGS proteins have been reported to be missing from the entire monocot lineage, with two exceptions. A single amino acid substitution-based adaptive coevolution of the Gα:RGS proteins was proposed to enable the loss of RGS in monocots. We used a combination of evolutionary and biochemical analyses and homology modeling of the Gα and RGS proteins to address their expansion and its potential effects on the G-protein cycle in plants. Our results show that RGS proteins are widely distributed in the monocot lineage, despite their frequent loss. There is no support for the adaptive coevolution of the Gα:RGS protein pair based on single amino acid substitutions. RGS proteins interact with, and affect the activity of, Gα proteins from species with or without endogenous RGS. This cross-functional compatibility expands between the metazoan and plant kingdoms, illustrating striking conservation of their interaction interface. We propose that additional proteins or alternative mechanisms may exist which compensate for the loss of RGS in certain plant species. © 2016 The Authors. New Phytologist © 2016 New Phytologist Trust.

Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs.

Science.gov (United States)

Kazakov, Alexei S; Sokolov, Andrei S; Vologzhannikova, Alisa A; Permyakova, Maria E; Khorn, Polina A; Ismailov, Ramis G; Denessiouk, Konstantin A; Denesyuk, Alexander I; Rastrygina, Victoria A; Baksheeva, Viktoriia E; Zernii, Evgeni Yu; Zinchenko, Dmitry V; Glazatov, Vladimir V; Uversky, Vladimir N; Mirzabekov, Tajib A; Permyakov, Eugene A; Permyakov, Sergei E

2017-01-01

Interleukin-11 (IL-11) is a hematopoietic cytokine engaged in numerous biological processes and validated as a target for treatment of various cancers. IL-11 contains intrinsically disordered regions that might recognize multiple targets. Recently we found that aside from IL-11RA and gp130 receptors, IL-11 interacts with calcium sensor protein S100P. Strict calcium dependence of this interaction suggests a possibility of IL-11 interaction with other calcium sensor proteins. Here we probed specificity of IL-11 to calcium-binding proteins of various types: calcium sensors of the EF-hand family (calmodulin, S100B and neuronal calcium sensors: recoverin, NCS-1, GCAP-1, GCAP-2), calcium buffers of the EF-hand family (S100G, oncomodulin), and a non-EF-hand calcium buffer (α-lactalbumin). A specific subset of the calcium sensor proteins (calmodulin, S100B, NCS-1, GCAP-1/2) exhibits metal-dependent binding of IL-11 with dissociation constants of 1-19 μM. These proteins share several amino acid residues belonging to conservative structural motifs of the EF-hand proteins, 'black' and 'gray' clusters. Replacements of the respective S100P residues by alanine drastically decrease its affinity to IL-11, suggesting their involvement into the association process. Secondary structure and accessibility of the hinge region of the EF-hand proteins studied are predicted to control specificity and selectivity of their binding to IL-11. The IL-11 interaction with the EF-hand proteins is expected to occur under numerous pathological conditions, accompanied by disintegration of plasma membrane and efflux of cellular components into the extracellular milieu.

The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP

DEFF Research Database (Denmark)

Kragelund, Birthe Brandt; Osmark, Peter; Neergaard, Thomas B.

1999-01-01

The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24...... probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding...... step and that a sequential framework model can describe the protein folding reaction....

Transcriptome analysis of reproductive tissue and intrauterine developmental stages of the tsetse fly (Glossina morsitans morsitans

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Wu Yineng

2010-03-01

Full Text Available Abstract Background Tsetse flies, vectors of African trypanosomes, undergo viviparous reproduction (the deposition of live offspring. This reproductive strategy results in a large maternal investment and the deposition of a small number of progeny during a female's lifespan. The reproductive biology of tsetse has been studied on a physiological level; however the molecular analysis of tsetse reproduction requires deeper investigation. To build a foundation from which to base molecular studies of tsetse reproduction, a cDNA library was generated from female tsetse (Glossina morsitans morsitans reproductive tissues and the intrauterine developmental stages. 3438 expressed sequence tags were sequenced and analyzed. Results Analysis of a nonredundant catalogue of 1391 contigs resulted in 520 predicted proteins. 475 of these proteins were full length. We predict that 412 of these represent cytoplasmic proteins while 57 are secreted. Comparison of these proteins with other tissue specific tsetse cDNA libraries (salivary gland, fat body/milk gland, and midgut identified 51 that are unique to the reproductive/immature cDNA library. 11 unique proteins were homologus to uncharacterized putative proteins within the NR database suggesting the identification of novel genes associated with reproductive functions in other insects (hypothetical conserved. The analysis also yielded seven putative proteins without significant homology to sequences present in the public database (unknown genes. These proteins may represent unique functions associated with tsetse's viviparous reproductive cycle. RT-PCR analysis of hypothetical conserved and unknown contigs was performed to determine basic tissue and stage specificity of the expression of these genes. Conclusion This paper identifies 51 putative proteins specific to a tsetse reproductive/immature EST library. 11 of these proteins correspond to hypothetical conserved genes and 7 proteins are tsetse specific.

Conservation of a proteinase cleavage site between an insect retrovirus (gypsy) Env protein and a baculovirus envelope fusion protein

International Nuclear Information System (INIS)

Pearson, Margot N.; Rohrmann, George F.

2004-01-01

The predicted Env protein of insect retroviruses (errantiviruses) is related to the envelope fusion protein of a major division of the Baculoviridae. The highest degree of homology is found in a region that contains a furin cleavage site in the baculovirus proteins and an adjacent sequence that has the properties of a fusion peptide. In this investigation, the homologous region in the Env protein of the gypsy retrovirus of Drosophila melanogaster (DmegypV) was investigated. Alteration of the predicted DmegypV Env proteinase cleavage site from RIAR to AIAR significantly reduced cleavage of Env in both Spodoptera frugiperda (Sf-9) and D. melanogaster (S2) cell lines. When the predicted DmegypV Env cleavage site RIAR was substituted for the cleavage sequence RRKR in the Lymantria dispar nucleopolyhedrovirus fusion protein (LD130) sequence, cleavage of the hybrid LD130 molecules still occurred, although at a reduced level. The conserved 21-amino acid sequence just downstream of the cleavage site, which is thought to be the fusion peptide in LD130, was also characterized. When this sequence from DmegypV Env was substituted for the homologous sequence in LD130, cleavage still occurred, but no fusion was observed in either cell type. In addition, although a DmegypV-Env-green fluorescent protein construct localized to cell membranes, no cell fusion was observed

Relative Stabilities of Conserved and Non-Conserved Structures in the OB-Fold Superfamily

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Andrei T. Alexandrescu

2009-05-01

Full Text Available The OB-fold is a diverse structure superfamily based on a β-barrel motif that is often supplemented with additional non-conserved secondary structures. Previous deletion mutagenesis and NMR hydrogen exchange studies of three OB-fold proteins showed that the structural stabilities of sites within the conserved β-barrels were larger than sites in non-conserved segments. In this work we examined a database of 80 representative domain structures currently classified as OB-folds, to establish the basis of this effect. Residue-specific values were obtained for the number of Cα-Cα distance contacts, sequence hydrophobicities, crystallographic B-factors, and theoretical B-factors calculated from a Gaussian Network Model. All four parameters point to a larger average flexibility for the non-conserved structures compared to the conserved β-barrels. The theoretical B-factors and contact densities show the highest sensitivity.Our results suggest a model of protein structure evolution in which novel structural features develop at the periphery of conserved motifs. Core residues are more resistant to structural changes during evolution since their substitution would disrupt a larger number of interactions. Similar factors are likely to account for the differences in stability to unfolding between conserved and non-conserved structures.

Conserved amino acids within the N-terminus of the West Nile virus NS4A protein contribute to virus replication, protein stability and membrane proliferation

International Nuclear Information System (INIS)

Ambrose, R.L.; Mackenzie, J.M.

2015-01-01

The West Nile virus strain Kunjin virus (WNV KUN ) NS4A protein is a multifunctional protein involved in many aspects of the virus life-cycle and is a major component of the WNV KUN replication complex (RC). Previously we identified a conserved region in the C-terminus of NS4A regulating proteolytic processing and RC assembly, and now investigate key conserved residues in the N-terminus of NS4A and their contribution to WNV KUN replication. Mutation of P13 completely ablated replication, whereas, mutation of P48 and D49, near the first transmembrane helix, and G66 within the helix, showed variable defects in replication, virion secretion and membrane proliferation. Intriguingly, the P48 and G66 NS4A mutants resulted in specific proteasome depletion of NS4A that could in part be rescued with a proteasome inhibitor. Our results suggest that the N-terminus of NS4A contributes to correct folding and stability, essential for facilitating the essential roles of NS4A during replication. - Highlights: • Mutation of Proline13 of the WNV NS4A protein is lethal to replication. • 1st TMB helix of NS4A contributes to protein stability and membrane remodelling. • Unstable mutants of NS4A can be rescued with a proteasome inhibitor. • This study (and of others) contributes to a functional mapping of the NS4A protein

Processing counterfactual and hypothetical conditionals: an fMRI investigation.

Science.gov (United States)

Kulakova, Eugenia; Aichhorn, Markus; Schurz, Matthias; Kronbichler, Martin; Perner, Josef

2013-05-15

Counterfactual thinking is ubiquitous in everyday life and an important aspect of cognition and emotion. Although counterfactual thought has been argued to differ from processing factual or hypothetical information, imaging data which elucidate these differences on a neural level are still scarce. We investigated the neural correlates of processing counterfactual sentences under visual and aural presentation. We compared conditionals in subjunctive mood which explicitly contradicted previously presented facts (i.e. counterfactuals) to conditionals framed in indicative mood which did not contradict factual world knowledge and thus conveyed a hypothetical supposition. Our results show activation in right occipital cortex (cuneus) and right basal ganglia (caudate nucleus) during counterfactual sentence processing. Importantly the occipital activation is not only present under visual presentation but also with purely auditory stimulus presentation, precluding a visual processing artifact. Thus our results can be interpreted as reflecting the fact that counterfactual conditionals pragmatically imply the relevance of keeping in mind both factual and supposed information whereas the hypothetical conditionals imply that real world information is irrelevant for processing the conditional and can be omitted. The need to sustain representations of factual and suppositional events during counterfactual sentence processing requires increased mental imagery and integration efforts. Our findings are compatible with predictions based on mental model theory. Copyright © 2013 Elsevier Inc. All rights reserved.

SURF'S UP! – Protein classification by surface comparisons

Indian Academy of Sciences (India)

2006-12-12

Dec 12, 2006 ... Large-scale genome sequencing and structural genomics projects generate numerous sequences and structures for 'hypothetical' proteins without functional characterizations. Detection of homology to experimentally characterized proteins can provide functional clues, but the accuracy of homology-based ...

Domain architecture conservation in orthologs

Science.gov (United States)

2011-01-01

Background As orthologous proteins are expected to retain function more often than other homologs, they are often used for functional annotation transfer between species. However, ortholog identification methods do not take into account changes in domain architecture, which are likely to modify a protein's function. By domain architecture we refer to the sequential arrangement of domains along a protein sequence. To assess the level of domain architecture conservation among orthologs, we carried out a large-scale study of such events between human and 40 other species spanning the entire evolutionary range. We designed a score to measure domain architecture similarity and used it to analyze differences in domain architecture conservation between orthologs and paralogs relative to the conservation of primary sequence. We also statistically characterized the extents of different types of domain swapping events across pairs of orthologs and paralogs. Results The analysis shows that orthologs exhibit greater domain architecture conservation than paralogous homologs, even when differences in average sequence divergence are compensated for, for homologs that have diverged beyond a certain threshold. We interpret this as an indication of a stronger selective pressure on orthologs than paralogs to retain the domain architecture required for the proteins to perform a specific function. In general, orthologs as well as the closest paralogous homologs have very similar domain architectures, even at large evolutionary separation. The most common domain architecture changes observed in both ortholog and paralog pairs involved insertion/deletion of new domains, while domain shuffling and segment duplication/deletion were very infrequent. Conclusions On the whole, our results support the hypothesis that function conservation between orthologs demands higher domain architecture conservation than other types of homologs, relative to primary sequence conservation. This supports the

Cytoplasmic protein binding to highly conserved sequences in the 3' untranslated region of mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells

International Nuclear Information System (INIS)

Kwon, Y.K.; Hecht, N.B.

