PoplarV1, Main, Exploration, bibRecord, 001D21

Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.

Identifieur interne : 001D21 ( Main/Exploration ); précédent : 001D20; suivant : 001D22

Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.

Auteurs : Pierre-Alexandre Lallement [France] ; Edgar Meux [France] ; José M. Gualberto [France] ; Stéphane Dumarcay [France] ; Frédérique Favier [France] ; Claude Didierjean [France] ; Frederick Saul [France] ; Ahmed Haouz [France] ; Mélanie Morel-Rouhier [France] ; Eric Gelhaye [France] ; Nicolas Rouhier [France] ; Arnaud Hecker [France]

Source :

FEBS letters [ 1873-3468 ] ; 2015.

RBID : pubmed:25455804

Descripteurs français

KwdFr :
- Domaine catalytique (MeSH), Multimérisation de protéines (physiologie), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Pliage des protéines (MeSH), Populus (enzymologie), Populus (génétique), Protéines chloroplastiques (composition chimique), Protéines chloroplastiques (génétique), Protéines chloroplastiques (métabolisme).
MESH :
- composition chimique : Oxidoreductases, Protéines chloroplastiques.
- enzymologie : Populus.
- génétique : Oxidoreductases, Populus, Protéines chloroplastiques.
- métabolisme : Oxidoreductases, Protéines chloroplastiques.
- physiologie : Multimérisation de protéines.
- Domaine catalytique, Oxydoréduction, Pliage des protéines.

English descriptors

KwdEn :
- Catalytic Domain (MeSH), Chloroplast Proteins (chemistry), Chloroplast Proteins (genetics), Chloroplast Proteins (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Populus (enzymology), Populus (genetics), Protein Folding (MeSH), Protein Multimerization (physiology).
MESH :
- chemical , chemistry : Chloroplast Proteins, Oxidoreductases.
- chemical , genetics : Chloroplast Proteins, Oxidoreductases.
- chemical , metabolism : Chloroplast Proteins, Oxidoreductases.
- enzymology : Populus.
- genetics : Populus.
- physiology : Protein Multimerization.
- Catalytic Domain, Oxidation-Reduction, Protein Folding.

Abstract

Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms.

