NMR reveals a novel glutaredoxin-glutaredoxin interaction interface.
Identifieur interne : 003F89 ( Main/Exploration ); précédent : 003F88; suivant : 003F90NMR reveals a novel glutaredoxin-glutaredoxin interaction interface.
Auteurs : Valerie Noguera [France] ; Olivier Walker ; Nicolas Rouhier ; Jean-Pierre Jacquot ; Isabelle Krimm ; Jean-Marc LancelinSource :
- Journal of molecular biology [ 0022-2836 ] ; 2005.
Descripteurs français
- KwdFr :
- Dimérisation (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Peroxidases (composition chimique), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Résonance magnétique nucléaire biomoléculaire (méthodes), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Oxidoreductases, Peroxidases.
- métabolisme : Glutathion, Oxidoreductases, Peroxidases.
- méthodes : Résonance magnétique nucléaire biomoléculaire.
- Dimérisation, Données de séquences moléculaires, Glutarédoxines, Liaison aux protéines, Modèles moléculaires, Peroxirédoxines, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Dimerization (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nuclear Magnetic Resonance, Biomolecular (methods), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Peroxidases (chemistry), Peroxidases (metabolism), Peroxiredoxins (MeSH), Protein Binding (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Oxidoreductases, Peroxidases.
- chemical , metabolism : Glutathione, Oxidoreductases, Peroxidases.
- chemical : Glutaredoxins, Peroxiredoxins.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Amino Acid Sequence, Dimerization, Models, Molecular, Molecular Sequence Data, Protein Binding, Sequence Homology, Amino Acid.
Abstract
Glutaredoxins (Grx) represent a large family of glutathione (GSH)-dependent oxidoreductases that catalyse the reduction of disulfides or glutathione mixed disulfide. Grx domains from pathogenic bacteria and plant Grxs have been recently reported to target specific peroxiredoxins (Prxs). The specificity that triggers the interaction between Grx and Prx is poorly understood and is only based on the structure of Haemophilus influenzae Prx-Grx hybrid (hyPrx5). We report here an NMR study of the Populus tremula Grx C4 that targets a P.tremula D-type II Prx. We show that Grx C4 specifically self-associates in a monomer-dimer equilibrium with an apparent K(d) of ca 2.6 mM. Grx C4 homodimer was docked under experimental restraints. The results reveal a novel Grx-Grx interface that is unrelated to the hyPrx5 Grx-Grx dimer interface. Chemical-shift perturbations and 15N spin-relaxation measurements show that the auto-association surface comprises both the active site and the GSH binding site. Reduced GSH is demonstrated to bind reduced Grx with a K(d) of ca 8.6 mM. The potential biological significance of the new Grx-Grx interaction interface is discussed.
DOI: 10.1016/j.jmb.2005.08.035
PubMed: 16181638
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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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="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Krimm, Isabelle" sort="Krimm, Isabelle" uniqKey="Krimm I" first="Isabelle" last="Krimm">Isabelle Krimm</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></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16181638</idno><idno type="pmid">16181638</idno><idno type="doi">10.1016/j.jmb.2005.08.035</idno><idno type="wicri:Area/Main/Corpus">003F52</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" 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nuts="2">Rhône-Alpes</region><settlement type="city">Villeurbanne</settlement></placeName></affiliation></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="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name></author><author><name sortKey="Krimm, Isabelle" sort="Krimm, Isabelle" uniqKey="Krimm I" first="Isabelle" last="Krimm">Isabelle Krimm</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></analytic><series><title level="j">Journal of molecular biology</title><idno type="ISSN">0022-2836</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Dimerization (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (methods)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (metabolism)</term><term>Peroxiredoxins (MeSH)</term><term>Protein Binding (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dimérisation (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Résonance magnétique nucléaire biomoléculaire (méthodes)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Nuclear Magnetic Resonance, Biomolecular</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutathion</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Résonance magnétique nucléaire biomoléculaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Dimerization</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peroxirédoxines</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grx) represent a large family of glutathione (GSH)-dependent oxidoreductases that catalyse the reduction of disulfides or glutathione mixed disulfide. Grx domains from pathogenic bacteria and plant Grxs have been recently reported to target specific peroxiredoxins (Prxs). The specificity that triggers the interaction between Grx and Prx is poorly understood and is only based on the structure of Haemophilus influenzae Prx-Grx hybrid (hyPrx5). We report here an NMR study of the Populus tremula Grx C4 that targets a P.tremula D-type II Prx. We show that Grx C4 specifically self-associates in a monomer-dimer equilibrium with an apparent K(d) of ca 2.6 mM. Grx C4 homodimer was docked under experimental restraints. The results reveal a novel Grx-Grx interface that is unrelated to the hyPrx5 Grx-Grx dimer interface. Chemical-shift perturbations and 15N spin-relaxation measurements show that the auto-association surface comprises both the active site and the GSH binding site. Reduced GSH is demonstrated to bind reduced Grx with a K(d) of ca 8.6 mM. The potential biological significance of the new Grx-Grx interaction interface is discussed.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16181638</PMID><DateCompleted><Year>2006</Year><Month>01</Month><Day>25</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0022-2836</ISSN><JournalIssue CitedMedium="Print"><Volume>353</Volume><Issue>3</Issue><PubDate><Year>2005</Year><Month>Oct</Month><Day>28</Day></PubDate></JournalIssue><Title>Journal of molecular biology</Title><ISOAbbreviation>J Mol Biol</ISOAbbreviation></Journal><ArticleTitle>NMR reveals a novel glutaredoxin-glutaredoxin interaction interface.</ArticleTitle><Pagination><MedlinePgn>629-41</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grx) represent a large family of glutathione (GSH)-dependent oxidoreductases that catalyse the reduction of disulfides or glutathione mixed disulfide. Grx domains from pathogenic bacteria and plant Grxs have been recently reported to target specific peroxiredoxins (Prxs). The specificity that triggers the interaction between Grx and Prx is poorly understood and is only based on the structure of Haemophilus influenzae Prx-Grx hybrid (hyPrx5). We report here an NMR study of the Populus tremula Grx C4 that targets a P.tremula D-type II Prx. We show that Grx C4 specifically self-associates in a monomer-dimer equilibrium with an apparent K(d) of ca 2.6 mM. Grx C4 homodimer was docked under experimental restraints. The results reveal a novel Grx-Grx interface that is unrelated to the hyPrx5 Grx-Grx dimer interface. Chemical-shift perturbations and 15N spin-relaxation measurements show that the auto-association surface comprises both the active site and the GSH binding site. Reduced GSH is demonstrated to bind reduced Grx with a K(d) of ca 8.6 mM. The potential biological significance of the new Grx-Grx interaction interface is discussed.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Noguera</LastName><ForeName>Valerie</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>RMN Biomoléculaire, Université Claude Bernard, Lyon 1, CNRS UMR 5180 Sciences Analytiques, ESCPE-Lyon, 69622 Villeurbanne, France.</Affiliation></AffiliationInfo></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>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Krimm</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials></Author><Author ValidYN="Y"><LastName>Lancelin</LastName><ForeName>Jean-Marc</ForeName><Initials>JM</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>2005</Year><Month>09</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Mol Biol</MedlineTA><NlmUniqueID>2985088R</NlmUniqueID><ISSNLinking>0022-2836</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</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>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2005</Year><Month>06</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2005</Year><Month>08</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2005</Year><Month>08</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>9</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>1</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>9</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16181638</ArticleId><ArticleId IdType="pii">S0022-2836(05)00972-1</ArticleId><ArticleId IdType="doi">10.1016/j.jmb.2005.08.035</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="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</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, Valerie" sort="Noguera, Valerie" uniqKey="Noguera V" first="Valerie" last="Noguera">Valerie Noguera</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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