Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.
Identifieur interne : 002A49 ( Main/Exploration ); précédent : 002A48; suivant : 002A50Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.
Auteurs : Jérémy Couturier [France] ; Florence Vignols ; Jean-Pierre Jacquot ; Nicolas RouhierSource :
- FEBS letters [ 1873-3468 ] ; 2012.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Glutathion (métabolisme), Gracilaria (enzymologie), Gracilaria (génétique), Methionine Sulfoxide Reductases (génétique), Methionine Sulfoxide Reductases (métabolisme), Méthionine (analogues et dérivés), Méthionine (métabolisme), Oxydoréduction (MeSH), Populus (enzymologie), Populus (génétique), Protéines chimériques mutantes (génétique), Protéines chimériques mutantes (métabolisme), Protéines recombinantes (MeSH), Saccharomyces cerevisiae (MeSH), Séquence d'acides aminés (MeSH), Test de complémentation (MeSH), Évolution biologique (MeSH).
- MESH :
- analogues et dérivés : Méthionine.
- enzymologie : Gracilaria, Populus.
- génétique : Glutarédoxines, Gracilaria, Methionine Sulfoxide Reductases, Populus, Protéines chimériques mutantes.
- métabolisme : Glutarédoxines, Glutathion, Methionine Sulfoxide Reductases, Méthionine, Protéines chimériques mutantes.
- Alignement de séquences, Cinétique, Données de séquences moléculaires, Escherichia coli, Oxydoréduction, Protéines recombinantes, Saccharomyces cerevisiae, Séquence d'acides aminés, Test de complémentation, Évolution biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Biological Evolution (MeSH), Escherichia coli (MeSH), Genetic Complementation Test (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Glutathione (metabolism), Gracilaria (enzymology), Gracilaria (genetics), Kinetics (MeSH), Methionine (analogs & derivatives), Methionine (metabolism), Methionine Sulfoxide Reductases (genetics), Methionine Sulfoxide Reductases (metabolism), Molecular Sequence Data (MeSH), Mutant Chimeric Proteins (genetics), Mutant Chimeric Proteins (metabolism), Oxidation-Reduction (MeSH), Populus (enzymology), Populus (genetics), Recombinant Proteins (MeSH), Saccharomyces cerevisiae (MeSH), Sequence Alignment (MeSH).
- MESH :
- chemical , analogs & derivatives : Methionine.
- chemical , genetics : Glutaredoxins, Methionine Sulfoxide Reductases, Mutant Chimeric Proteins.
- chemical , metabolism : Glutaredoxins, Glutathione, Methionine, Methionine Sulfoxide Reductases, Mutant Chimeric Proteins.
- enzymology : Gracilaria, Populus.
- genetics : Gracilaria, Populus.
- Amino Acid Sequence, Biological Evolution, Escherichia coli, Genetic Complementation Test, Kinetics, Molecular Sequence Data, Oxidation-Reduction, Recombinant Proteins, Saccharomyces cerevisiae, Sequence Alignment.
Abstract
A natural fusion occurring between two tandemly repeated glutaredoxin (Grx) modules and a methionine sulfoxide reductase A (MsrA) has been detected in Gracilaria gracilis. Using an in vivo yeast complementation assay and in vitro activity measurements, we demonstrated that this fusion enzyme was able to reduce methionine sulfoxide into methionine using glutathione as a reductant. Consistently, a poplar cytosolic MsrA can be regenerated in vitro by glutaredoxins with an efficiency comparable to that of thioredoxins, but using a different mechanism. We hypothesize that the glutathione/glutaredoxin system could constitute an evolutionary conserved alternative regeneration system for MsrA.
