Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin.
Identifieur interne : 000E22 ( Main/Exploration ); précédent : 000E21; suivant : 000E23Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin.
Auteurs : Martijn A. Huynen [Pays-Bas] ; Chris A E M. Spronk ; Toni Gabald N ; Berend SnelSource :
- FEBS letters [ 0014-5793 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Oxidoreductases.
- métabolisme : Oxidoreductases.
- Conformation des protéines, Glutarédoxines, Génome, Modèles moléculaires, Phylogenèse.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- chemical : Glutaredoxins.
- Genome, Models, Molecular, Phylogeny, Protein Conformation.
Abstract
Genomes, functional genomics data and 3D structure reflect different aspects of protein function. Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these.
DOI: 10.1016/j.febslet.2004.11.111
PubMed: 15670813
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Huynen</name><affiliation wicri:level="1"><nlm:affiliation>CMBI, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Toernooiveld 1, 6525ED Nijmegen, The Netherlands. huynen@cmbi.ru.nl</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CMBI, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Toernooiveld 1, 6525ED Nijmegen</wicri:regionArea><placeName><settlement type="city">Nimègue</settlement><region type="province" nuts="2">Gueldre</region></placeName></affiliation></author><author><name sortKey="Spronk, Chris A E M" sort="Spronk, Chris A E M" uniqKey="Spronk C" first="Chris A E M" last="Spronk">Chris A E M. 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Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15670813</PMID><DateCompleted><Year>2005</Year><Month>04</Month><Day>13</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>579</Volume><Issue>3</Issue><PubDate><Year>2005</Year><Month>Jan</Month><Day>31</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Combining data from genomes, Y2H and 3D structure indicates that BolA is a reductase interacting with a glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>591-6</MedlinePgn></Pagination><Abstract><AbstractText>Genomes, functional genomics data and 3D structure reflect different aspects of protein function. Here, we combine these data to predict that BolA, a widely distributed protein family with unknown function, is a reductase that interacts with a glutaredoxin. Comparisons at the 3D structure level as well as at the sequence profile level indicate homology between BolA and OsmC, an enzyme that reduces organic peroxides. Complementary to this, comparative analyses of genomes and genomics data provide strong evidence of an interaction between BolA and the mono-thiol glutaredoxin family. The interaction between BolA and a mono-thiol glutaredoxin is of particular interest because BolA does not, in contrast to its homolog OsmC, have evolutionarily conserved cysteines to provide it with reducing equivalents. We propose that BolA uses the mono-thiol glutaredoxin as the source for these.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huynen</LastName><ForeName>Martijn A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>CMBI, Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Toernooiveld 1, 6525ED Nijmegen, The Netherlands. huynen@cmbi.ru.nl</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Spronk</LastName><ForeName>Chris A E M</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Gabaldón</LastName><ForeName>Toni</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Snel</LastName><ForeName>Berend</ForeName><Initials>B</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016678" MajorTopicYN="Y">Genome</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>11</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>1</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>4</Month><Day>14</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>1</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15670813</ArticleId><ArticleId IdType="pii">S0014-5793(04)01597-2</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2004.11.111</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pays-Bas</li></country><region><li>Gueldre</li></region><settlement><li>Nimègue</li></settlement></list><tree><noCountry><name sortKey="Gabald N, Toni" sort="Gabald N, Toni" uniqKey="Gabald N T" first="Toni" last="Gabald N">Toni Gabald N</name><name sortKey="Snel, Berend" sort="Snel, Berend" uniqKey="Snel B" first="Berend" last="Snel">Berend Snel</name><name sortKey="Spronk, Chris A E M" sort="Spronk, Chris A E M" uniqKey="Spronk C" first="Chris A E M" last="Spronk">Chris A E M. Spronk</name></noCountry><country name="Pays-Bas"><region name="Gueldre"><name sortKey="Huynen, Martijn A" sort="Huynen, Martijn A" uniqKey="Huynen M" first="Martijn A" last="Huynen">Martijn A. Huynen</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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