Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1.
Identifieur interne : 000636 ( Main/Exploration ); précédent : 000635; suivant : 000637Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1.
Auteurs : Jérémy Couturier [France] ; Hui-Chen Wu ; Tiphaine Dhalleine ; Henri Pégeot ; Damien Sudre ; José M. Gualberto ; Jean-Pierre Jacquot ; Frédéric Gaymard ; Florence Vignols ; Nicolas RouhierSource :
- Molecular plant [ 1752-9867 ] ; 2014.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Arabidopsis (cytologie), Arabidopsis (enzymologie), Arabidopsis (métabolisme), Domaine catalytique (MeSH), Espace intracellulaire (métabolisme), Glutarédoxines (métabolisme), Liaison aux protéines (MeSH), Oxydoréduction (MeSH), Photosynthèse (MeSH), Phylogenèse (MeSH), Protéines d'Arabidopsis (composition chimique), Protéines d'Arabidopsis (métabolisme), Protéines de liaison à l'ADN (composition chimique), Protéines de liaison à l'ADN (métabolisme), Sulfurtransferases (métabolisme), Séquence conservée (MeSH), Transport des protéines (MeSH).
- MESH :
- composition chimique : Protéines d'Arabidopsis, Protéines de liaison à l'ADN.
- cytologie : Arabidopsis.
- enzymologie : Arabidopsis.
- métabolisme : Arabidopsis, Espace intracellulaire, Glutarédoxines, Protéines d'Arabidopsis, Protéines de liaison à l'ADN, Sulfurtransferases.
- Activation enzymatique, Domaine catalytique, Liaison aux protéines, Oxydoréduction, Photosynthèse, Phylogenèse, Séquence conservée, Transport des protéines.
English descriptors
- KwdEn :
- Arabidopsis (cytology), Arabidopsis (enzymology), Arabidopsis (metabolism), Arabidopsis Proteins (chemistry), Arabidopsis Proteins (metabolism), Catalytic Domain (MeSH), Conserved Sequence (MeSH), DNA-Binding Proteins (chemistry), DNA-Binding Proteins (metabolism), Enzyme Activation (MeSH), Glutaredoxins (metabolism), Intracellular Space (metabolism), Oxidation-Reduction (MeSH), Photosynthesis (MeSH), Phylogeny (MeSH), Protein Binding (MeSH), Protein Transport (MeSH), Sulfurtransferases (metabolism).
- MESH :
- chemical , chemistry : Arabidopsis Proteins, DNA-Binding Proteins.
- cytology : Arabidopsis.
- enzymology : Arabidopsis.
- metabolism : Arabidopsis, Arabidopsis Proteins, DNA-Binding Proteins, Glutaredoxins, Intracellular Space, Sulfurtransferases.
- Catalytic Domain, Conserved Sequence, Enzyme Activation, Oxidation-Reduction, Photosynthesis, Phylogeny, Protein Binding, Protein Transport.
Abstract
A functional relationship between monothiol glutaredoxins and BolAs has been unraveled by genomic analyses and in several high-throughput studies. Phylogenetic analyses coupled to transient expression of green fluorescent protein (GFP) fusions indicated that, in addition to the sulfurtransferase SufE1, which contains a C-terminal BolA domain, three BolA isoforms exist in Arabidopsis thaliana, BolA1 being plastidial, BolA2 nucleo-cytoplasmic, and BolA4 dual-targeted to mitochondria and plastids. Binary yeast two-hybrid experiments demonstrated that all BolAs and SufE1, via its BolA domain, can interact with all monothiol glutaredoxins. Most interactions between protein couples of the same subcellular compartment have been confirmed by bimolecular fluorescence complementation. In vitro experiments indicated that monothiol glutaredoxins could regulate the redox state of BolA2 and SufE1, both proteins possessing a single conserved reactive cysteine. Indeed, a glutathionylated form of SufE1 lost its capacity to activate the cysteine desulfurase, Nfs2, but it is reactivated by plastidial glutaredoxins. Besides, a monomeric glutathionylated form and a dimeric disulfide-bridged form of BolA2 can be preferentially reduced by the nucleo-cytoplasmic GrxS17. These results indicate that the glutaredoxin-BolA interaction occurs in several subcellular compartments and suggest that a redox regulation mechanism, disconnected from their capacity to form iron-sulfur cluster-bridged heterodimers, may be physiologically relevant for BolA2 and SufE1.