DOI: 10.1016/j.febslet.2014.11.021
PubMed: 25455804

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001E95
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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.</title>
<author><name sortKey="Lallement, Pierre Alexandre" sort="Lallement, Pierre Alexandre" uniqKey="Lallement P" first="Pierre-Alexandre" last="Lallement">Pierre-Alexandre Lallement</name>
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<author><name sortKey="Meux, Edgar" sort="Meux, Edgar" uniqKey="Meux E" first="Edgar" last="Meux">Edgar Meux</name>
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<author><name sortKey="Favier, Frederique" sort="Favier, Frederique" uniqKey="Favier F" first="Frédérique" last="Favier">Frédérique Favier</name>
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<author><name sortKey="Saul, Frederick" sort="Saul, Frederick" uniqKey="Saul F" first="Frederick" last="Saul">Frederick Saul</name>
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<wicri:regionArea>Institut Pasteur, Plate-Forme de Cristallographie, CNRS-UMR3528, 75724 Paris</wicri:regionArea>
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<settlement type="city">Paris</settlement>
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<author><name sortKey="Morel Rouhier, Melanie" sort="Morel Rouhier, Melanie" uniqKey="Morel Rouhier M" first="Mélanie" last="Morel-Rouhier">Mélanie Morel-Rouhier</name>
<affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea>
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</placeName>
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<author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
<affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea>
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<orgName type="university">Université de Lorraine</orgName>
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<author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
<affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea>
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<orgName type="university">Université de Lorraine</orgName>
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</author>
<author><name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name>
<affiliation wicri:level="4"><nlm:affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France. Electronic address: arnaud.hecker@univ-lorraine.fr.</nlm:affiliation>
<country xml:lang="fr">France</country>
<wicri:regionArea>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux</wicri:regionArea>
<placeName><region type="region" nuts="2">Grand Est</region>
<region type="old region" nuts="2">Lorraine (région)</region>
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<series><title level="j">FEBS letters</title>
<idno type="eISSN">1873-3468</idno>
<imprint><date when="2015" type="published">2015</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Catalytic Domain (MeSH)</term>
<term>Chloroplast Proteins (chemistry)</term>
<term>Chloroplast Proteins (genetics)</term>
<term>Chloroplast Proteins (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Oxidoreductases (chemistry)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Multimerization (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Domaine catalytique (MeSH)</term>
<term>Multimérisation de protéines (physiologie)</term>
<term>Oxidoreductases (composition chimique)</term>
<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Protéines chloroplastiques (composition chimique)</term>
<term>Protéines chloroplastiques (génétique)</term>
<term>Protéines chloroplastiques (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chloroplast Proteins</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Chloroplast Proteins</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Chloroplast Proteins</term>
<term>Oxidoreductases</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term>
<term>Protéines chloroplastiques</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term>
<term>Populus</term>
<term>Protéines chloroplastiques</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term>
<term>Protéines chloroplastiques</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Multimérisation de protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Multimerization</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term>
<term>Oxidation-Reduction</term>
<term>Protein Folding</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Domaine catalytique</term>
<term>Oxydoréduction</term>
<term>Pliage des protéines</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25455804</PMID>
<DateCompleted><Year>2015</Year>
<Month>02</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2014</Year>
<Month>12</Month>
<Day>22</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>589</Volume>
<Issue>1</Issue>
<PubDate><Year>2015</Year>
<Month>Jan</Month>
<Day>02</Day>
</PubDate>
</JournalIssue>
<Title>FEBS letters</Title>
<ISOAbbreviation>FEBS Lett</ISOAbbreviation>
</Journal>
<ArticleTitle>Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.</ArticleTitle>
<Pagination><MedlinePgn>37-44</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.febslet.2014.11.021</ELocationID>
<ELocationID EIdType="pii" ValidYN="Y">S0014-5793(14)00826-6</ELocationID>
<Abstract><AbstractText>Glutathionyl-hydroquinone reductases (GHRs) catalyze the deglutathionylation of quinones via a catalytic cysteine. The two GHR genes in the Populus trichocarpa genome, Pt-GHR1 and Pt-GHR2, are primarily expressed in reproductive organs. Both proteins are localized in plastids. More specifically, Pt-GHR2 localizes in nucleoids. At the structural level, Pt-GHR1 adopts a typical GHR fold, with a dimerization interface comparable to that of the bacterial and fungal GHR counterparts. Pt-GHR1 catalyzes the deglutathionylation of both reduced and oxidized glutathionylated quinones, but the enzyme is more catalytically efficient with the reduced forms. </AbstractText>