1991-01-01

The expression of the protamines, the predominant nuclear proteins of mammalian spermatozoa, is regulated translationally during male germ-cell development. The 3' untranslated region (UTR) of protamine 1 mRNA has been reported to control its time of translation. To understand the mechanisms controlling translation of the protamine mRNAs, we have sought to identify cis elements of the 3' UTR of protamine 2 mRNA that are recognized by cytoplasmic factors. From gel retardation assays, two sequence elements are shown to form specific RNA-protein complexes. Protein binding sites of the two complexes were determined by RNase T1 mapping, by blocking the putative binding sites with antisense oligonucleotides, and by competition assays. The sequences of these elements, located between nucleotides + 537 and + 572 in protamine 2 mRNA, are highly conserved among postmeiotic translationally regulated nuclear proteins of the mammalian testis. Two closely linked protein binding sites were detected. UV-crosslinking studies revealed that a protein of about 18 kDa binds to one of the conserved sequences. These data demonstrate specific protein binding to a highly conserved 3' UTR of translationally regulated testicular mRNA

Interferon-γ and proliferation responses to Salmonella enterica Serotype Typhi proteins in patients with S. Typhi Bacteremia in Dhaka, Bangladesh.

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Alaullah Sheikh

2011-06-01

Full Text Available Salmonella enterica serotype Typhi is a human-restricted intracellular pathogen and the cause of typhoid fever. Cellular immune responses are required to control and clear Salmonella infection. Despite this, there are limited data on cellular immune responses in humans infected with wild type S. Typhi.For this work, we used an automated approach to purify a subset of S. Typhi proteins identified in previous antibody-based immuno-affinity screens and antigens known to be expressed in vivo, including StaF-putative fimbrial protein-STY0202, StbB-fimbrial chaperone-STY0372, CsgF-involved in curli production-STY1177, CsgD- putative regulatory protein-STY1179, OppA-periplasmic oligopeptide binding protein precursor-STY1304, PagC-outer membrane invasion protein-STY1878, and conserved hypothetical protein-STY2195; we also generated and analyzed a crude membrane preparation of S. Typhi (MP. In comparison to samples collected from uninfected Bangladeshi and North American participants, we detected significant interferon-γ responses in PBMCs stimulated with MP, StaF, StbB, CsgF, CsgD, OppA, STY2195, and PagC in patients bacteremic with S. Typhi in Bangladesh. The majority of interferon-γ expressing T cells were CD4 cells, although CD8 responses also occurred. We also assessed cellular proliferation responses in bacteremic patients, and confirmed increased responses in infected individuals to MP, StaF, STY2195, and PagC in convalescent compared to acute phase samples and compared to controls. StaF is a fimbrial protein homologous to E. coli YadK, and contains a Pfam motif thought to be involved in cellular adhesion. PagC is expressed in vivo under the control of the virulence-associated PhoP-regulon required for intra-macrophage survival of Salmonella. STY2195 is a conserved hypothetical protein of unknown function.This is the first analysis of cellular immune responses to purified S. Typhi antigens in patients with typhoid fever. These results indicate

Macrolide Resistance Mediated by a Bifidobacterium breve Membrane Protein

OpenAIRE

Margolles, Abelardo; Moreno, José Antonio; van Sinderen, Douwe; de los Reyes-Gavilán, Clara G.

2005-01-01

A gene coding for a hypothetical membrane protein from Bifidobacterium breve was expressed in Lactococcus lactis. Immunoblotting demonstrated that this protein is located in the membrane. Phenotypical changes in sensitivity towards 21 antibiotics were determined. The membrane protein-expressing cells showed higher levels of resistance to several macrolides.

Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins.

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David Karlin

Full Text Available Paramyxovirinae are a large group of viruses that includes measles virus and parainfluenza viruses. The viral Phosphoprotein (P plays a central role in viral replication. It is composed of a highly variable, disordered N-terminus and a conserved C-terminus. A second viral protein alternatively expressed, the V protein, also contains the N-terminus of P, fused to a zinc finger. We suspected that, despite their high variability, the N-termini of P/V might all be homologous; however, using standard approaches, we could previously identify sequence conservation only in some Paramyxovirinae. We now compared the N-termini using sensitive sequence similarity search programs, able to detect residual similarities unnoticeable by conventional approaches. We discovered that all Paramyxovirinae share a short sequence motif in their first 40 amino acids, which we called soyuz1. Despite its short length (11-16aa, several arguments allow us to conclude that soyuz1 probably evolved by homologous descent, unlike linear motifs. Conservation across such evolutionary distances suggests that soyuz1 plays a crucial role and experimental data suggest that it binds the viral nucleoprotein to prevent its illegitimate self-assembly. In some Paramyxovirinae, the N-terminus of P/V contains a second motif, soyuz2, which might play a role in blocking interferon signaling. Finally, we discovered that the P of related Mononegavirales contain similarly overlooked motifs in their N-termini, and that their C-termini share a previously unnoticed structural similarity suggesting a common origin. Our results suggest several testable hypotheses regarding the replication of Mononegavirales and suggest that disordered regions with little overall sequence similarity, common in viral and eukaryotic proteins, might contain currently overlooked motifs (intermediate in length between linear motifs and disordered domains that could be detected simply by comparing orthologous proteins.

A highly conserved Poc1 protein characterized in embryos of the hydrozoan Clytia hemisphaerica: localization and functional studies.

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Cécile Fourrage

Full Text Available Poc1 (Protein of Centriole 1 proteins are highly conserved WD40 domain-containing centriole components, well characterized in the alga Chlamydomonas, the ciliated protazoan Tetrahymena, the insect Drosophila and in vertebrate cells including Xenopus and zebrafish embryos. Functions and localizations related to the centriole and ciliary axoneme have been demonstrated for Poc1 in a range of species. The vertebrate Poc1 protein has also been reported to show an additional association with mitochondria, including enrichment in the specialized "germ plasm" region of Xenopus oocytes. We have identified and characterized a highly conserved Poc1 protein in the cnidarian Clytia hemisphaerica. Clytia Poc1 mRNA was found to be strongly expressed in eggs and early embryos, showing a punctate perinuclear localization in young oocytes. Fluorescence-tagged Poc1 proteins expressed in developing embryos showed strong localization to centrioles, including basal bodies. Anti-human Poc1 antibodies decorated mitochondria in Clytia, as reported in human cells, but failed to recognise endogenous or fluorescent-tagged Clytia Poc1. Injection of specific morpholino oligonucleotides into Clytia eggs prior to fertilization to repress Poc1 mRNA translation interfered with cell division from the blastula stage, likely corresponding to when neosynthesis normally takes over from maternally supplied protein. Cell cycle lengthening and arrest were observed, phenotypes consistent with an impaired centriolar biogenesis or function. The specificity of the defects could be demonstrated by injection of synthetic Poc1 mRNA, which restored normal development. We conclude that in Clytia embryos, Poc1 has an essentially centriolar localization and function.

Designing protected areas to conserve riverine biodiversity: Lessons from a hypothetical redesign of the Kruger National Park

CSIR Research Space (South Africa)

Roux, JR

2008-01-01

Full Text Available that are largely contained within this park. Physical river types, fish species and invertebrate families or genera were used as surrogates of riverine biodiversity. Conservation planning software was used to select an optimal set of planning units to represent...

Low-protein diet for conservative management of chronic kidney disease: a systematic review and meta-analysis of controlled trials.

Science.gov (United States)

Rhee, Connie M; Ahmadi, Seyed-Foad; Kovesdy, Csaba P; Kalantar-Zadeh, Kamyar

2018-04-01

Recent data pose the question whether conservative management of chronic kidney disease (CKD) by means of a low-protein diet can be a safe and effective means to avoid or defer transition to dialysis therapy without causing protein-energy wasting or cachexia. We aimed to systematically review and meta-analyse the controlled clinical trials with adequate participants in each trial, providing rigorous contemporary evidence of the impact of a low-protein diet in the management of uraemia and its complications in patients with CKD. We searched MEDLINE (PubMed) and other sources for controlled trials on CKD to compare clinical management of CKD patients under various levels of dietary protein intake or to compare restricted protein intake with other interventions. Studies with similar patients, interventions, and outcomes were included in the meta-analyses. We identified 16 controlled trials of low-protein diet in CKD that met the stringent qualification criteria including having 30 or more participants. Compared with diets with protein intake of >0.8 g/kg/day, diets with restricted protein intake (disease, and a trend towards lower rates of all-cause death. In addition, very-low-protein diets (protein intake kidney function and reduction in the rate of progression to end-stage renal disease. Safety and adherence to a low-protein diet was not inferior to a normal protein diet, and there was no difference in the rate of malnutrition or protein-energy wasting. In this pooled analysis of moderate-size controlled trials, a low-protein diet appears to enhance the conservative management of non-dialysis-dependent CKD and may be considered as a potential option for CKD patients who wish to avoid or defer dialysis initiation and to slow down the progression of CKD, while the risk of protein-energy wasting and cachexia remains minimal. © 2017 The Authors. Journal of Cachexia, Sarcopenia and Muscle published by John Wiley & Sons Ltd on behalf of the Society on Sarcopenia

The conserved 12-amino acid stretch in the inter-bromodomain region of BET family proteins functions as a nuclear localization signal.

Science.gov (United States)

Fukazawa, Hidesuke; Masumi, Atsuko

2012-01-01

The bromodomain and extraterminal (BET) family is a group of chromatin-binding proteins characterized by two bromodomains, an extraterminal (ET) domain, and several other conserved regions of unknown function. In humans, the BET family consists of four members, BRD2, BRD3, BRD4 and BRDT, that all normally localize to the nucleus. We identified a 12-amino acid stretch in the inter-bromodomain region that is perfectly conserved among the BET family members. We deleted these residues and expressed the mutant proteins in HEK293T cells to investigate the function of this motif. We found that the deletion of this motif alters the localization of BET proteins. Mutated BRD3 and BRD4 were excluded from the nucleus, and BRDT was found to be diffused throughout the nucleus and cytoplasm. Although the mutant BRD2 remained predominantly in the nucleus, a punctate distribution was also observed in the cytosol. It has been reported that a conserved motif between the second bromodomain and the ET domain serves as a nuclear localization signal for BRD2. Nevertheless, BET mutants lacking the reported nuclear localization signal motif but retaining the 12-amino acid stretch resided in the nucleus. Furthermore, these mutants were diffused throughout the cytoplasm when the 12 residues were removed. These results indicate that the conserved amino acid stretch in the inter-bromodomain region of the BET family functions as a nuclear localization signal.

Further evidence of close correspondence for alcohol demand decision making for hypothetical and incentivized rewards.