DOI: 10.1093/mp/sst156
PubMed: 24203231
Affiliations:
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Gualberto</name></author><author><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Gaymard, Frederic" sort="Gaymard, Frederic" uniqKey="Gaymard F" first="Frédéric" last="Gaymard">Frédéric Gaymard</name></author><author><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></analytic><series><title level="j">Molecular plant</title><idno type="eISSN">1752-9867</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (cytology)</term><term>Arabidopsis (enzymology)</term><term>Arabidopsis (metabolism)</term><term>Arabidopsis Proteins (chemistry)</term><term>Arabidopsis Proteins (metabolism)</term><term>Catalytic Domain (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>DNA-Binding Proteins (chemistry)</term><term>DNA-Binding Proteins (metabolism)</term><term>Enzyme Activation (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>Intracellular Space (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Photosynthesis (MeSH)</term><term>Phylogeny (MeSH)</term><term>Protein Binding (MeSH)</term><term>Protein Transport (MeSH)</term><term>Sulfurtransferases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Arabidopsis (cytologie)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (métabolisme)</term><term>Domaine catalytique (MeSH)</term><term>Espace intracellulaire (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Photosynthèse (MeSH)</term><term>Phylogenèse (MeSH)</term><term>Protéines d'Arabidopsis (composition chimique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Protéines de liaison à l'ADN (composition chimique)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Sulfurtransferases (métabolisme)</term><term>Séquence conservée (MeSH)</term><term>Transport des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>DNA-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines d'Arabidopsis</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term><term>Arabidopsis Proteins</term><term>DNA-Binding Proteins</term><term>Glutaredoxins</term><term>Intracellular Space</term><term>Sulfurtransferases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Espace intracellulaire</term><term>Glutarédoxines</term><term>Protéines d'Arabidopsis</term><term>Protéines de liaison à l'ADN</term><term>Sulfurtransferases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term><term>Conserved Sequence</term><term>Enzyme Activation</term><term>Oxidation-Reduction</term><term>Photosynthesis</term><term>Phylogeny</term><term>Protein Binding</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term><term>Domaine catalytique</term><term>Liaison aux protéines</term><term>Oxydoréduction</term><term>Photosynthèse</term><term>Phylogenèse</term><term>Séquence conservée</term><term>Transport des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A functional relationship between monothiol glutaredoxins and BolAs has been unraveled by genomic analyses and in several high-throughput studies. Phylogenetic analyses coupled to transient expression of green fluorescent protein (GFP) fusions indicated that, in addition to the sulfurtransferase SufE1, which contains a C-terminal BolA domain, three BolA isoforms exist in Arabidopsis thaliana, BolA1 being plastidial, BolA2 nucleo-cytoplasmic, and BolA4 dual-targeted to mitochondria and plastids. Binary yeast two-hybrid experiments demonstrated that all BolAs and SufE1, via its BolA domain, can interact with all monothiol glutaredoxins. Most interactions between protein couples of the same subcellular compartment have been confirmed by bimolecular fluorescence complementation. In vitro experiments indicated that monothiol glutaredoxins could regulate the redox state of BolA2 and SufE1, both proteins possessing a single conserved reactive cysteine. Indeed, a glutathionylated form of SufE1 lost its capacity to activate the cysteine desulfurase, Nfs2, but it is reactivated by plastidial glutaredoxins. Besides, a monomeric glutathionylated form and a dimeric disulfide-bridged form of BolA2 can be preferentially reduced by the nucleo-cytoplasmic GrxS17. These results indicate that the glutaredoxin-BolA interaction occurs in several subcellular compartments and suggest that a redox regulation mechanism, disconnected from their capacity to form iron-sulfur cluster-bridged heterodimers, may be physiologically relevant for BolA2 and SufE1. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24203231</PMID><DateCompleted><Year>2014</Year><Month>07</Month><Day>01</Day></DateCompleted><DateRevised><Year>2014</Year><Month>01</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1752-9867</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>1</Issue><PubDate><Year>2014</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Molecular plant</Title><ISOAbbreviation>Mol Plant</ISOAbbreviation></Journal><ArticleTitle>Monothiol glutaredoxin-BolA interactions: redox control of Arabidopsis thaliana BolA2 and SufE1.