<CopyrightInformation>Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lallement</LastName>
<ForeName>Pierre-Alexandre</ForeName>
<Initials>PA</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Meux</LastName>
<ForeName>Edgar</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gualberto</LastName>
<ForeName>José M</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>Institut de Biologie Moléculaire des Plantes, CNRS-UPR 2357, 67084 Strasbourg, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dumarcay</LastName>
<ForeName>Stéphane</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Laboratoire d'Etudes et de Recherches sur le Matériau Bois, EA 1093, Vandœuvre-lès-Nancy F-54506, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Favier</LastName>
<ForeName>Frédérique</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, CRM(2), Equipe BioMod, UMR 7036, Faculté des Sciences et Technologies, BP 70239, 54506 Vandœuvre-lès-Nancy, France; CNRS, CRM(2), Equipe BioMod, UMR 7036, Faculté des Sciences et Technologies, BP 70239, 54506 Vandœuvre-lès-Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Didierjean</LastName>
<ForeName>Claude</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, CRM(2), Equipe BioMod, UMR 7036, Faculté des Sciences et Technologies, BP 70239, 54506 Vandœuvre-lès-Nancy, France; CNRS, CRM(2), Equipe BioMod, UMR 7036, Faculté des Sciences et Technologies, BP 70239, 54506 Vandœuvre-lès-Nancy, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Saul</LastName>
<ForeName>Frederick</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur, Plate-Forme de Cristallographie, CNRS-UMR3528, 75724 Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Haouz</LastName>
<ForeName>Ahmed</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Institut Pasteur, Plate-Forme de Cristallographie, CNRS-UMR3528, 75724 Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Morel-Rouhier</LastName>
<ForeName>Mélanie</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gelhaye</LastName>
<ForeName>Eric</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rouhier</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hecker</LastName>
<ForeName>Arnaud</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Université de Lorraine, Interactions Arbres - Microorganismes, UMR1136, F-54500 Vandœuvre-lès-Nancy, France; INRA, Interactions Arbres - Microorganismes, UMR1136, F-54280 Champenoux, France. Electronic address: arnaud.hecker@univ-lorraine.fr.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>11</Month>
<Day>29</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>FEBS Lett</MedlineTA>
<NlmUniqueID>0155157</NlmUniqueID>
<ISSNLinking>0014-5793</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D060365">Chloroplast Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
<NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060365" MajorTopicYN="N">Chloroplast Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017510" MajorTopicYN="Y">Protein Folding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Deglutathionylation</Keyword>
<Keyword MajorTopicYN="N">Glutathione transferase</Keyword>
<Keyword MajorTopicYN="N">Plastid</Keyword>
<Keyword MajorTopicYN="N">Poplar</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year>
<Month>07</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2014</Year>
<Month>11</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2014</Year>
<Month>11</Month>
<Day>15</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2014</Year>
<Month>12</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="pubmed"><Year>2014</Year>
<Month>12</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2015</Year>
<Month>2</Month>
<Day>18</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
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<ArticleIdList><ArticleId IdType="pubmed">25455804</ArticleId>
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<ArticleId IdType="doi">10.1016/j.febslet.2014.11.021</ArticleId>
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<affiliations><list><country><li>France</li>
</country>
<region><li>Alsace (région administrative)</li>
<li>Grand Est</li>
<li>Lorraine (région)</li>
<li>Île-de-France</li>
</region>
<settlement><li>Champenoux</li>
<li>Paris</li>
<li>Strasbourg</li>
<li>Vandœuvre-lès-Nancy</li>
</settlement>
<orgName><li>Université de Lorraine</li>
</orgName>
</list>
<tree><country name="France"><region name="Grand Est"><name sortKey="Lallement, Pierre Alexandre" sort="Lallement, Pierre Alexandre" uniqKey="Lallement P" first="Pierre-Alexandre" last="Lallement">Pierre-Alexandre Lallement</name>
</region>
<name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name>
<name sortKey="Dumarcay, Stephane" sort="Dumarcay, Stephane" uniqKey="Dumarcay S" first="Stéphane" last="Dumarcay">Stéphane Dumarcay</name>
<name sortKey="Favier, Frederique" sort="Favier, Frederique" uniqKey="Favier F" first="Frédérique" last="Favier">Frédérique Favier</name>
<name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name>
<name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M" last="Gualberto">José M. Gualberto</name>
<name sortKey="Haouz, Ahmed" sort="Haouz, Ahmed" uniqKey="Haouz A" first="Ahmed" last="Haouz">Ahmed Haouz</name>
<name sortKey="Hecker, Arnaud" sort="Hecker, Arnaud" uniqKey="Hecker A" first="Arnaud" last="Hecker">Arnaud Hecker</name>
<name sortKey="Meux, Edgar" sort="Meux, Edgar" uniqKey="Meux E" first="Edgar" last="Meux">Edgar Meux</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="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name>
<name sortKey="Saul, Frederick" sort="Saul, Frederick" uniqKey="Saul F" first="Frederick" last="Saul">Frederick Saul</name>
</country>
</tree>
</affiliations>
</record>

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Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.

Glutathionyl-hydroquinone reductases from poplar are plastidial proteins that deglutathionylate both reduced and oxidized glutathionylated quinones.

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