Science.gov (United States)

Amlung, Michael; MacKillop, James

2015-04-01

Alcohol purchase tasks (APTs) are increasingly being used to assess behavioral economic demand for alcohol. Prior studies utilizing APTs have typically assessed demand for hypothetical outcomes, making the extent to which these hypothetical measures reflect preferences when actual rewards are at stake an important empirical question. This study examined alcohol demand across hypothetical and incentivized APTs. Nineteen male heavy drinkers completed two APTs - one for hypothetical alcohol and another in which one randomly-selected outcome was provided. Participants were given an opportunity to consume the alcohol associated with their choice on the incentivized APT during a self-administration period in a simulated bar environment. Results indicated generally close correspondence between APT versions, though participants were more sensitive to increases in price and tended to consume more at low prices on the incentivized version. Estimated consumption on the incentivized APT was highly correlated with the amount of alcohol consumed in the laboratory (r=.87, pdecision-making when rewards are hypothetical vs. actually available. Implications for behavioral economic approaches to addictive behavior and directions for future research are discussed. Copyright © 2015 Elsevier B.V. All rights reserved.

Properties of Sequence Conservation in Upstream Regulatory and Protein Coding Sequences among Paralogs in Arabidopsis thaliana

Science.gov (United States)

Richardson, Dale N.; Wiehe, Thomas

Whole genome duplication (WGD) has catalyzed the formation of new species, genes with novel functions, altered expression patterns, complexified signaling pathways and has provided organisms a level of genetic robustness. We studied the long-term evolution and interrelationships of 5’ upstream regulatory sequences (URSs), protein coding sequences (CDSs) and expression correlations (EC) of duplicated gene pairs in Arabidopsis. Three distinct methods revealed significant evolutionary conservation between paralogous URSs and were highly correlated with microarray-based expression correlation of the respective gene pairs. Positional information on exact matches between sequences unveiled the contribution of micro-chromosomal rearrangements on expression divergence. A three-way rank analysis of URS similarity, CDS divergence and EC uncovered specific gene functional biases. Transcription factor activity was associated with gene pairs exhibiting conserved URSs and divergent CDSs, whereas a broad array of metabolic enzymes was found to be associated with gene pairs showing diverged URSs but conserved CDSs.

Astrophysical implications of hypothetical stable TeV-scale black holes

International Nuclear Information System (INIS)

Giddings, Steven B.; Mangano, Michelangelo L.

2008-01-01

We analyze macroscopic effects of TeV-scale black holes, such as could possibly be produced at the LHC, in what is regarded as an extremely hypothetical scenario in which they are stable and, if trapped inside Earth, begin to accrete matter. We examine a wide variety of TeV-scale gravity scenarios, basing the resulting accretion models on first-principles, basic, and well-tested physical laws. These scenarios fall into two classes, depending on whether accretion could have any macroscopic effect on the Earth at times shorter than the Sun's natural lifetime. We argue that cases with such an effect at shorter times than the solar lifetime are ruled out, since in these scenarios black holes produced by cosmic rays impinging on much denser white dwarfs and neutron stars would then catalyze their decay on time scales incompatible with their known lifetimes. We also comment on relevant lifetimes for astronomical objects that capture primordial black holes. In short, this study finds no basis for concerns that TeV-scale black holes from the LHC could pose a risk to Earth on time scales shorter than the Earth's natural lifetime. Indeed, conservative arguments based on detailed calculations and the best-available scientific knowledge, including solid astronomical data, conclude, from multiple perspectives, that there is no risk of any significance whatsoever from such black holes.

Shock loading of reactor vessel following hypothetical core disruptive accident

International Nuclear Information System (INIS)

Srinivas, G.; Doshi, J.B.

1990-01-01

Hypothetical Core Disruptive Accident (HCDA) has been historically considered as the maximum credible accident in Fast Breeder Reactor systems. Environmental consequences of such an accident depends to a great extent on the ability of the reactor vessel to maintain integrity during the shock loading following an HCDA. In the present paper, a computational model of the reactor core and the surrounding coolant with a free surface is numerical technique. The equations for conservation of mass, momentum and energy along with an equation of state are considered in two dimensional cylindrical geometry. The reactor core at the end of HCDA is taken as a bubble of hot, vaporized fuel at high temperature and pressure, formed at the center of the reactor vessel and expanding against the surrounding liquid sodium coolant. The free surface of sodium at the top of the vessel and the movement of the core bubble-liquid coolant interface are tracked by Marker and Cell (MAC) procedure. The results are obtained for the transient pressure at the vessel wall and also for the loading on the roof plug by the impact of the slug of liquid sodium. The computer code developed is validated against a benchmark experiment chosen to be ISPRA experiment reported in literature. The computer code is next applied to predict the loading on the Indian Prototype Fast Breeder Reactor (PFBR) being developed at Kalpakkam

Rearrangement of a polar core provides a conserved mechanism for constitutive activation of class B G protein-coupled receptors

Science.gov (United States)

Yin, Yanting; de Waal, Parker W.; He, Yuanzheng; Zhao, Li-Hua; Yang, Dehua; Cai, Xiaoqing; Jiang, Yi; Melcher, Karsten; Wang, Ming-Wei; Xu, H. Eric

2017-01-01

The glucagon receptor (GCGR) belongs to the secretin-like (class B) family of G protein-coupled receptors (GPCRs) and is activated by the peptide hormone glucagon. The structures of an activated class B GPCR have remained unsolved, preventing a mechanistic understanding of how these receptors are activated. Using a combination of structural modeling and mutagenesis studies, we present here two modes of ligand-independent activation of GCGR. First, we identified a GCGR-specific hydrophobic lock comprising Met-338 and Phe-345 within the IC3 loop and transmembrane helix 6 (TM6) and found that this lock stabilizes the TM6 helix in the inactive conformation. Disruption of this hydrophobic lock led to constitutive G protein and arrestin signaling. Second, we discovered a polar core comprising conserved residues in TM2, TM3, TM6, and TM7, and mutations that disrupt this polar core led to constitutive GCGR activity. On the basis of these results, we propose a mechanistic model of GCGR activation in which TM6 is held in an inactive conformation by the conserved polar core and the hydrophobic lock. Mutations that disrupt these inhibitory elements allow TM6 to swing outward to adopt an active TM6 conformation similar to that of the canonical β2-adrenergic receptor complexed with G protein and to that of rhodopsin complexed with arrestin. Importantly, mutations in the corresponding polar core of several other members of class B GPCRs, including PTH1R, PAC1R, VIP1R, and CRFR1, also induce constitutive G protein signaling, suggesting that the rearrangement of the polar core is a conserved mechanism for class B GPCR activation. PMID:28356352

Role of Bacterioferritin & Ferritin in M. tuberculosis Pathogenesis and Drug Resistance: A Future Perspective by Interactomic Approach

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Divakar Sharma

2017-06-01

Full Text Available Tuberculosis is caused by Mycobacterium tuberculosis, one of the most successful and deadliest human pathogen. Aminoglycosides resistance leads to emergence of extremely drug resistant strains of M. tuberculosis. Iron is crucial for the biological functions of the cells. Iron assimilation, storage and their utilization is not only involved in pathogenesis but also in emergence of drug resistance strains. We previously reported that iron storing proteins (bacterioferritin and ferritin were found to be overexpressed in aminoglycosides resistant isolates. In this study we performed the STRING analysis of bacterioferritin & ferritin proteins and predicted their interactive partners [ferrochelatase (hemH, Rv1877 (hypothetical protein/probable conserved integral membrane protein, uroporphyrinogen decarboxylase (hemE trigger factor (tig, transcriptional regulatory protein (MT3948, hypothetical protein (MT1928, glnA3 (glutamine synthetase, molecular chaperone GroEL (groEL1 & hsp65, and hypothetical protein (MT3947]. We suggested that interactive partners of bacterioferritin and ferritin are directly or indirectly involved in M. tuberculosis growth, homeostasis, iron assimilation, virulence, resistance, and stresses.

Conformational coupling between receptor and kinase binding sites through a conserved salt bridge in a signaling complex scaffold protein.

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Davi R Ortega

Full Text Available Bacterial chemotaxis is one of the best studied signal transduction pathways. CheW is a scaffold protein that mediates the association of the chemoreceptors and the CheA kinase in a ternary signaling complex. The effects of replacing conserved Arg62 of CheW with other residues suggested that the scaffold protein plays a more complex role than simply binding its partner proteins. Although R62A CheW had essentially the same affinity for chemoreceptors and CheA, cells expressing the mutant protein are impaired in chemotaxis. Using a combination of molecular dynamics simulations (MD, NMR spectroscopy, and circular dichroism (CD, we addressed the role of Arg62. Here we show that Arg62 forms a salt bridge with another highly conserved residue, Glu38. Although this interaction is unimportant for overall protein stability, it is essential to maintain the correct alignment of the chemoreceptor and kinase binding sites of CheW. Computational and experimental data suggest that the role of the salt bridge in maintaining the alignment of the two partner binding sites is fundamental to the function of the signaling complex but not to its assembly. We conclude that a key feature of CheW is to maintain the specific geometry between the two interaction sites required for its function as a scaffold.

Preliminary crystallographic analysis of two hypothetical ribose-5-phosphate isomerases from Streptococcus mutans

International Nuclear Information System (INIS)

Wang, Chen; Fan, Xuexin; Cao, Xiaofang; Liu, Xiang; Li, Lanfen; Su, Xiaodong

2012-01-01

Two hypothetical ribose-5-phosphate isomerases from S. mutans have been produced in E. coli and crystallized. The crystals diffracted to high resolutions suitable for crystallographic analyses. Study of the enzymes from sugar metabolic pathways may provide a better understanding of the pathogenesis of the human oral pathogen Streptococcus mutans. Bioinformatics, biochemical and crystallization methods were used to characterize and understand the function of two putative ribose-5-phosphate isomerases: SMU1234 and SMU2142. The proteins were cloned and constructed with N-terminal His tags. Protein purification was performed by Ni 2+ -chelating and size-exclusion chromatography. The crystals of SUM1234 diffracted to 1.9 Å resolution and belonged to space group P2 1 2 1 2 1 , with unit-cell parameters a = 48.97, b = 98.27, c = 101.09 Å, α = β = γ = 90°. The optimized SMU2142 crystals diffracted to 2.7 Å resolution and belonged to space group P1, with unit-cell parameters a = 53.7, b = 54.1, c = 86.5 Å, α = 74.2, β = 73.5, γ = 83.7°. Initial phasing of both proteins was attempted by molecular replacement; the structure of SMU1234 could easily be solved, but no useful results were obtained for SMU2142. Therefore, SeMet-labelled SMU2142 will be prepared for phasing

Structural and Function Prediction of Musa acuminata subsp. Malaccensis Protein

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Anum Munir

2016-03-01

Full Text Available Hypothetical proteins (HPs are the proteins whose presence has been anticipated, yet in vivo function has not been built up. Illustrating the structural and functional privileged insights of these HPs might likewise prompt a superior comprehension of the protein-protein associations or networks in diverse types of life. Bananas (Musa acuminata spp., including sweet and cooking types, are giant perennial monocotyledonous herbs of the order Zingiberales, a sister grouped to the all-around considered Poales, which incorporate oats. Bananas are crucial for nourishment security in numerous tropical and subtropical nations and the most prominent organic product in industrialized nations. In the present study, the hypothetical protein of M. acuminata (Banana was chosen for analysis and modeling by distinctive bioinformatics apparatuses and databases. As indicated by primary and secondary structure analysis, XP_009393594.1 is a stable hydrophobic protein containing a noteworthy extent of α-helices; Homology modeling was done utilizing SWISS-MODEL server where the templates identity with XP_009393594.1 protein was less which demonstrated novelty of our protein. Ab initio strategy was conducted to produce its 3D structure. A few evaluations of quality assessment and validation parameters determined the generated protein model as stable with genuinely great quality. Functional analysis was completed by ProtFun 2.2, and KEGG (KAAS, recommended that the hypothetical protein is a transcription factor with cytoplasmic domain as zinc finger. The protein was observed to be vital for translation process, involved in metabolism, signaling and cellular processes, genetic information processing and Zinc ion binding. It is suggested that further test approval would help to anticipate the structures and functions of other uncharacterized proteins of different plants and living being.

Deorphanization and target validation of cross-tick species conserved novel Amblyomma americanum tick saliva protein.

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Mulenga, Albert; Kim, Tae Kwon; Ibelli, Adriana Mércia Guaratini

2013-05-01

We previously identified a cross-tick species conserved tick feeding stimuli responsive Amblyomma americanum (Aam) AV422 gene. This study demonstrates that AamAV422 belongs to a novel group of arthropod proteins that is characterized by 14 cysteine amino acid residues: C(23)-X7/9-C(33)-X23/24-C(58)-X8-C(67)-X7-C(75)-X23-C(99)-X15-C(115)-X10-C(126)-X24/25/33-C(150)C(151)-X7-C(159)-X8-C(168)-X23/24-C(192)-X9/10-C(202) predicted to form seven disulfide bonds. We show that AamAV422 protein is a ubiquitously expressed protein that is injected into the host within the first 24h of the tick attaching onto the host as revealed by Western blotting analyses of recombinant (r)AamAV422, tick saliva and dissected tick organ protein extracts using antibodies to 24 and 48 h tick saliva proteins. Native AamAV422 is apparently involved with mediating tick anti-hemostasis and anti-complement functions in that rAamAV422 delayed plasma clotting time in a dose responsive manner by up to ≈ 160 s, prevented platelet aggregation by up to ≈ 16% and caused ≈ 24% reduction in production of terminal complement complexes. Target validation analysis revealed that rAamAV422 is a potential candidate for a cocktail or multivalent tick vaccine preparation in that RNA interference (RNAi)-mediated silencing of AamAV422 mRNA caused a statistically significant (≈ 44%) reduction in tick engorgement weights, which is proxy for amounts of ingested blood. We speculate that AamAV422 is a potential target antigen for development of the highly desired universal tick vaccine in that consistent with high conservation among ticks, antibodies to 24h Ixodes scapularis tick saliva proteins specifically bound rAamAV422. We discuss data in this study in the context of advancing the biology of tick feeding physiology and discovery of potential target antigens for tick vaccine development. Copyright © 2013 Australian Society for Parasitology Inc. Published by Elsevier Ltd. All rights reserved.

Demand curves for hypothetical cocaine in cocaine-dependent individuals.

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Bruner, Natalie R; Johnson, Matthew W

2014-03-01

Drug purchasing tasks have been successfully used to examine demand for hypothetical consumption of abused drugs including heroin, nicotine, and alcohol. In these tasks, drug users make hypothetical choices whether to buy drugs, and if so, at what quantity, at various potential prices. These tasks allow for behavioral economic assessment of that drug's intensity of demand (preferred level of consumption at extremely low prices) and demand elasticity (sensitivity of consumption to price), among other metrics. However, a purchasing task for cocaine in cocaine-dependent individuals has not been investigated. This study examined a novel Cocaine Purchasing Task and the relation between resulting demand metrics and self-reported cocaine use data. Participants completed a questionnaire assessing hypothetical purchases of cocaine units at prices ranging from $0.01 to $1,000. Demand curves were generated from responses on the Cocaine Purchasing Task. Correlations compared metrics from the demand curve to measures of real-world cocaine use. Group and individual data were well modeled by a demand curve function. The validity of the Cocaine Purchasing Task was supported by a significant correlation between the demand curve metrics of demand intensity and O max (determined from Cocaine Purchasing Task data) and self-reported measures of cocaine use. Partial correlations revealed that after controlling for demand intensity, demand elasticity and the related measure, P max, were significantly correlated with real-world cocaine use. Results indicate that the Cocaine Purchasing Task produces orderly demand curve data, and that these data relate to real-world measures of cocaine use.

Regulation of G-protein coupled receptor traffic by an evolutionary conserved hydrophobic signal.

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Angelotti, Tim; Daunt, David; Shcherbakova, Olga G; Kobilka, Brian; Hurt, Carl M

2010-04-01

Plasma membrane (PM) expression of G-protein coupled receptors (GPCRs) is required for activation by extracellular ligands; however, mechanisms that regulate PM expression of GPCRs are poorly understood. For some GPCRs, such as alpha2c-adrenergic receptors (alpha(2c)-ARs), heterologous expression in non-native cells results in limited PM expression and extensive endoplasmic reticulum (ER) retention. Recently, ER export/retentions signals have been proposed to regulate cellular trafficking of several GPCRs. By utilizing a chimeric alpha(2a)/alpha(2c)-AR strategy, we identified an evolutionary conserved hydrophobic sequence (ALAAALAAAAA) in the extracellular amino terminal region that is responsible in part for alpha(2c)-AR subtype-specific trafficking. To our knowledge, this is the first luminal ER retention signal reported for a GPCR. Removal or disruption of the ER retention signal dramatically increased PM expression and decreased ER retention. Conversely, transplantation of this hydrophobic sequence into alpha(2a)-ARs reduced their PM expression and increased ER retention. This evolutionary conserved hydrophobic trafficking signal within alpha(2c)-ARs serves as a regulator of GPCR trafficking.

Evolutionary conservation of nuclear and nucleolar targeting sequences in yeast ribosomal protein S6A

International Nuclear Information System (INIS)

Lipsius, Edgar; Walter, Korden; Leicher, Torsten; Phlippen, Wolfgang; Bisotti, Marc-Angelo; Kruppa, Joachim

2005-01-01

Over 1 billion years ago, the animal kingdom diverged from the fungi. Nevertheless, a high sequence homology of 62% exists between human ribosomal protein S6 and S6A of Saccharomyces cerevisiae. To investigate whether this similarity in primary structure is mirrored in corresponding functional protein domains, the nuclear and nucleolar targeting signals were delineated in yeast S6A and compared to the known human S6 signals. The complete sequence of S6A and cDNA fragments was fused to the 5'-end of the LacZ gene, the constructs were transiently expressed in COS cells, and the subcellular localization of the fusion proteins was detected by indirect immunofluorescence. One bipartite and two monopartite nuclear localization signals as well as two nucleolar binding domains were identified in yeast S6A, which are located at homologous regions in human S6 protein. Remarkably, the number, nature, and position of these targeting signals have been conserved, albeit their amino acid sequences have presumably undergone a process of co-evolution with their corresponding rRNAs

The effectiveness of celebrities in conservation marketing.

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Duthie, Elizabeth; Veríssimo, Diogo; Keane, Aidan; Knight, Andrew T

2017-01-01

Celebrities are frequently used in conservation marketing as a tool to raise awareness, generate funding and effect behaviour change. The importance of evaluating effectiveness is widely recognised in both marketing and conservation but, to date, little research into the effectiveness of celebrity endorsement as a tool for conservation marketing has been published. Using a combination of interviews and an online choice survey instrument, we investigated the extent to which a sample of UK-based conservation organisations, and other charities, evaluate their own usage of celebrity endorsement, and then carried out an experimental evaluation of a hypothetical marketing campaign. This experiment compared participants' willingness-to-engage (WTE) with, and recall of, a conservation message presented in versions of an advert featuring one of three prominent UK celebrities (David Beckham, Chris Packham or HRH Prince William) or a non-celebrity control treatment (featuring Crawford Allan, a director of TRAFFIC USA). We find that the organisations we interviewed did not routinely evaluate their marketing campaigns featuring celebrities. Furthermore, our experiment provides evidence that celebrity endorsement can produce both positive and negative effects. Participants were more willing to engage when presented with an advert featuring one of the three celebrities than the non-celebrity control, and WTE varied according to the characteristics of the celebrity and the respondent. However, celebrities were less effective at generating campaign message recall than non-celebrities. These findings suggest that celebrity endorsement should be used carefully. Further work is required to fully understand the role celebrity endorsers can play in conservation but, drawing on best practice from the field of marketing, this study introduces an approach to evaluation which could be applied more widely to improve the effectiveness of conservation marketing.

The effectiveness of celebrities in conservation marketing.

Directory of Open Access Journals (Sweden)

Elizabeth Duthie

Full Text Available Celebrities are frequently used in conservation marketing as a tool to raise awareness, generate funding and effect behaviour change. The importance of evaluating effectiveness is widely recognised in both marketing and conservation but, to date, little research into the effectiveness of celebrity endorsement as a tool for conservation marketing has been published. Using a combination of interviews and an online choice survey instrument, we investigated the extent to which a sample of UK-based conservation organisations, and other charities, evaluate their own usage of celebrity endorsement, and then carried out an experimental evaluation of a hypothetical marketing campaign. This experiment compared participants' willingness-to-engage (WTE with, and recall of, a conservation message presented in versions of an advert featuring one of three prominent UK celebrities (David Beckham, Chris Packham or HRH Prince William or a non-celebrity control treatment (featuring Crawford Allan, a director of TRAFFIC USA. We find that the organisations we interviewed did not routinely evaluate their marketing campaigns featuring celebrities. Furthermore, our experiment provides evidence that celebrity endorsement can produce both positive and negative effects. Participants were more willing to engage when presented with an advert featuring one of the three celebrities than the non-celebrity control, and WTE varied according to the characteristics of the celebrity and the respondent. However, celebrities were less effective at generating campaign message recall than non-celebrities. These findings suggest that celebrity endorsement should be used carefully. Further work is required to fully understand the role celebrity endorsers can play in conservation but, drawing on best practice from the field of marketing, this study introduces an approach to evaluation which could be applied more widely to improve the effectiveness of conservation marketing.

Rearrangement of a polar core provides a conserved mechanism for constitutive activation of class B G protein-coupled receptors.

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Yin, Yanting; de Waal, Parker W; He, Yuanzheng; Zhao, Li-Hua; Yang, Dehua; Cai, Xiaoqing; Jiang, Yi; Melcher, Karsten; Wang, Ming-Wei; Xu, H Eric

2017-06-16

The glucagon receptor (GCGR) belongs to the secretin-like (class B) family of G protein-coupled receptors (GPCRs) and is activated by the peptide hormone glucagon. The structures of an activated class B GPCR have remained unsolved, preventing a mechanistic understanding of how these receptors are activated. Using a combination of structural modeling and mutagenesis studies, we present here two modes of ligand-independent activation of GCGR. First, we identified a GCGR-specific hydrophobic lock comprising Met-338 and Phe-345 within the IC3 loop and transmembrane helix 6 (TM6) and found that this lock stabilizes the TM6 helix in the inactive conformation. Disruption of this hydrophobic lock led to constitutive G protein and arrestin signaling. Second, we discovered a polar core comprising conserved residues in TM2, TM3, TM6, and TM7, and mutations that disrupt this polar core led to constitutive GCGR activity. On the basis of these results, we propose a mechanistic model of GCGR activation in which TM6 is held in an inactive conformation by the conserved polar core and the hydrophobic lock. Mutations that disrupt these inhibitory elements allow TM6 to swing outward to adopt an active TM6 conformation similar to that of the canonical β 2 -adrenergic receptor complexed with G protein and to that of rhodopsin complexed with arrestin. Importantly, mutations in the corresponding polar core of several other members of class B GPCRs, including PTH1R, PAC1R, VIP1R, and CRFR1, also induce constitutive G protein signaling, suggesting that the rearrangement of the polar core is a conserved mechanism for class B GPCR activation. © 2017 by The American Society for Biochemistry and Molecular Biology, Inc.

The conserved baculovirus protein p33 (Ac92) is a flavin adenine dinucleotide-linked sulfhydryl oxidase

International Nuclear Information System (INIS)

Long, C.M.; Rohrmann, G.F.; Merrill, G.F.

