Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins.
Identifieur interne : 002F91 ( Main/Exploration ); précédent : 002F90; suivant : 002F92Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins.
Auteurs : Jérémy Couturier [France] ; Elke Ströher ; Angela-Nadia Albetel ; Thomas Roret ; Meenakumari Muthuramalingam ; Lionel Tarrago ; Thorsten Seidel ; Pascale Tsan ; Jean-Pierre Jacquot ; Michael K. Johnson ; Karl-Josef Dietz ; Claude Didierjean ; Nicolas RouhierSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
Descripteurs français
- KwdFr :
- Arabidopsis (génétique), Arabidopsis (métabolisme), Chloroplastes (métabolisme), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Ferrosulfoprotéines (métabolisme), Fractions subcellulaires (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Liaison aux protéines (MeSH), Mutagenèse dirigée (MeSH), Spectrométrie de masse ESI (MeSH).
- MESH :
English descriptors
- KwdEn :
- Arabidopsis (genetics), Arabidopsis (metabolism), Chloroplasts (metabolism), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Iron-Sulfur Proteins (metabolism), Mutagenesis, Site-Directed (MeSH), Protein Binding (MeSH), Spectrometry, Mass, Electrospray Ionization (MeSH), Subcellular Fractions (metabolism).
- MESH :
- chemical , genetics : Glutaredoxins.
- genetics : Arabidopsis.
- metabolism : Arabidopsis, Chloroplasts, Glutaredoxins, Iron-Sulfur Proteins, Subcellular Fractions.
- Cloning, Molecular, Crystallography, X-Ray, Mutagenesis, Site-Directed, Protein Binding, Spectrometry, Mass, Electrospray Ionization.
Abstract
Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides (i.e. protein-glutathione adducts), and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, was shown to be localized in chloroplasts. A comparison of the biochemical, structural, and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicated that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the x-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys(32)) is required for cluster formation. In addition, thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism.
DOI: 10.1074/jbc.M111.228726
PubMed: 21632542
PubMed Central: PMC3149344
Affiliations:
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Johnson</name></author><author><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name></author><author><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</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">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (genetics)</term><term>Arabidopsis (metabolism)</term><term>Chloroplasts (metabolism)</term><term>Cloning, Molecular (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Iron-Sulfur Proteins (metabolism)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Protein Binding (MeSH)</term><term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term><term>Subcellular Fractions (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (génétique)</term><term>Arabidopsis (métabolisme)</term><term>Chloroplastes (métabolisme)</term><term>Clonage moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Ferrosulfoprotéines (métabolisme)</term><term>Fractions subcellulaires (métabolisme)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Spectrométrie de masse ESI (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term><term>Chloroplasts</term><term>Glutaredoxins</term><term>Iron-Sulfur Proteins</term><term>Subcellular Fractions</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Chloroplastes</term><term>Ferrosulfoprotéines</term><term>Fractions subcellulaires</term><term>Glutarédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Mutagenesis, Site-Directed</term><term>Protein Binding</term><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Liaison aux protéines</term><term>Mutagenèse dirigée</term><term>Spectrométrie de masse ESI</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides (i.e. protein-glutathione adducts), and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, was shown to be localized in chloroplasts. A comparison of the biochemical, structural, and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicated that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the x-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys(32)) is required for cluster formation. In addition, thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21632542</PMID><DateCompleted><Year>2011</Year><Month>10</Month><Day>10</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>286</Volume><Issue>31</Issue><PubDate><Year>2011</Year><Month>Aug</Month><Day>05</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins.