One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.
Identifieur interne : 000040 ( Main/Exploration ); précédent : 000039; suivant : 000041One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.
Auteurs : Jannik Zimmermann [Allemagne] ; Julian Oestreicher [Allemagne] ; Steffen Hess [Allemagne] ; Johannes M. Herrmann [Allemagne] ; Marcel Deponte [Allemagne] ; Bruce Morgan [Allemagne]Source :
- Redox biology [ 2213-2317 ] ; 2020.
Abstract
Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies. Class I glutaredoxins are glutathione-dependent thiol-disulfide oxidoreductases whilst class II glutaredoxins coordinate Fe-S clusters. Class I glutaredoxins are typically dithiol enzymes with two active-site cysteine residues, however, some enzymatically active monothiol glutaredoxins are also known. Whilst both monothiol and dithiol class I glutaredoxins mediate protein deglutathionylation, it is widely claimed that only dithiol glutaredoxins are competent to reduce protein disulfide bonds. In this study, using a combination of yeast 'viability rescue', growth, and redox-sensitive GFP-based assays, we show that two different monothiol class I glutaredoxins can each facilitate the reduction of protein disulfide bonds in ribonucleotide reductase, methionine sulfoxide reductase and roGFP2. Our observations thus challenge the generalization of the dithiol mechanism for glutaredoxin catalysis and raise the question of why most class I glutaredoxins have two active-site cysteine residues.
DOI: 10.1016/j.redox.2020.101598
PubMed: 32521506
PubMed Central: PMC7286987
Affiliations:
- Allemagne
- Rhénanie-Palatinat, Sarre (Land)
- Kaiserslautern, Sarrebruck
- Université technique de Kaiserslautern
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.</title><author><name sortKey="Zimmermann, Jannik" sort="Zimmermann, Jannik" uniqKey="Zimmermann J" first="Jannik" last="Zimmermann">Jannik Zimmermann</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author><author><name sortKey="Oestreicher, Julian" sort="Oestreicher, Julian" uniqKey="Oestreicher J" first="Julian" last="Oestreicher">Julian Oestreicher</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author><author><name sortKey="Hess, Steffen" sort="Hess, Steffen" uniqKey="Hess S" first="Steffen" last="Hess">Steffen Hess</name><affiliation wicri:level="4"><nlm:affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Cell Biology, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Herrmann, Johannes M" sort="Herrmann, Johannes M" uniqKey="Herrmann J" first="Johannes M" last="Herrmann">Johannes M. Herrmann</name><affiliation wicri:level="4"><nlm:affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Cell Biology, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Chemistry, Department of Biochemistry, University of Kaiserslautern, Kaiserslautern, Germany. Electronic address: deponte@chemie.uni-kl.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Faculty of Chemistry, Department of Biochemistry, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany. Electronic address: bruce.morgan@uni-saarland.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32521506</idno><idno type="pmid">32521506</idno><idno type="doi">10.1016/j.redox.2020.101598</idno><idno type="pmc">PMC7286987</idno><idno type="wicri:Area/Main/Corpus">000048</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000048</idno><idno type="wicri:Area/Main/Curation">000048</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000048</idno><idno type="wicri:Area/Main/Exploration">000048</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.</title><author><name sortKey="Zimmermann, Jannik" sort="Zimmermann, Jannik" uniqKey="Zimmermann J" first="Jannik" last="Zimmermann">Jannik Zimmermann</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author><author><name sortKey="Oestreicher, Julian" sort="Oestreicher, Julian" uniqKey="Oestreicher J" first="Julian" last="Oestreicher">Julian Oestreicher</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author><author><name sortKey="Hess, Steffen" sort="Hess, Steffen" uniqKey="Hess S" first="Steffen" last="Hess">Steffen Hess</name><affiliation wicri:level="4"><nlm:affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Cell Biology, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Herrmann, Johannes M" sort="Herrmann, Johannes M" uniqKey="Herrmann J" first="Johannes M" last="Herrmann">Johannes M. Herrmann</name><affiliation wicri:level="4"><nlm:affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Cell Biology, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Chemistry, Department of Biochemistry, University of Kaiserslautern, Kaiserslautern, Germany. Electronic address: deponte@chemie.uni-kl.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Faculty of Chemistry, Department of Biochemistry, University of Kaiserslautern, Kaiserslautern</wicri:regionArea><placeName><region type="land" nuts="2">Rhénanie-Palatinat</region><settlement type="city">Kaiserslautern</settlement></placeName><orgName type="university">Université technique de Kaiserslautern</orgName></affiliation></author><author><name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name><affiliation wicri:level="3"><nlm:affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany. Electronic address: bruce.morgan@uni-saarland.