2009-01-01

Open reading frame 92 of the Autographa californica baculovirus (Ac92) is one of about 30 core genes present in all sequenced baculovirus genomes. Computer analyses predicted that the Ac92 encoded protein (called p33) and several of its baculovirus orthologs were related to a family of flavin adenine dinucleotide (FAD)-linked sulfhydryl oxidases. Alignment of these proteins indicated that, although they were highly diverse, a number of amino acids in common with the Erv1p/Alrp family of sulfhydryl oxidases are present. Some of these conserved amino acids are predicted to stack against the isoalloxazine and adenine components of FAD, whereas others are involved in electron transfer. To investigate this relationship, Ac92 was expressed in bacteria as a His-tagged fusion protein, purified, and characterized both spectrophotometrically and for its enzymatic activity. The purified protein was found to have the color (yellow) and absorption spectrum consistent with it being a FAD-containing protein. Furthermore, it was demonstrated to have sulfhydryl oxidase activity using dithiothreitol and thioredoxin as substrates.

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface

Science.gov (United States)

2011-01-01

Background Halophiles are extremophilic microorganisms growing optimally at high salt concentrations. There are two strategies used by halophiles to maintain proper osmotic pressure in their cytoplasm: accumulation of molar concentrations of potassium and chloride with extensive adaptation of the intracellular macromolecules ("salt-in" strategy) or biosynthesis and/or accumulation of organic osmotic solutes ("osmolyte" strategy). Our work was aimed at contributing to the understanding of the shared molecular mechanisms of protein haloadaptation through a detailed and systematic comparison of a sample of several three-dimensional structures of halophilic and non-halophilic proteins. Structural differences observed between the "salt-in" and the mesophilic homologous proteins were contrasted to those observed between the "osmolyte" and mesophilic pairs. Results The results suggest that haloadaptation strategy in the presence of molar salt concentration, but not of osmolytes, necessitates a weakening of the hydrophobic interactions, in particular at the level of conserved hydrophobic contacts. Weakening of these interactions counterbalances their strengthening by the presence of salts in solution and may help the structure preventing aggregation and/or loss of function in hypersaline environments. Conclusions Considering the significant increase of biotechnology applications of halophiles, the understanding of halophilicity can provide the theoretical basis for the engineering of proteins of great interest because stable at concentrations of salts that cause the denaturation or aggregation of the majority of macromolecules. PMID:22192175

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface

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Siglioccolo Alessandro

2011-12-01

Full Text Available Abstract Background Halophiles are extremophilic microorganisms growing optimally at high salt concentrations. There are two strategies used by halophiles to maintain proper osmotic pressure in their cytoplasm: accumulation of molar concentrations of potassium and chloride with extensive adaptation of the intracellular macromolecules ("salt-in" strategy or biosynthesis and/or accumulation of organic osmotic solutes ("osmolyte" strategy. Our work was aimed at contributing to the understanding of the shared molecular mechanisms of protein haloadaptation through a detailed and systematic comparison of a sample of several three-dimensional structures of halophilic and non-halophilic proteins. Structural differences observed between the "salt-in" and the mesophilic homologous proteins were contrasted to those observed between the "osmolyte" and mesophilic pairs. Results The results suggest that haloadaptation strategy in the presence of molar salt concentration, but not of osmolytes, necessitates a weakening of the hydrophobic interactions, in particular at the level of conserved hydrophobic contacts. Weakening of these interactions counterbalances their strengthening by the presence of salts in solution and may help the structure preventing aggregation and/or loss of function in hypersaline environments. Conclusions Considering the significant increase of biotechnology applications of halophiles, the understanding of halophilicity can provide the theoretical basis for the engineering of proteins of great interest because stable at concentrations of salts that cause the denaturation or aggregation of the majority of macromolecules.

A human protein interaction network shows conservation of aging processes between human and invertebrate species.

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Russell Bell

2009-03-01

Full Text Available We have mapped a protein interaction network of human homologs of proteins that modify longevity in invertebrate species. This network is derived from a proteome-scale human protein interaction Core Network generated through unbiased high-throughput yeast two-hybrid searches. The longevity network is composed of 175 human homologs of proteins known to confer increased longevity through loss of function in yeast, nematode, or fly, and 2,163 additional human proteins that interact with these homologs. Overall, the network consists of 3,271 binary interactions among 2,338 unique proteins. A comparison of the average node degree of the human longevity homologs with random sets of proteins in the Core Network indicates that human homologs of longevity proteins are highly connected hubs with a mean node degree of 18.8 partners. Shortest path length analysis shows that proteins in this network are significantly more connected than would be expected by chance. To examine the relationship of this network to human aging phenotypes, we compared the genes encoding longevity network proteins to genes known to be changed transcriptionally during aging in human muscle. In the case of both the longevity protein homologs and their interactors, we observed enrichments for differentially expressed genes in the network. To determine whether homologs of human longevity interacting proteins can modulate life span in invertebrates, homologs of 18 human FRAP1 interacting proteins showing significant changes in human aging muscle were tested for effects on nematode life span using RNAi. Of 18 genes tested, 33% extended life span when knocked-down in Caenorhabditis elegans. These observations indicate that a broad class of longevity genes identified in invertebrate models of aging have relevance to human aging. They also indicate that the longevity protein interaction network presented here is enriched for novel conserved longevity proteins.

An evolutionary model for protein-coding regions with conserved RNA structure

DEFF Research Database (Denmark)

Pedersen, Jakob Skou; Forsberg, Roald; Meyer, Irmtraud Margret

2004-01-01

in the RNA structure. The overlap of these fundamental dependencies is sufficient to cause "contagious" context dependencies which cascade across many nucleotide sites. Such large-scale dependencies challenge the use of traditional phylogenetic models in evolutionary inference because they explicitly assume...... components of traditional phylogenetic models. We applied this to a data set of full-genome sequences from the hepatitis C virus where five RNA structures are mapped within the coding region. This allowed us to partition the effects of selection on different structural elements and to test various hypotheses......Here we present a model of nucleotide substitution in protein-coding regions that also encode the formation of conserved RNA structures. In such regions, apparent evolutionary context dependencies exist, both between nucleotides occupying the same codon and between nucleotides forming a base pair...

A conserved mammalian protein interaction network.

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Åsa Pérez-Bercoff

Full Text Available Physical interactions between proteins mediate a variety of biological functions, including signal transduction, physical structuring of the cell and regulation. While extensive catalogs of such interactions are known from model organisms, their evolutionary histories are difficult to study given the lack of interaction data from phylogenetic outgroups. Using phylogenomic approaches, we infer a upper bound on the time of origin for a large set of human protein-protein interactions, showing that most such interactions appear relatively ancient, dating no later than the radiation of placental mammals. By analyzing paired alignments of orthologous and putatively interacting protein-coding genes from eight mammals, we find evidence for weak but significant co-evolution, as measured by relative selective constraint, between pairs of genes with interacting proteins. However, we find no strong evidence for shared instances of directional selection within an interacting pair. Finally, we use a network approach to show that the distribution of selective constraint across the protein interaction network is non-random, with a clear tendency for interacting proteins to share similar selective constraints. Collectively, the results suggest that, on the whole, protein interactions in mammals are under selective constraint, presumably due to their functional roles.

A conserved small RNA promotes silencing of the outer membrane protein YbfM

DEFF Research Database (Denmark)

Rasmussen, Anders Aamann; Johansen, Jesper; Nielsen, Jesper S

2009-01-01

important physiological role of regulatory RNA molecules in Gram-negative bacteria is to modulate the cell surface and/or to prevent accumulation of OMPs in the envelope. Here, we extend the OMP-sRNA network by showing that the expression of the outer membrane protein YbfM is silenced by a conserved sRNA......In the past few years an increasing number of small non-coding RNAs (sRNAs) in enterobacteria have been found to negatively regulate the expression of outer membrane proteins (OMPs) at the post-transcriptional level. These RNAs act under various growth and stress conditions, suggesting that one......, designated MicM (also known as RybC/SroB). The regulation is strictly dependent on the RNA chaperone Hfq, and mutational analysis indicates that MicM sequesters the ribosome binding site of ybfM mRNA by an antisense mechanism. Furthermore, we provide evidence that Hfq strongly enhances the on-rate of duplex...

Conserved TRAM Domain Functions as an Archaeal Cold Shock Protein via RNA Chaperone Activity

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Bo Zhang

2017-08-01

Full Text Available Cold shock proteins (Csps enable organisms to acclimate to and survive in cold environments and the bacterial CspA family exerts the cold protection via its RNA chaperone activity. However, most Archaea do not contain orthologs to the bacterial csp. TRAM, a conserved domain among RNA modification proteins ubiquitously distributed in organisms, occurs as an individual protein in most archaeal phyla and has a structural similarity to Csp proteins, yet its biological functions remain unknown. Through physiological and biochemical studies on four TRAM proteins from a cold adaptive archaeon Methanolobus psychrophilus R15, this work demonstrated that TRAM is an archaeal Csp and exhibits RNA chaperone activity. Three TRAM encoding genes (Mpsy_0643, Mpsy_3043, and Mpsy_3066 exhibited remarkable cold-shock induced transcription and were preferentially translated at lower temperature (18°C, while the fourth (Mpsy_2002 was constitutively expressed. They were all able to complement the cspABGE mutant of Escherichia coli BX04 that does not grow in cold temperatures and showed transcriptional antitermination. TRAM3066 (gene product of Mpsy_3066 and TRAM2002 (gene product of Mpsy_2002 displayed sequence-non-specific RNA but not DNA binding activity, and TRAM3066 assisted RNases in degradation of structured RNA, thus validating the RNA chaperone activity of TRAMs. Given the chaperone activity, TRAM is predicted to function beyond a Csp.

A Conserved Acidic Motif in the N-Terminal Domain of Nitrate Reductase Is Necessary for the Inactivation of the Enzyme in the Dark by Phosphorylation and 14-3-3 Binding1

Science.gov (United States)

Pigaglio, Emmanuelle; Durand, Nathalie; Meyer, Christian

1999-01-01

It has previously been shown that the N-terminal domain of tobacco (Nicotiana tabacum) nitrate reductase (NR) is involved in the inactivation of the enzyme by phosphorylation, which occurs in the dark (L. Nussaume, M. Vincentz, C. Meyer, J.P. Boutin, and M. Caboche [1995] Plant Cell 7: 611–621). The activity of a mutant NR protein lacking this N-terminal domain was no longer regulated by light-dark transitions. In this study smaller deletions were performed in the N-terminal domain of tobacco NR that removed protein motifs conserved among higher plant NRs. The resulting truncated NR-coding sequences were then fused to the cauliflower mosaic virus 35S RNA promoter and introduced in NR-deficient mutants of the closely related species Nicotiana plumbaginifolia. We found that the deletion of a conserved stretch of acidic residues led to an active NR protein that was more thermosensitive than the wild-type enzyme, but it was relatively insensitive to the inactivation by phosphorylation in the dark. Therefore, the removal of this acidic stretch seems to have the same effects on NR activation state as the deletion of the N-terminal domain. A hypothetical explanation for these observations is that a specific factor that impedes inactivation remains bound to the truncated enzyme. A synthetic peptide derived from this acidic protein motif was also found to be a good substrate for casein kinase II. PMID:9880364

Using a choice experiment and birder preferences to guide bird-conservation funding.