</ArticleTitle><Pagination><MedlinePgn>27515-27</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M111.228726</ELocationID><Abstract><AbstractText>Unlike thioredoxins, glutaredoxins are involved in iron-sulfur cluster assembly and in reduction of specific disulfides (i.e. protein-glutathione adducts), and thus they are also important redox regulators of chloroplast metabolism. Using GFP fusion, AtGrxC5 isoform, present exclusively in Brassicaceae, was shown to be localized in chloroplasts. A comparison of the biochemical, structural, and spectroscopic properties of Arabidopsis GrxC5 (WCSYC active site) with poplar GrxS12 (WCSYS active site), a chloroplastic paralog, indicated that, contrary to the solely apomonomeric GrxS12 isoform, AtGrxC5 exists as two forms when expressed in Escherichia coli. The monomeric apoprotein possesses deglutathionylation activity mediating the recycling of plastidial methionine sulfoxide reductase B1 and peroxiredoxin IIE, whereas the dimeric holoprotein incorporates a [2Fe-2S] cluster. Site-directed mutagenesis experiments and resolution of the x-ray crystal structure of AtGrxC5 in its holoform revealed that, although not involved in its ligation, the presence of the second active site cysteine (Cys(32)) is required for cluster formation. In addition, thiol titrations, fluorescence measurements, and mass spectrometry analyses showed that, despite the presence of a dithiol active site, AtGrxC5 does not form any inter- or intramolecular disulfide bond and that its activity exclusively relies on a monothiol mechanism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Unité Mixte de Recherches 1136, Institut National de la Recherche Agronomique-Nancy Université, Interactions Arbres Microorganismes, Institut Fédératif de Recherche 110 Ecosystèmes Forestiers, Agroressources, Biomolécule et Alimentation, 54506 Vandoeuvre-lès-Nancy Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ströher</LastName><ForeName>Elke</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Albetel</LastName><ForeName>Angela-Nadia</ForeName><Initials>AN</Initials></Author><Author ValidYN="Y"><LastName>Roret</LastName><ForeName>Thomas</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Muthuramalingam</LastName><ForeName>Meenakumari</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Tarrago</LastName><ForeName>Lionel</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Seidel</LastName><ForeName>Thorsten</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Tsan</LastName><ForeName>Pascale</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Johnson</LastName><ForeName>Michael K</ForeName><Initials>MK</Initials></Author><Author ValidYN="Y"><LastName>Dietz</LastName><ForeName>Karl-Josef</ForeName><Initials>KJ</Initials></Author><Author ValidYN="Y"><LastName>Didierjean</LastName><ForeName>Claude</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>3RHB</AccessionNumber><AccessionNumber>3RHC</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R37 GM062524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM62524</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>06</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002736" MajorTopicYN="N">Chloroplasts</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>6</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId 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IdType="pubmed">14713336</ArticleId></ArticleIdList></Reference></ReferenceList></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></list><tree><noCountry><name sortKey="Albetel, Angela Nadia" sort="Albetel, Angela Nadia" uniqKey="Albetel A" first="Angela-Nadia" last="Albetel">Angela-Nadia Albetel</name><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Dietz, Karl Josef" sort="Dietz, Karl Josef" uniqKey="Dietz K" first="Karl-Josef" last="Dietz">Karl-Josef Dietz</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Johnson, Michael K" sort="Johnson, Michael K" uniqKey="Johnson M" first="Michael K" last="Johnson">Michael K. Johnson</name><name sortKey="Muthuramalingam, Meenakumari" sort="Muthuramalingam, Meenakumari" uniqKey="Muthuramalingam M" first="Meenakumari" last="Muthuramalingam">Meenakumari Muthuramalingam</name><name sortKey="Roret, Thomas" sort="Roret, Thomas" uniqKey="Roret T" first="Thomas" last="Roret">Thomas Roret</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Seidel, Thorsten" sort="Seidel, Thorsten" uniqKey="Seidel T" first="Thorsten" last="Seidel">Thorsten Seidel</name><name sortKey="Stroher, Elke" sort="Stroher, Elke" uniqKey="Stroher E" first="Elke" last="Ströher">Elke Ströher</name><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name><name sortKey="Tsan, Pascale" sort="Tsan, Pascale" uniqKey="Tsan P" first="Pascale" last="Tsan">Pascale Tsan</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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