Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems.
Identifieur interne : 000F24 ( Main/Exploration ); précédent : 000F23; suivant : 000F25Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems.
Auteurs : Eleanor W. Trotter [Royaume-Uni] ; Chris M. GrantSource :
- EMBO reports [ 1469-221X ] ; 2003.
Descripteurs français
- KwdFr :
- Glutarédoxines (MeSH), Glutathion (métabolisme), Glutathione reductase (génétique), Glutathione reductase (métabolisme), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Thioredoxin reductase 1 (MeSH), Thioredoxin-disulfide reductase (génétique), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- croissance et développement : Saccharomyces cerevisiae.
- génétique : Glutathione reductase, Saccharomyces cerevisiae, Thioredoxin-disulfide reductase.
- métabolisme : Glutathion, Glutathione reductase, Protéines, Saccharomyces cerevisiae, Thioredoxin-disulfide reductase, Thiorédoxines.
- Glutarédoxines, Oxidoreductases, Oxydoréduction, Thioredoxin reductase 1.
English descriptors
- KwdEn :
- Glutaredoxins (MeSH), Glutathione (metabolism), Glutathione Reductase (genetics), Glutathione Reductase (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Proteins (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Thioredoxin Reductase 1 (MeSH), Thioredoxin-Disulfide Reductase (genetics), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , genetics : Glutathione Reductase, Thioredoxin-Disulfide Reductase.
- chemical , metabolism : Glutathione, Glutathione Reductase, Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical : Glutaredoxins, Oxidoreductases, Thioredoxin Reductase 1.
- genetics : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Oxidation-Reduction.
Abstract
Our studies in yeast show that there is an essential requirement for either an active thioredoxin or an active glutathione (GSH)-glutaredoxin system for cell viability. Glutathione reductase (Glr1) and thioredoxin reductase (Trr1) are key regulatory enzymes that determine the redox state of the GSH-glutaredoxin and thioredoxin systems, respectively. Here we show that Trr1 is required during normal cell growth, whereas there is no apparent requirement for Glr1. Analysis of the redox state of thioredoxins and glutaredoxins in glr1 and trr1 mutants reveals that thioredoxins are maintained independently of the glutathione system. In contrast, there is a strong correlation between the redox state of glutaredoxins and the oxidation state of the GSSG/2GSH redox couple. We suggest that independent redox regulation of thioredoxins enables cells to survive in conditions under which the GSH-glutaredoxin system is oxidized.
DOI: 10.1038/sj.embor.embor729
PubMed: 12612609
PubMed Central: PMC1315827
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Trotter</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, PO Box 88, Manchester M60 1QD, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, PO Box 88, Manchester M60 1QD</wicri:regionArea><wicri:noRegion>Manchester M60 1QD</wicri:noRegion></affiliation></author><author><name sortKey="Grant, Chris M" sort="Grant, Chris M" uniqKey="Grant C" first="Chris M" last="Grant">Chris M. 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Glutathione reductase (Glr1) and thioredoxin reductase (Trr1) are key regulatory enzymes that determine the redox state of the GSH-glutaredoxin and thioredoxin systems, respectively. Here we show that Trr1 is required during normal cell growth, whereas there is no apparent requirement for Glr1. Analysis of the redox state of thioredoxins and glutaredoxins in glr1 and trr1 mutants reveals that thioredoxins are maintained independently of the glutathione system. In contrast, there is a strong correlation between the redox state of glutaredoxins and the oxidation state of the GSSG/2GSH redox couple. We suggest that independent redox regulation of thioredoxins enables cells to survive in conditions under which the GSH-glutaredoxin system is oxidized.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12612609</PMID><DateCompleted><Year>2003</Year><Month>08</Month><Day>11</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1469-221X</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><Issue>2</Issue><PubDate><Year>2003</Year><Month>Feb</Month></PubDate></JournalIssue><Title>EMBO reports</Title><ISOAbbreviation>EMBO Rep</ISOAbbreviation></Journal><ArticleTitle>Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems.</ArticleTitle><Pagination><MedlinePgn>184-8</MedlinePgn></Pagination><Abstract><AbstractText>Our studies in yeast show that there is an essential requirement for either an active thioredoxin or an active glutathione (GSH)-glutaredoxin system for cell viability. Glutathione reductase (Glr1) and thioredoxin reductase (Trr1) are key regulatory enzymes that determine the redox state of the GSH-glutaredoxin and thioredoxin systems, respectively. Here we show that Trr1 is required during normal cell growth, whereas there is no apparent requirement for Glr1. Analysis of the redox state of thioredoxins and glutaredoxins in glr1 and trr1 mutants reveals that thioredoxins are maintained independently of the glutathione system. In contrast, there is a strong correlation between the redox state of glutaredoxins and the oxidation state of the GSSG/2GSH redox couple. We suggest that independent redox regulation of thioredoxins enables cells to survive in conditions under which the GSH-glutaredoxin system is oxidized.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Trotter</LastName><ForeName>Eleanor W</ForeName><Initials>EW</Initials><AffiliationInfo><Affiliation>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, PO Box 88, Manchester M60 1QD, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grant</LastName><ForeName>Chris M</ForeName><Initials>CM</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>EMBO 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Grant</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Trotter, Eleanor W" sort="Trotter, Eleanor W" uniqKey="Trotter E" first="Eleanor W" last="Trotter">Eleanor W. Trotter</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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