Oxidized glutathione promotes association between Eukaryotic Translation Elongation Factor 1Bγ and Ure2p glutathione transferase from Phanerochaete chrysosporium.
Identifieur interne : 000016 ( Main/Exploration ); précédent : 000015; suivant : 000017Oxidized glutathione promotes association between Eukaryotic Translation Elongation Factor 1Bγ and Ure2p glutathione transferase from Phanerochaete chrysosporium.
Auteurs : Raphael Bchini [France] ; Jean-Michel Girardet [France] ; Rodnay Sormani [France] ; Eric Gelhaye [France] ; Mélanie Morel-Rouhier [France]Source :
- The FEBS journal [ 1742-4658 ] ; 2020.
Abstract
The Eukaryotic Translation Elongation Factor 1Bγ (eEF1Bγ) is an atypical member of the glutathione transferase (GST) superfamily. Contrary to more classical GSTs having a role in toxic compound detoxification, eEF1Bγ is suggested to act as a scaffold protein, anchoring the elongation factor complex EF1B to the endoplasmic reticulum. In this study we show that eEF1Bγ from the basidiomycete Phanerochaete chrysosporium is fully active as a glutathione transferase in vitro and undergoes conformational changes upon binding of oxidized glutathione. Using real-time analyses of biomolecular interactions, we show that GSSG allows eEF1Bγ to physically interact with other GSTs from the Ure2p class, opening new perspectives for a better understanding of the role of eEF1Bγ in cellular oxidative stress response.
DOI: 10.1111/febs.15614
PubMed: 33124131
Affiliations:
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Contrary to more classical GSTs having a role in toxic compound detoxification, eEF1Bγ is suggested to act as a scaffold protein, anchoring the elongation factor complex EF1B to the endoplasmic reticulum. In this study we show that eEF1Bγ from the basidiomycete Phanerochaete chrysosporium is fully active as a glutathione transferase in vitro and undergoes conformational changes upon binding of oxidized glutathione. Using real-time analyses of biomolecular interactions, we show that GSSG allows eEF1Bγ to physically interact with other GSTs from the Ure2p class, opening new perspectives for a better understanding of the role of eEF1Bγ in cellular oxidative stress response.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33124131</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1742-4658</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>30</Day></PubDate></JournalIssue><Title>The FEBS journal</Title><ISOAbbreviation>FEBS J</ISOAbbreviation></Journal><ArticleTitle>Oxidized glutathione promotes association between Eukaryotic Translation Elongation Factor 1Bγ and Ure2p glutathione transferase from Phanerochaete chrysosporium.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/febs.15614</ELocationID><Abstract><AbstractText>The Eukaryotic Translation Elongation Factor 1Bγ (eEF1Bγ) is an atypical member of the glutathione transferase (GST) superfamily. Contrary to more classical GSTs having a role in toxic compound detoxification, eEF1Bγ is suggested to act as a scaffold protein, anchoring the elongation factor complex EF1B to the endoplasmic reticulum. In this study we show that eEF1Bγ from the basidiomycete Phanerochaete chrysosporium is fully active as a glutathione transferase in vitro and undergoes conformational changes upon binding of oxidized glutathione. Using real-time analyses of biomolecular interactions, we show that GSSG allows eEF1Bγ to physically interact with other GSTs from the Ure2p class, opening new perspectives for a better understanding of the role of eEF1Bγ in cellular oxidative stress response.</AbstractText><CopyrightInformation>This article is protected by copyright. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bchini</LastName><ForeName>Raphael</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Université de Lorraine INRAE, Interactions Arbres/Micro-organismes (IAM), UMR 1136, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Girardet</LastName><ForeName>Jean-Michel</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Université de Lorraine INRAE, Interactions Arbres/Micro-organismes (IAM), UMR 1136, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sormani</LastName><ForeName>Rodnay</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Université de Lorraine INRAE, Interactions Arbres/Micro-organismes (IAM), UMR 1136, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Université de Lorraine INRAE, Interactions Arbres/Micro-organismes (IAM), UMR 1136, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morel-Rouhier</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-5149-0474</Identifier><AffiliationInfo><Affiliation>Université de Lorraine INRAE, Interactions Arbres/Micro-organismes (IAM), UMR 1136, F-54000, Nancy, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS J</MedlineTA><NlmUniqueID>101229646</NlmUniqueID><ISSNLinking>1742-464X</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">GSSG</Keyword><Keyword MajorTopicYN="N">eEF1Bγ</Keyword><Keyword MajorTopicYN="N">glutathione transferase</Keyword><Keyword MajorTopicYN="N">time-resolved molecular dynamics</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>06</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>09</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>10</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>30</Day><Hour>6</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33124131</ArticleId><ArticleId IdType="doi">10.1111/febs.15614</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement></list><tree><country name="France"><region name="Grand Est"><name sortKey="Bchini, Raphael" sort="Bchini, Raphael" uniqKey="Bchini R" first="Raphael" last="Bchini">Raphael Bchini</name></region><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Girardet, Jean Michel" sort="Girardet, Jean Michel" uniqKey="Girardet J" first="Jean-Michel" last="Girardet">Jean-Michel Girardet</name><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name><name sortKey="Sormani, Rodnay" sort="Sormani, Rodnay" uniqKey="Sormani R" first="Rodnay" last="Sormani">Rodnay Sormani</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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