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Steven, Rochelle; Smart, James C R; Morrison, Clare; Castley, J Guy

2017-08-01

Conservation of biodiversity, including birds, continues to challenge natural-area managers. Stated-preference methods (e.g., choice experiment [CE]) are increasingly used to provide data for valuation of natural ecosystems. We used a CE to calculate birders' willingness to pay for different levels of bioecological attributes (threatened species, endemic species, and diversity) of birding sites with hypothetical entry fees. The CE was delivered at popular birding and avitourism sites in Australia and the United Kingdom. Latent-class modeling results revealed heterogeneous preferences among birders and correspondingly variable willingness to pay. Four clear groups were apparent: quantity-driven birders, special-birds seekers, confused respondents, and price-is-no-object birders. Quantity-driven birders were attracted to sites that deliver high levels of diversity and endemic species for which they were willing to pay $135 and $66 to visit, respectively, above what they were willing to pay to visit a site with low levels of diversity and few endemic and threatened species . Special-bird seekers valued threatened species and high levels of endemic species most (willingness to pay $45 and $46, respectively). Confused respondents' preferences were difficult to determine, but they were the most sensitive to the hypothetical entry fees, unlike the price-is-no-object birders, who were not at all sensitive to cost. Our findings demonstrate that birders are amenable to paying for their preferred birding experience. These payments could provide an alternative source of funding in some avitourism sites on both public and private land. Such alternative revenue streams should be explored and given full consideration in increasingly competitive conservation-financing environments. © 2016 Society for Conservation Biology.

Explaining the discrepancy between intentions and actions: the case of hypothetical bias in contingent valuation

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Icek Ajzen; Thomas C. Brown; Franklin Carvajal

2004-01-01

An experiment was designed to account for intention-behavior discrepancies by applying the theory of planned behavior to contingent valuation. College students (N = 160) voted in hypothetical and real payment referenda to contribute $8 to a scholarship fund. Overestimates of willingness to pay in the hypothetical referendum could not be attributed to moderately...

A configuration space of homologous proteins conserving mutual information and allowing a phylogeny inference based on pair-wise Z-score probabilities.

Science.gov (United States)

Bastien, Olivier; Ortet, Philippe; Roy, Sylvaine; Maréchal, Eric

2005-03-10

Popular methods to reconstruct molecular phylogenies are based on multiple sequence alignments, in which addition or removal of data may change the resulting tree topology. We have sought a representation of homologous proteins that would conserve the information of pair-wise sequence alignments, respect probabilistic properties of Z-scores (Monte Carlo methods applied to pair-wise comparisons) and be the basis for a novel method of consistent and stable phylogenetic reconstruction. We have built up a spatial representation of protein sequences using concepts from particle physics (configuration space) and respecting a frame of constraints deduced from pair-wise alignment score properties in information theory. The obtained configuration space of homologous proteins (CSHP) allows the representation of real and shuffled sequences, and thereupon an expression of the TULIP theorem for Z-score probabilities. Based on the CSHP, we propose a phylogeny reconstruction using Z-scores. Deduced trees, called TULIP trees, are consistent with multiple-alignment based trees. Furthermore, the TULIP tree reconstruction method provides a solution for some previously reported incongruent results, such as the apicomplexan enolase phylogeny. The CSHP is a unified model that conserves mutual information between proteins in the way physical models conserve energy. Applications include the reconstruction of evolutionary consistent and robust trees, the topology of which is based on a spatial representation that is not reordered after addition or removal of sequences. The CSHP and its assigned phylogenetic topology, provide a powerful and easily updated representation for massive pair-wise genome comparisons based on Z-score computations.

A configuration space of homologous proteins conserving mutual information and allowing a phylogeny inference based on pair-wise Z-score probabilities

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Maréchal Eric

2005-03-01

Full Text Available Abstract Background Popular methods to reconstruct molecular phylogenies are based on multiple sequence alignments, in which addition or removal of data may change the resulting tree topology. We have sought a representation of homologous proteins that would conserve the information of pair-wise sequence alignments, respect probabilistic properties of Z-scores (Monte Carlo methods applied to pair-wise comparisons and be the basis for a novel method of consistent and stable phylogenetic reconstruction. Results We have built up a spatial representation of protein sequences using concepts from particle physics (configuration space and respecting a frame of constraints deduced from pair-wise alignment score properties in information theory. The obtained configuration space of homologous proteins (CSHP allows the representation of real and shuffled sequences, and thereupon an expression of the TULIP theorem for Z-score probabilities. Based on the CSHP, we propose a phylogeny reconstruction using Z-scores. Deduced trees, called TULIP trees, are consistent with multiple-alignment based trees. Furthermore, the TULIP tree reconstruction method provides a solution for some previously reported incongruent results, such as the apicomplexan enolase phylogeny. Conclusion The CSHP is a unified model that conserves mutual information between proteins in the way physical models conserve energy. Applications include the reconstruction of evolutionary consistent and robust trees, the topology of which is based on a spatial representation that is not reordered after addition or removal of sequences. The CSHP and its assigned phylogenetic topology, provide a powerful and easily updated representation for massive pair-wise genome comparisons based on Z-score computations.

Modelling of melting and solidification transport phenomena during hypothetical NPP severe accidents

Energy Technology Data Exchange (ETDEWEB)

Sarler, B [Inst. Jozef Stefan, Ljubljana (Slovenia)

1992-07-01

A physical and mathematical framework to deal with the transport phenomena occuring during melting and solidification of the hypothetical NPP severe accidents is presented. It concentrates on the transient temperature, velocity, and species concentration distributions during such events. The framework is based on the Mixture Continuum Formulation of the components and phases, cast in the boundary-domain integral shape structured by the fundamental solution of the Laplace equation. The formulation could cope with various solid-liquid sub-systems through the inclusion of the specific closure relations. The deduced system of boundary-domain integral equations for conservation of mass, energy, momentum, and species could be solved by the boundary element discrete approximative method. (author) [Slovenian] Predstavljeno je fizikalno in matematicno ogrodje za obravnavo prenosnih pojavov taljenja in strjevanja med hipoteticnimi tezkimi nezgodami v jedrskih elektrarnah. Osredotoceno je na popis neustaljene porazdelitve temperatur, hitrosti in koncentracij sestavin med taksnimi dogodki. Ogrodje temelji na formulaciji kontinuuma mesanice komponent in faz, v obliki robno obmocnih integralskih enacb, ki so sestavljena na podlagi fundamentalne resitve Laplace-ove enacbe. Formulacija lahko popisuje stevilne trdno-tekoce pod-sisteme na podlagi specificnih sklopitvenih relacij. Izpeljan sistem robno-obmocnih integralskih enacb za popis ohranitve mase, energije, gibalne kolicine in sestavin lahko resimo na podlagi diskretne aproksimativne metode robnih elementov. (author)

Evolutionary Conservation and Emerging Functional Diversity of the Cytosolic Hsp70:J Protein Chaperone Network of Arabidopsis thaliana.

Science.gov (United States)

Verma, Amit K; Diwan, Danish; Raut, Sandeep; Dobriyal, Neha; Brown, Rebecca E; Gowda, Vinita; Hines, Justin K; Sahi, Chandan

2017-06-07

Heat shock proteins of 70 kDa (Hsp70s) partner with structurally diverse Hsp40s (J proteins), generating distinct chaperone networks in various cellular compartments that perform myriad housekeeping and stress-associated functions in all organisms. Plants, being sessile, need to constantly maintain their cellular proteostasis in response to external environmental cues. In these situations, the Hsp70:J protein machines may play an important role in fine-tuning cellular protein quality control. Although ubiquitous, the functional specificity and complexity of the plant Hsp70:J protein network has not been studied. Here, we analyzed the J protein network in the cytosol of Arabidopsis thaliana and, using yeast genetics, show that the functional specificities of most plant J proteins in fundamental chaperone functions are conserved across long evolutionary timescales. Detailed phylogenetic and functional analysis revealed that increased number, regulatory differences, and neofunctionalization in J proteins together contribute to the emerging functional diversity and complexity in the Hsp70:J protein network in higher plants. Based on the data presented, we propose that higher plants have orchestrated their "chaperome," especially their J protein complement, according to their specialized cellular and physiological stipulations. Copyright © 2017 Verma et al.

A highly conserved glycine within linker I and the extreme C terminus of G protein alpha subunits interact cooperatively in switching G protein-coupled receptor-to-effector specificity

DEFF Research Database (Denmark)

Kostenis, Evi; Martini, Lene; Ellis, James

2004-01-01

Numerous studies have attested to the importance of the extreme C terminus of G protein alpha subunits in determining their selectivity of receptor recognition. We have previously reported that a highly conserved glycine residue within linker I is important for constraining the fidelity of receptor...... recognition by Galpha(q) proteins. Herein, we explored whether both modules (linker I and extreme C terminus) interact cooperatively in switching G protein-coupled receptor (GPCR)-to-effector specificity and created as models mutant Galpha(q) proteins in which glycine was replaced with various amino acids...... and the C-terminal five Galpha(q) residues with the corresponding Galpha(i) or Galpha(s) sequence. Coupling properties of the mutated Galpha(q) proteins were determined after coexpression with a panel of 13 G(i)-and G(s) -selective receptors and compared with those of Galpha proteins modified in only one...

Analysis of hypothetical LMFBR whole-core accidents in the USA

International Nuclear Information System (INIS)

Ferguson, D.R.; Deitrich, L.W.; Brown, N.W.; Waltar, A.E.

1978-01-01

Methods used for analysis of material behaviour, accident phenomenology and integrated accident calculations are reviewed. Applications of these methods to hypothetical LOF and TOP accidents are discussed. Recent results obtained from applications to FFTF and CRBRP are presented. (author)

Ecosystem services and opportunity costs shift spatial priorities for conserving forest biodiversity.

Directory of Open Access Journals (Sweden)

Matthias Schröter

Full Text Available Inclusion of spatially explicit information on ecosystem services in conservation planning is a fairly new practice. This study analyses how the incorporation of ecosystem services as conservation features can affect conservation of forest biodiversity and how different opportunity cost constraints can change spatial priorities for conservation. We created spatially explicit cost-effective conservation scenarios for 59 forest biodiversity features and five ecosystem services in the county of Telemark (Norway with the help of the heuristic optimisation planning software, Marxan with Zones. We combined a mix of conservation instruments where forestry is either completely (non-use zone or partially restricted (partial use zone. Opportunity costs were measured in terms of foregone timber harvest, an important provisioning service in Telemark. Including a number of ecosystem services shifted priority conservation sites compared to a case where only biodiversity was considered, and increased the area of both the partial (+36.2% and the non-use zone (+3.2%. Furthermore, opportunity costs increased (+6.6%, which suggests that ecosystem services may not be a side-benefit of biodiversity conservation in this area. Opportunity cost levels were systematically changed to analyse their effect on spatial conservation priorities. Conservation of biodiversity and ecosystem services trades off against timber harvest. Currently designated nature reserves and landscape protection areas achieve a very low proportion (9.1% of the conservation targets we set in our scenario, which illustrates the high importance given to timber production at present. A trade-off curve indicated that large marginal increases in conservation target achievement are possible when the budget for conservation is increased. Forty percent of the maximum hypothetical opportunity costs would yield an average conservation target achievement of 79%.

