Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.
Identifieur interne : 003E03 ( Main/Exploration ); précédent : 003E02; suivant : 003E04Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.
Auteurs : Valérie Noguera-Mazon [France] ; Jérôme Lemoine ; Olivier Walker ; Nicolas Rouhier ; Arnaud Salvador ; Jean-Pierre Jacquot ; Jean-Marc Lancelin ; Isabelle KrimmSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Concentration en ions d'hydrogène (MeSH), Cystéine (composition chimique), Dimérisation (MeSH), Disulfures (composition chimique), Dithiothréitol (composition chimique), Glutathion (composition chimique), Glutathion (métabolisme), Glutathione transferase (métabolisme), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxirédoxines (MeSH), Populus (MeSH), Sites de fixation (MeSH), Spectroscopie par résonance magnétique (MeSH).
- MESH :
- composition chimique : Cystéine, Disulfures, Dithiothréitol, Glutathion, Peroxidases.
- métabolisme : Glutathion, Glutathione transferase.
- Concentration en ions d'hydrogène, Dimérisation, Liaison aux protéines, Modèles moléculaires, Oxydoréduction, Peroxirédoxines, Populus, Sites de fixation, Spectroscopie par résonance magnétique.
English descriptors
- KwdEn :
- Binding Sites (MeSH), Cysteine (chemistry), Dimerization (MeSH), Disulfides (chemistry), Dithiothreitol (chemistry), Glutathione (chemistry), Glutathione (metabolism), Glutathione Transferase (metabolism), Hydrogen-Ion Concentration (MeSH), Magnetic Resonance Spectroscopy (MeSH), Models, Molecular (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxiredoxins (MeSH), Populus (MeSH), Protein Binding (MeSH).
- MESH :
- chemical , chemistry : Cysteine, Disulfides, Dithiothreitol, Glutathione, Peroxidases.
- chemical , metabolism : Glutathione, Glutathione Transferase.
- Binding Sites, Dimerization, Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, Models, Molecular, Oxidation-Reduction, Peroxiredoxins, Populus, Protein Binding.
Abstract
1-Cys peroxiredoxins (1-Cys Prxs) are antioxidant enzymes that catalyze the reduction of hydroperoxides into alcohols using a strictly conserved cysteine. 1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) pi via the formation of a GST-Prx heterodimer and Prx glutathionylation. In contrast, 1-Cys D-Prxs, homologous to human PrxV, are reactivated by the glutaredoxin-glutathione system through an unknown mechanism. To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR. This work reveals that the Prx can be glutathionylated on its active site cysteine. Evidences are reported that the glutathionylation of 1-Cys D-Prx induces the dissociation of the Prx non-covalent homodimer, which can be recovered by reduction with dithiothreitol. This work demonstrates for the first time the existence of a redox-dependent dimer-monomer switch in the Prx family, similar to the decamer-dimer switch for the 2-Cys Prxs.
DOI: 10.1074/jbc.M602188200
PubMed: 16916801
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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first="Valérie" last="Noguera-Mazon">Valérie Noguera-Mazon</name><affiliation wicri:level="3"><nlm:affiliation>CNRS, Unité Mixte de Recherche, 5180 Sciences Analytiques,Ecole Supérieure Chimie PhysiqueElectronique de Lyon, Domaine Scientifique de la Doua, Université Claude Bernard, Lyon1, 69622 Villeurbanne, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS, Unité Mixte de Recherche, 5180 Sciences Analytiques,Ecole Supérieure Chimie PhysiqueElectronique de Lyon, Domaine Scientifique de la Doua, Université Claude Bernard, Lyon1, 69622 Villeurbanne</wicri:regionArea><placeName><region type="region" nuts="2">Auvergne-Rhône-Alpes</region><region type="old region" nuts="2">Rhône-Alpes</region><settlement type="city">Villeurbanne</settlement></placeName></affiliation></author><author><name sortKey="Lemoine, Jerome" sort="Lemoine, Jerome" uniqKey="Lemoine J" first="Jérôme" last="Lemoine">Jérôme Lemoine</name></author><author><name sortKey="Walker, Olivier" sort="Walker, Olivier" uniqKey="Walker O" first="Olivier" last="Walker">Olivier Walker</name></author><author><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author><author><name sortKey="Salvador, Arnaud" sort="Salvador, Arnaud" uniqKey="Salvador A" first="Arnaud" last="Salvador">Arnaud Salvador</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="Lancelin, Jean Marc" sort="Lancelin, Jean Marc" uniqKey="Lancelin J" first="Jean-Marc" last="Lancelin">Jean-Marc Lancelin</name></author><author><name sortKey="Krimm, Isabelle" sort="Krimm, Isabelle" uniqKey="Krimm I" first="Isabelle" last="Krimm">Isabelle Krimm</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Binding Sites (MeSH)</term><term>Cysteine (chemistry)</term><term>Dimerization (MeSH)</term><term>Disulfides (chemistry)</term><term>Dithiothreitol (chemistry)</term><term>Glutathione (chemistry)</term><term>Glutathione (metabolism)</term><term>Glutathione Transferase (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Magnetic Resonance Spectroscopy (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxiredoxins (MeSH)</term><term>Populus (MeSH)</term><term>Protein Binding (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cystéine (composition chimique)</term><term>Dimérisation (MeSH)</term><term>Disulfures (composition chimique)</term><term>Dithiothréitol (composition chimique)</term><term>Glutathion (composition chimique)</term><term>Glutathion (métabolisme)</term><term>Glutathione transferase (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxirédoxines (MeSH)</term><term>Populus (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Spectroscopie par résonance magnétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Disulfides</term><term>Dithiothreitol</term><term>Glutathione</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Glutathione Transferase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Disulfures</term><term>Dithiothréitol</term><term>Glutathion</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Glutathione transferase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Dimerization</term><term>Hydrogen-Ion Concentration</term><term>Magnetic Resonance Spectroscopy</term><term>Models, Molecular</term><term>Oxidation-Reduction</term><term>Peroxiredoxins</term><term>Populus</term><term>Protein Binding</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Dimérisation</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Populus</term><term>Sites de fixation</term><term>Spectroscopie par résonance magnétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">1-Cys peroxiredoxins (1-Cys Prxs) are antioxidant enzymes that catalyze the reduction of hydroperoxides into alcohols using a strictly conserved cysteine. 1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) pi via the formation of a GST-Prx heterodimer and Prx glutathionylation. In contrast, 1-Cys D-Prxs, homologous to human PrxV, are reactivated by the glutaredoxin-glutathione system through an unknown mechanism. To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR. This work reveals that the Prx can be glutathionylated on its active site cysteine. Evidences are reported that the glutathionylation of 1-Cys D-Prx induces the dissociation of the Prx non-covalent homodimer, which can be recovered by reduction with dithiothreitol. This work demonstrates for the first time the existence of a redox-dependent dimer-monomer switch in the Prx family, similar to the decamer-dimer switch for the 2-Cys Prxs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16916801</PMID><DateCompleted><Year>2006</Year><Month>12</Month><Day>06</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>42</Issue><PubDate><Year>2006</Year><Month>Oct</Month><Day>20</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.</ArticleTitle><Pagination><MedlinePgn>31736-42</MedlinePgn></Pagination><Abstract><AbstractText>1-Cys peroxiredoxins (1-Cys Prxs) are antioxidant enzymes that catalyze the reduction of hydroperoxides into alcohols using a strictly conserved cysteine. 1-Cys B-Prxs, homologous to human PrxVI, were recently shown to be reactivated by glutathione S-transferase (GST) pi via the formation of a GST-Prx heterodimer and Prx glutathionylation. In contrast, 1-Cys D-Prxs, homologous to human PrxV, are reactivated by the glutaredoxin-glutathione system through an unknown mechanism. To investigate the mechanistic events that mediate the 1-Cys D-Prx regeneration, interaction of the Prx with glutathione was studied by mass spectrometry and NMR. This work reveals that the Prx can be glutathionylated on its active site cysteine. Evidences are reported that the glutathionylation of 1-Cys D-Prx induces the dissociation of the Prx non-covalent homodimer, which can be recovered by reduction with dithiothreitol. This work demonstrates for the first time the existence of a redox-dependent dimer-monomer switch in the Prx family, similar to the decamer-dimer switch for the 2-Cys Prxs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Noguera-Mazon</LastName><ForeName>Valérie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>CNRS, Unité Mixte de Recherche, 5180 Sciences Analytiques,Ecole Supérieure Chimie PhysiqueElectronique de Lyon, Domaine Scientifique de la Doua, Université Claude Bernard, Lyon1, 69622 Villeurbanne, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lemoine</LastName><ForeName>Jérôme</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Walker</LastName><ForeName>Olivier</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Salvador</LastName><ForeName>Arnaud</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Lancelin</LastName><ForeName>Jean-Marc</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Krimm</LastName><ForeName>Isabelle</ForeName><Initials>I</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>2006</Year><Month>08</Month><Day>17</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="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>T8ID5YZU6Y</RegistryNumber><NameOfSubstance UI="D004229">Dithiothreitol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>12</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>8</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16916801</ArticleId><ArticleId IdType="pii">M602188200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M602188200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Villeurbanne</li></settlement></list><tree><noCountry><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Krimm, Isabelle" sort="Krimm, Isabelle" uniqKey="Krimm I" first="Isabelle" last="Krimm">Isabelle Krimm</name><name sortKey="Lancelin, Jean Marc" sort="Lancelin, Jean Marc" uniqKey="Lancelin J" first="Jean-Marc" last="Lancelin">Jean-Marc Lancelin</name><name sortKey="Lemoine, Jerome" sort="Lemoine, Jerome" uniqKey="Lemoine J" first="Jérôme" last="Lemoine">Jérôme Lemoine</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Salvador, Arnaud" sort="Salvador, Arnaud" uniqKey="Salvador A" first="Arnaud" last="Salvador">Arnaud Salvador</name><name sortKey="Walker, Olivier" sort="Walker, Olivier" uniqKey="Walker O" first="Olivier" last="Walker">Olivier Walker</name></noCountry><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Noguera Mazon, Valerie" sort="Noguera Mazon, Valerie" uniqKey="Noguera Mazon V" first="Valérie" last="Noguera-Mazon">Valérie Noguera-Mazon</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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