</ArticleTitle><Pagination><MedlinePgn>187-205</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/mp/sst156</ELocationID><Abstract><AbstractText>A functional relationship between monothiol glutaredoxins and BolAs has been unraveled by genomic analyses and in several high-throughput studies. Phylogenetic analyses coupled to transient expression of green fluorescent protein (GFP) fusions indicated that, in addition to the sulfurtransferase SufE1, which contains a C-terminal BolA domain, three BolA isoforms exist in Arabidopsis thaliana, BolA1 being plastidial, BolA2 nucleo-cytoplasmic, and BolA4 dual-targeted to mitochondria and plastids. Binary yeast two-hybrid experiments demonstrated that all BolAs and SufE1, via its BolA domain, can interact with all monothiol glutaredoxins. Most interactions between protein couples of the same subcellular compartment have been confirmed by bimolecular fluorescence complementation. In vitro experiments indicated that monothiol glutaredoxins could regulate the redox state of BolA2 and SufE1, both proteins possessing a single conserved reactive cysteine. Indeed, a glutathionylated form of SufE1 lost its capacity to activate the cysteine desulfurase, Nfs2, but it is reactivated by plastidial glutaredoxins. Besides, a monomeric glutathionylated form and a dimeric disulfide-bridged form of BolA2 can be preferentially reduced by the nucleo-cytoplasmic GrxS17. These results indicate that the glutaredoxin-BolA interaction occurs in several subcellular compartments and suggest that a redox regulation mechanism, disconnected from their capacity to form iron-sulfur cluster-bridged heterodimers, may be physiologically relevant for BolA2 and SufE1. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>a Université de Lorraine, Interactions Arbres-Microorganismes, UMR1136, F-54500 Vandoeuvre-lès-Nancy, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Hui-Chen</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Dhalleine</LastName><ForeName>Tiphaine</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Pégeot</LastName><ForeName>Henri</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Sudre</LastName><ForeName>Damien</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Gualberto</LastName><ForeName>José M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Gaymard</LastName><ForeName>Frédéric</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Vignols</LastName><ForeName>Florence</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</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><ArticleDate DateType="Electronic"><Year>2013</Year><Month>11</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Plant</MedlineTA><NlmUniqueID>101465514</NlmUniqueID><ISSNLinking>1674-2052</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000589128">BolA protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber><NameOfSubstance UI="D013466">Sulfurtransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.-</RegistryNumber><NameOfSubstance UI="C557797">sulfurtransferase 1, Arabidopsis</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D042541" MajorTopicYN="N">Intracellular Space</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010788" MajorTopicYN="N">Photosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013466" MajorTopicYN="N">Sulfurtransferases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BolA</Keyword><Keyword MajorTopicYN="N">glutaredoxin</Keyword><Keyword MajorTopicYN="N">interaction</Keyword><Keyword MajorTopicYN="N">plants</Keyword><Keyword MajorTopicYN="N">redox control.</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>11</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>11</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>7</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24203231</ArticleId><ArticleId IdType="pii">S1674-2052(14)60863-7</ArticleId><ArticleId IdType="doi">10.1093/mp/sst156</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandœuvre-lès-Nancy</li></settlement><orgName><li>Université de Lorraine</li></orgName></list><tree><noCountry><name sortKey="Dhalleine, Tiphaine" sort="Dhalleine, Tiphaine" uniqKey="Dhalleine T" first="Tiphaine" last="Dhalleine">Tiphaine Dhalleine</name><name sortKey="Gaymard, Frederic" sort="Gaymard, Frederic" uniqKey="Gaymard F" first="Frédéric" last="Gaymard">Frédéric Gaymard</name><name sortKey="Gualberto, Jose M" sort="Gualberto, Jose M" uniqKey="Gualberto J" first="José M" last="Gualberto">José M. Gualberto</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Pegeot, Henri" sort="Pegeot, Henri" uniqKey="Pegeot H" first="Henri" last="Pégeot">Henri Pégeot</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Sudre, Damien" sort="Sudre, Damien" uniqKey="Sudre D" first="Damien" last="Sudre">Damien Sudre</name><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</name><name sortKey="Wu, Hui Chen" sort="Wu, Hui Chen" uniqKey="Wu H" first="Hui-Chen" last="Wu">Hui-Chen Wu</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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