DOI: 10.1016/j.febslet.2012.09.020
PubMed: 23022439
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Jeremy.Couturier@scbiol.uhp-nancy.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR1136 Université de Lorraine-INRA, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, 54500 Vandoeuvre</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName></affiliation></author><author><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</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="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:23022439</idno><idno type="pmid">23022439</idno><idno type="doi">10.1016/j.febslet.2012.09.020</idno><idno type="wicri:Area/Main/Corpus">002869</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002869</idno><idno type="wicri:Area/Main/Curation">002869</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002869</idno><idno type="wicri:Area/Main/Exploration">002869</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.</title><author><name sortKey="Couturier, Jeremy" sort="Couturier, Jeremy" uniqKey="Couturier J" first="Jérémy" last="Couturier">Jérémy Couturier</name><affiliation wicri:level="3"><nlm:affiliation>UMR1136 Université de Lorraine-INRA, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, 54500 Vandoeuvre, France. Jeremy.Couturier@scbiol.uhp-nancy.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR1136 Université de Lorraine-INRA, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, 54500 Vandoeuvre</wicri:regionArea><placeName><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region><settlement type="city">Vandoeuvre</settlement></placeName></affiliation></author><author><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</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="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></author></analytic><series><title level="j">FEBS letters</title><idno type="eISSN">1873-3468</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Biological Evolution (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Genetic Complementation Test (MeSH)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Gracilaria (enzymology)</term><term>Gracilaria (genetics)</term><term>Kinetics (MeSH)</term><term>Methionine (analogs & derivatives)</term><term>Methionine (metabolism)</term><term>Methionine Sulfoxide Reductases (genetics)</term><term>Methionine Sulfoxide Reductases (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutant Chimeric Proteins (genetics)</term><term>Mutant Chimeric Proteins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>Recombinant Proteins (MeSH)</term><term>Saccharomyces cerevisiae (MeSH)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Cinétique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Gracilaria (enzymologie)</term><term>Gracilaria (génétique)</term><term>Methionine Sulfoxide Reductases (génétique)</term><term>Methionine Sulfoxide Reductases (métabolisme)</term><term>Méthionine (analogues et dérivés)</term><term>Méthionine (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines chimériques mutantes (génétique)</term><term>Protéines chimériques mutantes (métabolisme)</term><term>Protéines recombinantes (MeSH)</term><term>Saccharomyces cerevisiae (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Test de complémentation (MeSH)</term><term>Évolution biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Methionine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Methionine Sulfoxide Reductases</term><term>Mutant Chimeric Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Methionine</term><term>Methionine Sulfoxide Reductases</term><term>Mutant Chimeric Proteins</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Méthionine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Gracilaria</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Gracilaria</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Gracilaria</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Gracilaria</term><term>Methionine Sulfoxide Reductases</term><term>Populus</term><term>Protéines chimériques mutantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term><term>Methionine Sulfoxide Reductases</term><term>Méthionine</term><term>Protéines chimériques mutantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Biological Evolution</term><term>Escherichia coli</term><term>Genetic Complementation Test</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Escherichia coli</term><term>Oxydoréduction</term><term>Protéines recombinantes</term><term>Saccharomyces cerevisiae</term><term>Séquence d'acides aminés</term><term>Test de complémentation</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A natural fusion occurring between two tandemly repeated glutaredoxin (Grx) modules and a methionine sulfoxide reductase A (MsrA) has been detected in Gracilaria gracilis. Using an in vivo yeast complementation assay and in vitro activity measurements, we demonstrated that this fusion enzyme was able to reduce methionine sulfoxide into methionine using glutathione as a reductant. Consistently, a poplar cytosolic MsrA can be regenerated in vitro by glutaredoxins with an efficiency comparable to that of thioredoxins, but using a different mechanism. We hypothesize that the glutathione/glutaredoxin system could constitute an evolutionary conserved alternative regeneration system for MsrA.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23022439</PMID><DateCompleted><Year>2013</Year><Month>01</Month><Day>03</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-3468</ISSN><JournalIssue CitedMedium="Internet"><Volume>586</Volume><Issue>21</Issue><PubDate><Year>2012</Year><Month>Nov</Month><Day>02</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Glutathione- and glutaredoxin-dependent reduction of methionine sulfoxide reductase A.</ArticleTitle><Pagination><MedlinePgn>3894-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.febslet.2012.09.020</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0014-5793(12)00728-4</ELocationID><Abstract><AbstractText>A natural fusion occurring between two tandemly repeated glutaredoxin (Grx) modules and a methionine sulfoxide reductase A (MsrA) has been detected in Gracilaria gracilis. Using an in vivo yeast complementation assay and in vitro activity measurements, we demonstrated that this fusion enzyme was able to reduce methionine sulfoxide into methionine using glutathione as a reductant. Consistently, a poplar cytosolic MsrA can be regenerated in vitro by glutaredoxins with an efficiency comparable to that of thioredoxins, but using a different mechanism. We hypothesize that the glutathione/glutaredoxin system could constitute an evolutionary conserved alternative regeneration system for MsrA.</AbstractText><CopyrightInformation>Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Couturier</LastName><ForeName>Jérémy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>UMR1136 Université de Lorraine-INRA, Interactions Arbres-Microorganismes, IFR 110, Faculté des Sciences, 54500 Vandoeuvre, France. Jeremy.Couturier@scbiol.uhp-nancy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vignols</LastName><ForeName>Florence</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</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>2012</Year><Month>09</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="N">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</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="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044724" MajorTopicYN="N">Gracilaria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008715" MajorTopicYN="N">Methionine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051150" MajorTopicYN="N">Methionine Sulfoxide Reductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050506" MajorTopicYN="N">Mutant Chimeric Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>07</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>09</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>09</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>10</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23022439</ArticleId><ArticleId IdType="pii">S0014-5793(12)00728-4</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2012.09.020</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Vandoeuvre</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="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Vignols, Florence" sort="Vignols, Florence" uniqKey="Vignols F" first="Florence" last="Vignols">Florence Vignols</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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