Ecosystem Services and Opportunity Costs Shift Spatial Priorities for Conserving Forest Biodiversity

Science.gov (United States)

Schröter, Matthias; Rusch, Graciela M.; Barton, David N.; Blumentrath, Stefan; Nordén, Björn

2014-01-01

Inclusion of spatially explicit information on ecosystem services in conservation planning is a fairly new practice. This study analyses how the incorporation of ecosystem services as conservation features can affect conservation of forest biodiversity and how different opportunity cost constraints can change spatial priorities for conservation. We created spatially explicit cost-effective conservation scenarios for 59 forest biodiversity features and five ecosystem services in the county of Telemark (Norway) with the help of the heuristic optimisation planning software, Marxan with Zones. We combined a mix of conservation instruments where forestry is either completely (non-use zone) or partially restricted (partial use zone). Opportunity costs were measured in terms of foregone timber harvest, an important provisioning service in Telemark. Including a number of ecosystem services shifted priority conservation sites compared to a case where only biodiversity was considered, and increased the area of both the partial (+36.2%) and the non-use zone (+3.2%). Furthermore, opportunity costs increased (+6.6%), which suggests that ecosystem services may not be a side-benefit of biodiversity conservation in this area. Opportunity cost levels were systematically changed to analyse their effect on spatial conservation priorities. Conservation of biodiversity and ecosystem services trades off against timber harvest. Currently designated nature reserves and landscape protection areas achieve a very low proportion (9.1%) of the conservation targets we set in our scenario, which illustrates the high importance given to timber production at present. A trade-off curve indicated that large marginal increases in conservation target achievement are possible when the budget for conservation is increased. Forty percent of the maximum hypothetical opportunity costs would yield an average conservation target achievement of 79%. PMID:25393951

Immunogenic membrane-associated proteins of Mycobacterium tuberculosis revealed by proteomics.

Science.gov (United States)

Sinha, Sudhir; Kosalai, K; Arora, Shalini; Namane, Abdelkader; Sharma, Pawan; Gaikwad, Anil N; Brodin, Priscille; Cole, Stewart T

2005-07-01

Membrane-associated proteins of Mycobacterium tuberculosis offer a challenge, as well as an opportunity, in the quest for better therapeutic and prophylactic interventions against tuberculosis. The authors have previously reported that extraction with the detergent Triton X-114 (TX-114) is a useful step in proteomic analysis of mycobacterial cell membranes, and detergent-soluble membrane proteins of mycobacteria are potent stimulators of human T cells. In this study 1-D and 2-D gel electrophoresis-based protocols were used for the analysis of proteins in the TX-114 extract of M. tuberculosis membranes. Peptide mass mapping (using MALDI-TOF-MS, matrix assisted laser desorption/ionization time of flight mass spectrometry) of 116 samples led to the identification of 105 proteins, 9 of which were new to the M. tuberculosis proteome. Functional orthologues of 73 of these proteins were also present in Mycobacterium leprae, suggesting their relative importance. Bioinformatics predicted that as many as 73% of the proteins had a hydrophobic disposition. 1-D gel electrophoresis revealed more hydrophobic/transmembrane and basic proteins than 2-D gel electrophoresis. Identified proteins fell into the following major categories: protein synthesis, cell wall biogenesis/architecture and conserved hypotheticals/unknowns. To identify immunodominant proteins of the detergent phase (DP), 14 low-molecular-mass fractions prepared by continuous-elution gel electrophoresis were subjected to T cell activation assays using blood samples from BCG-vaccinated healthy donors from a tuberculosis endemic area. Analysis of the responses (cell proliferation and IFN-gamma production) showed that the immunodominance of certain DP fractions was most probably due to ribosomal proteins, which is consistent with both their specificity for mycobacteria and their abundance. Other membrane-associated proteins, including transmembrane proteins/lipoproteins and ESAT-6, did not appear to contribute

Soymilk plant simulation to predict the formula of a new Hypothetical Product

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Iacobi Boanerges Boanerges

2018-01-01

Full Text Available Ideal Patterns reactors alteration by real reactor patterns, for better accuracy was done using industrial software: Aspen Plus and Hysys Version 7.1 to represent the batch real mixer and soymilk production system. Fluid package for properties prediction was chosen from the software list. A feed steam of 41,67 Kg/h (Soybean was taken; mass fractions were given by element since the Soybean has a wide blend of substances which cannot be described as a unique compound formula. The elements were C, N, H, O, S, Na, K, Mg, Ca, Fe, P, and Cu. Final flow of 8,333 Kg/h was used to achieve the objective of this study: the elemental analysis method for the hypothetical new product prediction (based only in presence of Amino-acids and other macro and multiple substances. The macromolecules described here are the onset for new specific soymilk compounds such as the concluded on this study. Fulminic Acid Family compound and the protein analysis may correspond to new proteins which are not well-known such as the ones found in studies by the Hospital de Rhode Island in 2014. Presence of Fe and Cu in soybean was ascribed to the micronutrients that could be present in the soil of crop cultivation and in soybeans by absorption.

Characterization of leptospiral proteins that afford partial protection in hamsters against lethal challenge with Leptospira interrogans.

Science.gov (United States)

Atzingen, Marina V; Gonçales, Amane P; de Morais, Zenaide M; Araújo, Eduardo R; De Brito, Thales; Vasconcellos, Silvio A; Nascimento, Ana L T O

2010-09-01

Leptospirosis is a worldwide zoonosis caused by pathogenic Leptospira. The whole-genome sequence of Leptospira interrogans serovar Copenhageni together with bioinformatic tools allow us to search for novel antigen candidates suitable for improved vaccines against leptospirosis. This study focused on three genes encoding conserved hypothetical proteins predicted to be exported to the outer membrane. The genes were amplified by PCR from six predominant pathogenic serovars in Brazil. The genes were cloned and expressed in Escherichia coli strain BL21-SI using the expression vector pDEST17. The recombinant proteins tagged with N-terminal 6xHis were purified by metal-charged chromatography. The proteins were recognized by antibodies present in sera from hamsters that were experimentally infected. Immunization of hamsters followed by challenge with a lethal dose of a virulent strain of Leptospira showed that the recombinant protein rLIC12730 afforded statistically significant protection to animals (44 %), followed by rLIC10494 (40 %) and rLIC12922 (30 %). Immunization with these proteins produced an increase in antibody titres during subsequent boosters, suggesting the involvement of a T-helper 2 response. Although more studies are needed, these data suggest that rLIC12730 and rLIC10494 are promising candidates for a multivalent vaccine for the prevention of leptospirosis.

The Relationship Between Personality and Schadenfreude in Hypothetical Versus Live Situations.

Science.gov (United States)

Greenier, Keegan D

2018-06-01

This study sought to investigate how individual differences are related to schadenfreude (pleasure derived from another's misfortune) by replicating past findings and extending them to additional personality traits. Because most past research on schadenfreude has relied heavily on the use of reactions to hypothetical scenarios, an attempt was made to demonstrate external validity by also including a reaction to a live event (confederate misfortune). For the scenarios, schadenfreude was positively correlated with the Dark Triad and just world beliefs; negatively correlated with empathy and agreeableness; and uncorrelated with dispositional envy, self-esteem, or the remaining Big Five traits. For the live event, no personality traits were correlated with schadenfreude, suggesting responses to hypothetical situations may not be representative of real-life schadenfreude events.

Restricted Predicates for Hypothetical Datalog

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Fernando Sáenz-Pérez

2015-12-01

Full Text Available Hypothetical Datalog is based on an intuitionistic semantics rather than on a classical logic semantics, and embedded implications are allowed in rule bodies. While the usual implication (i.e., the neck of a Horn clause stands for inferring facts, an embedded implication plays the role of assuming its premise for deriving its consequence. A former work introduced both a formal framework and a goal-oriented tabled implementation, allowing negation in rule bodies. While in that work positive assumptions for both facts and rules can occur in the premise, negative assumptions are not allowed. In this work, we cover this subject by introducing a new concept: a restricted predicate, which allows negative assumptions by pruning the usual semantics of a predicate. This new setting has been implemented in the deductive system DES.

The Conserved Spore Coat Protein SpoVM Is Largely Dispensable in Clostridium difficile Spore Formation.

Science.gov (United States)

Ribis, John W; Ravichandran, Priyanka; Putnam, Emily E; Pishdadian, Keyan; Shen, Aimee

2017-01-01

The spore-forming bacterial pathogen Clostridium difficile is a leading cause of health care-associated infections in the United States. In order for this obligate anaerobe to transmit infection, it must form metabolically dormant spores prior to exiting the host. A key step during this process is the assembly of a protective, multilayered proteinaceous coat around the spore. Coat assembly depends on coat morphogenetic proteins recruiting distinct subsets of coat proteins to the developing spore. While 10 coat morphogenetic proteins have been identified in Bacillus subtilis , only two of these morphogenetic proteins have homologs in the Clostridia : SpoIVA and SpoVM. C. difficile SpoIVA is critical for proper coat assembly and functional spore formation, but the requirement for SpoVM during this process was unknown. Here, we show that SpoVM is largely dispensable for C. difficile spore formation, in contrast with B. subtilis . Loss of C. difficile SpoVM resulted in modest decreases (~3-fold) in heat- and chloroform-resistant spore formation, while morphological defects such as coat detachment from the forespore and abnormal cortex thickness were observed in ~30% of spoVM mutant cells. Biochemical analyses revealed that C. difficile SpoIVA and SpoVM directly interact, similarly to their B. subtilis counterparts. However, in contrast with B. subtilis , C. difficile SpoVM was not essential for SpoIVA to encase the forespore. Since C. difficile coat morphogenesis requires SpoIVA-interacting protein L (SipL), which is conserved exclusively in the Clostridia , but not the more broadly conserved SpoVM, our results reveal another key difference between C. difficile and B. subtilis spore assembly pathways. IMPORTANCE The spore-forming obligate anaerobe Clostridium difficile is the leading cause of antibiotic-associated diarrheal disease in the United States. When C. difficile spores are ingested by susceptible individuals, they germinate within the gut and

Testing QCD with Hypothetical Tau Leptons

Energy Technology Data Exchange (ETDEWEB)

Brodsky, Stanley J.

1998-10-21

We construct new tests of perturbative QCD by considering a hypothetical {tau} lepton of arbitrary mass, which decays hadronically through the electromagnetic current. We can explicitly compute its hadronic width ratio directly as an integral over the e{sup +}e{sup -} annihilation cross section ratio, R{sub e{sup +}e{sup -}}. Furthermore, we can design a set of commensurate scale relations and perturbative QCD tests by varying the weight function away from the form associated with the V-A decay of the physical {tau}. This method allows the wide range of the R{sub e{sup +}e{sup -}} data to be used as a probe of perturbative QCD.

A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition

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Hiromi Daiyasu

2005-01-01

Full Text Available Cellular membrane lipids, of which phospholipids are the major constituents, form one of the characteristic features that distinguish Archaea from other organisms. In this study, we focused on the steps in archaeal phospholipid synthetic pathways that generate polar lipids such as archaetidylserine, archaetidylglycerol, and archaetidylinositol. Only archaetidylserine synthase (ASS, from Methanothermobacter thermautotrophicus, has been experimentally identified. Other enzymes have not been fully examined. Through database searching, we detected many archaeal hypothetical proteins that show sequence similarity to members of the CDP alcohol phosphatidyltransferase family, such as phosphatidylserine synthase (PSS, phosphatidylglycerol synthase (PGS and phosphatidylinositol synthase (PIS derived from Bacteria and Eukarya. The archaeal hypothetical proteins were classified into two groups, based on the sequence similarity. Members of the first group, including ASS from M. thermautotrophicus, were closely related to PSS. The rough agreement between PSS homologue distribution within Archaea and the experimentally identified distribution of archaetidylserine suggested that the hypothetical proteins are ASSs. We found that an open reading frame (ORF tends to be adjacent to that of ASS in the genome, and that the order of the two ORFs is conserved. The sequence similarity of phosphatidylserine decarboxylase to the product of the ORF next to the ASS gene, together with the genomic context conservation, suggests that the ORF encodes archaetidylserine decarboxylase, which may transform archaetidylserine to archaetidylethanolamine. The second group of archaeal hypothetical proteins was related to PGS and PIS. The members of this group were subjected to molecular phylogenetic analysis, together with PGSs and PISs and it was found that they formed two distinct clusters in the molecular phylogenetic tree. The distribution of members of each cluster within Archaea

Gclust Server: 136236 [Gclust Server

Lifescience Database Archive (English)

Full Text Available 136236 NCR_NCU07310 Cluster Sequences - 163 conserved hypothetical protein (transla...tion) (164 aa); no annotation 1 1.00e-80 0.0 0.0 0.0 0.0 0.0 12.5 Show 136236 Cluster ID 136236 Sequence ID

Reducing therapeutic misconception: A randomized intervention trial in hypothetical clinical trials.