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken</wicri:regionArea><placeName><region type="land" nuts="2">Sarre (Land)</region><settlement type="city">Sarrebruck</settlement></placeName></affiliation></author></analytic><series><title level="j">Redox biology</title><idno type="eISSN">2213-2317</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies. Class I glutaredoxins are glutathione-dependent thiol-disulfide oxidoreductases whilst class II glutaredoxins coordinate Fe-S clusters. Class I glutaredoxins are typically dithiol enzymes with two active-site cysteine residues, however, some enzymatically active monothiol glutaredoxins are also known. Whilst both monothiol and dithiol class I glutaredoxins mediate protein deglutathionylation, it is widely claimed that only dithiol glutaredoxins are competent to reduce protein disulfide bonds. In this study, using a combination of yeast 'viability rescue', growth, and redox-sensitive GFP-based assays, we show that two different monothiol class I glutaredoxins can each facilitate the reduction of protein disulfide bonds in ribonucleotide reductase, methionine sulfoxide reductase and roGFP2. Our observations thus challenge the generalization of the dithiol mechanism for glutaredoxin catalysis and raise the question of why most class I glutaredoxins have two active-site cysteine residues.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32521506</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2213-2317</ISSN><JournalIssue CitedMedium="Internet"><Volume>36</Volume><PubDate><Year>2020</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Redox biology</Title><ISOAbbreviation>Redox Biol</ISOAbbreviation></Journal><ArticleTitle>One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.</ArticleTitle><Pagination><MedlinePgn>101598</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S2213-2317(20)30548-6</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.redox.2020.101598</ELocationID><Abstract><AbstractText>Glutaredoxins are small proteins of the thioredoxin superfamily that are present throughout life. Most glutaredoxins fall into two major subfamilies. Class I glutaredoxins are glutathione-dependent thiol-disulfide oxidoreductases whilst class II glutaredoxins coordinate Fe-S clusters. Class I glutaredoxins are typically dithiol enzymes with two active-site cysteine residues, however, some enzymatically active monothiol glutaredoxins are also known. Whilst both monothiol and dithiol class I glutaredoxins mediate protein deglutathionylation, it is widely claimed that only dithiol glutaredoxins are competent to reduce protein disulfide bonds. In this study, using a combination of yeast 'viability rescue', growth, and redox-sensitive GFP-based assays, we show that two different monothiol class I glutaredoxins can each facilitate the reduction of protein disulfide bonds in ribonucleotide reductase, methionine sulfoxide reductase and roGFP2. Our observations thus challenge the generalization of the dithiol mechanism for glutaredoxin catalysis and raise the question of why most class I glutaredoxins have two active-site cysteine residues.</AbstractText><CopyrightInformation>Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zimmermann</LastName><ForeName>Jannik</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oestreicher</LastName><ForeName>Julian</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hess</LastName><ForeName>Steffen</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Johannes M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Cell Biology, University of Kaiserslautern, Kaiserslautern, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Deponte</LastName><ForeName>Marcel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Faculty of Chemistry, Department of Biochemistry, University of Kaiserslautern, Kaiserslautern, Germany. Electronic address: deponte@chemie.uni-kl.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morgan</LastName><ForeName>Bruce</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Zentrum für Human- und Molekularbiologie (ZHMB), Saarland University, Saarbrücken, Germany. Electronic address: bruce.morgan@uni-saarland.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>05</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Redox Biol</MedlineTA><NlmUniqueID>101605639</NlmUniqueID><ISSNLinking>2213-2317</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutaredoxins</Keyword><Keyword MajorTopicYN="N">Protein disulfide</Keyword><Keyword MajorTopicYN="N">Redox catalysis</Keyword><Keyword MajorTopicYN="N">Thioredoxins</Keyword><Keyword MajorTopicYN="N">roGFP2</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>04</Month><Day>07</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>05</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>05</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>6</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>6</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>6</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32521506</ArticleId><ArticleId IdType="pii">S2213-2317(20)30548-6</ArticleId><ArticleId IdType="doi">10.1016/j.redox.2020.101598</ArticleId><ArticleId IdType="pmc">PMC7286987</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Rhénanie-Palatinat</li><li>Sarre (Land)</li></region><settlement><li>Kaiserslautern</li><li>Sarrebruck</li></settlement><orgName><li>Université technique de Kaiserslautern</li></orgName></list><tree><country name="Allemagne"><region name="Sarre (Land)"><name sortKey="Zimmermann, Jannik" sort="Zimmermann, Jannik" uniqKey="Zimmermann J" first="Jannik" last="Zimmermann">Jannik Zimmermann</name></region><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><name sortKey="Herrmann, Johannes M" sort="Herrmann, Johannes M" uniqKey="Herrmann J" first="Johannes M" last="Herrmann">Johannes M. Herrmann</name><name sortKey="Hess, Steffen" sort="Hess, Steffen" uniqKey="Hess S" first="Steffen" last="Hess">Steffen Hess</name><name sortKey="Morgan, Bruce" sort="Morgan, Bruce" uniqKey="Morgan B" first="Bruce" last="Morgan">Bruce Morgan</name><name sortKey="Oestreicher, Julian" sort="Oestreicher, Julian" uniqKey="Oestreicher J" first="Julian" last="Oestreicher">Julian Oestreicher</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000040 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000040 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:32521506
|texte= One cysteine is enough: A monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:32521506" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |