Thioredoxins and glutaredoxins: unifying elements in redox biology.
Identifieur interne : 000A67 ( Main/Exploration ); précédent : 000A66; suivant : 000A68Thioredoxins and glutaredoxins: unifying elements in redox biology.
Auteurs : Yves Meyer [France] ; Bob B. Buchanan ; Florence Vignols ; Jean-Philippe ReichheldSource :
- Annual review of genetics [ 1545-2948 ] ; 2009.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Escherichia coli, Saccharomyces cerevisiae.
- métabolisme : Glutarédoxines, Mammifères, Thiorédoxines.
- Animaux, Humains, Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutaredoxins, Thioredoxins.
- enzymology : Escherichia coli, Saccharomyces cerevisiae.
- metabolism : Mammals.
- Animals, Humans, Oxidation-Reduction.
Abstract
Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.
DOI: 10.1146/annurev-genet-102108-134201
PubMed: 19691428
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Buchanan</name></author><author><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name></author><author><name sortKey="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19691428</idno><idno type="pmid">19691428</idno><idno type="doi">10.1146/annurev-genet-102108-134201</idno><idno type="wicri:Area/Main/Corpus">000A85</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000A85</idno><idno type="wicri:Area/Main/Curation">000A85</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000A85</idno><idno type="wicri:Area/Main/Exploration">000A85</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thioredoxins and glutaredoxins: unifying elements in redox biology.</title><author><name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</name><affiliation wicri:level="3"><nlm:affiliation>Université de Perpignan, Génome et dévelopement des plantes, CNRS-UP-IRD UMR 5096, F 66860 Perpignan Cedex, France. ymeyer@univ-perp.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Perpignan, Génome et dévelopement des plantes, CNRS-UP-IRD UMR 5096, F 66860 Perpignan Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Occitanie (région administrative)</region><region type="old region" nuts="2">Languedoc-Roussillon</region><settlement type="city">Perpignan</settlement></placeName></affiliation></author><author><name sortKey="Buchanan, Bob B" sort="Buchanan, Bob B" uniqKey="Buchanan B" first="Bob B" last="Buchanan">Bob B. 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Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19691428</PMID><DateCompleted><Year>2009</Year><Month>12</Month><Day>11</Day></DateCompleted><DateRevised><Year>2009</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1545-2948</ISSN><JournalIssue CitedMedium="Internet"><Volume>43</Volume><PubDate><Year>2009</Year></PubDate></JournalIssue><Title>Annual review of genetics</Title><ISOAbbreviation>Annu Rev Genet</ISOAbbreviation></Journal><ArticleTitle>Thioredoxins and glutaredoxins: unifying elements in redox biology.</ArticleTitle><Pagination><MedlinePgn>335-67</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1146/annurev-genet-102108-134201</ELocationID><Abstract><AbstractText>Since their discovery as a substrate for ribonucleotide reductase (RNR), the role of thioredoxin (Trx) and glutaredoxin (Grx) has been largely extended through their regulatory function. Both proteins act by changing the structure and activity of a broad spectrum of target proteins, typically by modifying redox status. Trx and Grx are members of families with multiple and partially redundant genes. The number of genes clearly increased with the appearance of multicellular organisms, in part because of new types of Trx and Grx with orthologs throughout the animal and plant kingdoms. The function of Trx and Grx also broadened as cells achieved increased complexity, especially in the regulation arena. In view of these progressive changes, the ubiquitous distribution of Trx and the wide occurrence of Grx enable these proteins to serve as indicators of the evolutionary history of redox regulation. In so doing, they add a unifying element that links the diverse forms of life to one another in an uninterrupted continuum. It is anticipated that future research will embellish this continuum and further elucidate the properties of these proteins and their impact on biology. The new information will be important not only to our understanding of the role of Trx and Grx in fundamental cell processes but also to future societal benefits as the proteins find new applications in a range of fields.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Yves</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Université de Perpignan, Génome et dévelopement des plantes, CNRS-UP-IRD UMR 5096, F 66860 Perpignan Cedex, France. ymeyer@univ-perp.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Buchanan</LastName><ForeName>Bob B</ForeName><Initials>BB</Initials></Author><Author ValidYN="Y"><LastName>Vignols</LastName><ForeName>Florence</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Reichheld</LastName><ForeName>Jean-Philippe</ForeName><Initials>JP</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Annu Rev Genet</MedlineTA><NlmUniqueID>0117605</NlmUniqueID><ISSNLinking>0066-4197</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008322" MajorTopicYN="N">Mammals</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>232</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>8</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>8</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>12</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19691428</ArticleId><ArticleId IdType="doi">10.1146/annurev-genet-102108-134201</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Languedoc-Roussillon</li><li>Occitanie (région administrative)</li></region><settlement><li>Perpignan</li></settlement></list><tree><noCountry><name sortKey="Buchanan, Bob B" sort="Buchanan, Bob B" uniqKey="Buchanan B" first="Bob B" last="Buchanan">Bob B. Buchanan</name><name sortKey="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name></noCountry><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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