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Paul P Christopher

Full Text Available Participants in clinical trials frequently fail to appreciate key differences between research and clinical care. This phenomenon, known as therapeutic misconception, undermines informed consent to clinical research, but to date there have been no effective interventions to reduce it and concerns have been expressed that to do so might impede recruitment. We determined whether a scientific reframing intervention reduces therapeutic misconception without significantly reducing willingness to participate in hypothetical clinical trials.This prospective randomized trial was conducted from 2015 to 2016 to test the efficacy of an informed consent intervention based on scientific reframing compared to a traditional informed consent procedure (control in reducing therapeutic misconception among patients considering enrollment in hypothetical clinical trials modeled on real-world studies for one of five disease categories. Patients with diabetes mellitus, hypertension, coronary artery disease, head/neck cancer, breast cancer, and major depression were recruited from medical clinics and a clinical research volunteer database. The primary outcomes were therapeutic misconception, as measured by a validated, ten-item Therapeutic Misconception Scale (range = 10-50, and willingness to participate in the clinical trial.154 participants completed the study (age range, 23-87 years; 92.3% white, 56.5% female; 74 (48.1% had been randomized to receive the experimental intervention. Therapeutic misconception was significantly lower (p = 0.004 in the scientific reframing group (26.4, 95% CI [23.7 to 29.1] compared to the control group (30.9, 95% CI [28.4 to 33.5], and remained so after controlling for education (p = 0.017. Willingness to participate in the hypothetical trial was not significantly different (p = 0.603 between intervention (52.1%, 95% CI [40.2% to 62.4%] and control (56.3%, 95% CI [45.3% to 66.6%] groups.An enhanced educational intervention augmenting

Analyses of hypothetical FCI's in a fast reactor

International Nuclear Information System (INIS)

Padilla, A. Jr.; Martin, F.J.; Niccoli, L.G.

1981-01-01

Parametric analyses using the SIMMER code were performed to evaluate the potential for a severe recriticality from a pressure-driven recompaction caused by an energetic FCI during the transition phase of a hypothetical accident in a fast reactor. For realistic and reasonable estimates for the assumed accident conditions, a severe recriticality was not predicted. The conditions under which a severe recriticality would be obtained or averted were identified. 10 figures, 2 tables

Flotillin-1 is an evolutionary-conserved memory-related protein up-regulated in implicit and explicit learning paradigms.

Science.gov (United States)

Monje, Francisco J; Divisch, Isabella; Demit, Marvie; Lubec, Gert; Pollak, Daniela D

2013-06-01

Studies of synaptic plasticity using the marine mollusk Aplysia californica as model system have been successfully used to identify proteins involved in learning and memory. The importance of molecular elements regulated by the learning- related neurotransmitter serotonin in Aplysia can then be explored in rodent models and finally tested for their relevance for human physiology and pathology. Herein, 2-DE gel-based electrophoresis has been used to investigate protein level changes after treatment with serotonin in Aplysia abdominal ganglia. Twenty-one proteins have been found to be regulated by serotonin, and protein level changes of actin depolymerizing factor (ADF), deleted in azoospermia associated protein (DAZAP-1), and Flotillin-1 have been verified by Western blotting. Flotillin-1, a member of the flotillin/reggie family of scaffolding proteins, has been previously found to be involved in neuritic branching and synapse formation in hippocampal neurons in vitro. However, its importance for hippocampal- dependent learning and memory in the mouse has not been examined. Here, elevated levels of Flotillin-1 in hippocampal tissue of mice trained in the Morris water maze confirmed the relevance of Flotillin-1 for memory-related processes in a mammalian system. Thus, a translational approach-from invertebrates to rodents-led to the identification of Flotillin-1 as evolutionary-conserved memory-related protein.

Biodiversity gains from efficient use of private sponsorship for flagship species conservation.

Science.gov (United States)

Bennett, Joseph R; Maloney, Richard; Possingham, Hugh P

2015-04-22

To address the global extinction crisis, both efficient use of existing conservation funding and new sources of funding are vital. Private sponsorship of charismatic 'flagship' species conservation represents an important source of new funding, but has been criticized as being inefficient. However, the ancillary benefits of privately sponsored flagship species conservation via actions benefiting other species have not been quantified, nor have the benefits of incorporating such sponsorship into objective prioritization protocols. Here, we use a comprehensive dataset of conservation actions for the 700 most threatened species in New Zealand to examine the potential biodiversity gains from national private flagship species sponsorship programmes. We find that private funding for flagship species can clearly result in additional species and phylogenetic diversity conserved, via conservation actions shared with other species. When private flagship species funding is incorporated into a prioritization protocol to preferentially sponsor shared actions, expected gains can be more than doubled. However, these gains are consistently smaller than expected gains in a hypothetical scenario where private funding could be optimally allocated among all threatened species. We recommend integrating private sponsorship of flagship species into objective prioritization protocols to sponsor efficient actions that maximize biodiversity gains, or wherever possible, encouraging private donations for broader biodiversity goals. © 2015 The Author(s) Published by the Royal Society. All rights reserved.

Conserved host-pathogen PPIs. Globally conserved inter-species bacterial PPIs based conserved host-pathogen interactome derived novel target in C. pseudotuberculosis, C. diphtheriae, M. tuberculosis, C. ulcerans, Y. pestis, and E. coli targeted by Piper betel compounds

DEFF Research Database (Denmark)

Barh, Debmalya; Gupta, Krishnakant; Jain, Neha

2013-01-01

of Caseous Lymphadenitis (CLA). In this study, we used computational approaches to develop common conserved intra-species protein-protein interaction (PPI) networks first time for four Cp strains (Cp FRC41, Cp 316, Cp 3/99-5, and Cp P54B96) followed by development of a common conserved inter...

Interplay between chaperones and protein disorder promotes the evolution of protein networks.

Directory of Open Access Journals (Sweden)

Sebastian Pechmann

2014-06-01

Full Text Available Evolution is driven by mutations, which lead to new protein functions but come at a cost to protein stability. Non-conservative substitutions are of interest in this regard because they may most profoundly affect both function and stability. Accordingly, organisms must balance the benefit of accepting advantageous substitutions with the possible cost of deleterious effects on protein folding and stability. We here examine factors that systematically promote non-conservative mutations at the proteome level. Intrinsically disordered regions in proteins play pivotal roles in protein interactions, but many questions regarding their evolution remain unanswered. Similarly, whether and how molecular chaperones, which have been shown to buffer destabilizing mutations in individual proteins, generally provide robustness during proteome evolution remains unclear. To this end, we introduce an evolutionary parameter λ that directly estimates the rate of non-conservative substitutions. Our analysis of λ in Escherichia coli, Saccharomyces cerevisiae, and Homo sapiens sequences reveals how co- and post-translationally acting chaperones differentially promote non-conservative substitutions in their substrates, likely through buffering of their destabilizing effects. We further find that λ serves well to quantify the evolution of intrinsically disordered proteins even though the unstructured, thus generally variable regions in proteins are often flanked by very conserved sequences. Crucially, we show that both intrinsically disordered proteins and highly re-wired proteins in protein interaction networks, which have evolved new interactions and functions, exhibit a higher λ at the expense of enhanced chaperone assistance. Our findings thus highlight an intricate interplay of molecular chaperones and protein disorder in the evolvability of protein networks. Our results illuminate the role of chaperones in enabling protein evolution, and underline the

EST Table: FY739073 [KAIKOcDNA[Archive

Lifescience Database Archive (English)

Full Text Available FY739073 E_FL_famL_07K17_F_0 11/11/04 35 %/254 aa ref|XP_001600679.1| PREDICTED: si...milar to conserved hypothetical protein [Nasonia vitripennis] 11/11/04 30 %/250 aa FBpp0153473|DgriGH19567-P

Expressed proteins of Herbaspirillum seropedicae in maize (DKB240) roots-bacteria interaction revealed using proteomics.

Science.gov (United States)

Ferrari, Cibele Santos; Amaral, Fernanda Plucani; Bueno, Jessica Cavalheiro Ferreira; Scariot, Mirella Christine; Valentim-Neto, Pedro Alexandre; Arisi, Ana Carolina Maisonnave

2014-11-01

Several molecular tools have been used to clarify the basis of plant-bacteria interaction; however, the mechanism behind the association is still unclear. In this study, we used a proteomic approach to investigate the root proteome of Zea mays (cv. DKB240) inoculated with Herbaspirillum seropedicae strain SmR1 grown in vitro and harvested 7 days after inoculation. Eighteen differentially accumulated proteins were observed in root samples, ten of which were identified by MALDI-TOF mass spectrometry peptide mass fingerprint. Among the identified proteins, we observed three proteins present exclusively in inoculated root samples and six upregulated proteins and one downregulated protein relative to control. Differentially expressed maize proteins were identified as hypothetical protein ZEAMMB73_483204, hypothetical protein ZEAMMB73_269466, and tubulin beta-7 chain. The following were identified as H. seropedicae proteins: peroxiredoxin protein, EF-Tu elongation factor protein, cation transport ATPase, NADPH:quinone oxidoreductase, dinitrogenase reductase, and type III secretion ATP synthase. Our results presented the first evidence of type III secretion ATP synthase expression during H. seropedicae-maize root interaction.

Phylogeny and molecular signatures (conserved proteins and indels that are specific for the Bacteroidetes and Chlorobi species

Directory of Open Access Journals (Sweden)

Lorenzini Emily

2007-05-01

Full Text Available Abstract Background The Bacteroidetes and Chlorobi species constitute two main groups of the Bacteria that are closely related in phylogenetic trees. The Bacteroidetes species are widely distributed and include many important periodontal pathogens. In contrast, all Chlorobi are anoxygenic obligate photoautotrophs. Very few (or no biochemical or molecular characteristics are known that are distinctive characteristics of these bacteria, or are commonly shared by them. Results Systematic blast searches were performed on each open reading frame in the genomes of Porphyromonas gingivalis W83, Bacteroides fragilis YCH46, B. thetaiotaomicron VPI-5482, Gramella forsetii KT0803, Chlorobium luteolum (formerly Pelodictyon luteolum DSM 273 and Chlorobaculum tepidum (formerly Chlorobium tepidum TLS to search for proteins that are uniquely present in either all or certain subgroups of Bacteroidetes and Chlorobi. These studies have identified > 600 proteins for which homologues are not found in other organisms. This includes 27 and 51 proteins that are specific for most of the sequenced Bacteroidetes and Chlorobi genomes, respectively; 52 and 38 proteins that are limited to species from the Bacteroidales and Flavobacteriales orders, respectively, and 5 proteins that are common to species from these two orders; 185 proteins that are specific for the Bacteroides genus. Additionally, 6 proteins that are uniquely shared by species from the Bacteroidetes and Chlorobi phyla (one of them also present in the Fibrobacteres have also been identified. This work also describes two large conserved inserts in DNA polymerase III (DnaE and alanyl-tRNA synthetase that are distinctive characteristics of the Chlorobi species and a 3 aa deletion in ClpB chaperone that is mainly found in various Bacteroidales, Flavobacteriales and Flexebacteraceae, but generally not found in the homologs from other organisms. Phylogenetic analyses of the Bacteroidetes and Chlorobi species is also

Trial of risk assessment of a hypothetical nuclear facility

International Nuclear Information System (INIS)