Putative roles of glutaredoxin-BolA holo-heterodimers in plants.
Identifieur interne : 000623 ( Main/Exploration ); précédent : 000622; suivant : 000624Putative roles of glutaredoxin-BolA holo-heterodimers in plants.
Auteurs : Tiphaine Dhalleine [France] ; Nicolas Rouhier [France] ; Jérémy Couturier [France]Source :
- Plant signaling & behavior [ 1559-2324 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Arabidopsis, Glutarédoxines, Protéines d'Arabidopsis, Protéines de liaison à l'ADN.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Arabidopsis Proteins, DNA-Binding Proteins, Glutaredoxins.
- metabolism : Arabidopsis.
Abstract
Several genomic analyses, high-throughput or targeted interaction studies including the purification of protein complexes indicated a physical and functional link between BolAs and monothiol glutaredoxins (Grxs) that is conserved both in prokaryotes and eukaryotes. In a recent work, we confirmed that several Arabidopsis protein couples, used as plant representatives, also physically interact. More interestingly, we determined that two BolA proteins, BolA2 and SufE1, contain a conserved cysteine that is sensitive to oxidizing treatments, unraveling a possible redox-control of BolA2 and SufE1 by monothiol glutaredoxins. By coexpressing physiological partners in E. coli, Grx-BolA heterodimers binding a labile, oxygen sensitive iron-sulfur cluster were isolated. Altogether, these results illustrate the existence of different modes of interaction between monothiol glutaredoxins and BolA proteins in plants and probably in other organisms. Incidentally, the function of each partner could be differentially modulated depending on the type of interaction.
DOI: 10.4161/psb.28564
PubMed: 24714563
PubMed Central: PMC4091568
Affiliations:
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Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:regionArea><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion></affiliation></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:regionArea><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion></affiliation></author><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="1"><nlm:affiliation>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:regionArea><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion><wicri:noRegion>France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux</wicri:noRegion></affiliation></author></analytic><series><title level="j">Plant signaling & behavior</title><idno type="eISSN">1559-2324</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (metabolism)</term><term>Arabidopsis Proteins (metabolism)</term><term>DNA-Binding Proteins (metabolism)</term><term>Glutaredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Protéines de liaison à l'ADN (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>DNA-Binding Proteins</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Glutarédoxines</term><term>Protéines d'Arabidopsis</term><term>Protéines de liaison à l'ADN</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Several genomic analyses, high-throughput or targeted interaction studies including the purification of protein complexes indicated a physical and functional link between BolAs and monothiol glutaredoxins (Grxs) that is conserved both in prokaryotes and eukaryotes. In a recent work, we confirmed that several Arabidopsis protein couples, used as plant representatives, also physically interact. More interestingly, we determined that two BolA proteins, BolA2 and SufE1, contain a conserved cysteine that is sensitive to oxidizing treatments, unraveling a possible redox-control of BolA2 and SufE1 by monothiol glutaredoxins. By coexpressing physiological partners in E. coli, Grx-BolA heterodimers binding a labile, oxygen sensitive iron-sulfur cluster were isolated. Altogether, these results illustrate the existence of different modes of interaction between monothiol glutaredoxins and BolA proteins in plants and probably in other organisms. Incidentally, the function of each partner could be differentially modulated depending on the type of interaction. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24714563</PMID><DateCompleted><Year>2015</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1559-2324</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>3</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Plant signaling & behavior</Title><ISOAbbreviation>Plant Signal Behav</ISOAbbreviation></Journal><ArticleTitle>Putative roles of glutaredoxin-BolA holo-heterodimers in plants.</ArticleTitle><Pagination><MedlinePgn>e28564</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">28564</ELocationID><Abstract><AbstractText>Several genomic analyses, high-throughput or targeted interaction studies including the purification of protein complexes indicated a physical and functional link between BolAs and monothiol glutaredoxins (Grxs) that is conserved both in prokaryotes and eukaryotes. In a recent work, we confirmed that several Arabidopsis protein couples, used as plant representatives, also physically interact. More interestingly, we determined that two BolA proteins, BolA2 and SufE1, contain a conserved cysteine that is sensitive to oxidizing treatments, unraveling a possible redox-control of BolA2 and SufE1 by monothiol glutaredoxins. By coexpressing physiological partners in E. coli, Grx-BolA heterodimers binding a labile, oxygen sensitive iron-sulfur cluster were isolated. Altogether, these results illustrate the existence of different modes of interaction between monothiol glutaredoxins and BolA proteins in plants and probably in other organisms. Incidentally, the function of each partner could be differentially modulated depending on the type of interaction. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dhalleine</LastName><ForeName>Tiphaine</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; 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; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Université de Lorraine; Interactions Arbres - Microorganismes; UMR1136; Vandoeuvre-lès-Nancy, France; INRA; Interactions Arbres - Microorganismes; UMR1136; Champenoux, France.</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>04</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Signal Behav</MedlineTA><NlmUniqueID>101291431</NlmUniqueID><ISSNLinking>1559-2316</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C509435">At4g26500 protein, 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