Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.
Identifieur interne : 003B88 ( Main/Exploration ); précédent : 003B87; suivant : 003B89Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.
Auteurs : Nicolas Rouhier [France] ; Brice Kauffmann ; Frédérique Tete-Favier ; Pasquale Palladino ; Pierre Gans ; Guy Branlant ; Jean-Pierre Jacquot ; Sandrine Boschi-MullerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2007.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Cystéine (analyse), Cytosol (enzymologie), Données de séquences moléculaires (MeSH), Escherichia coli (enzymologie), Escherichia coli (génétique), Methionine Sulfoxide Reductases (MeSH), Mutagenèse (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (isolement et purification), Oxidoreductases (métabolisme), Plastes (enzymologie), Populus (enzymologie), Protéines recombinantes (composition chimique), Protéines recombinantes (métabolisme), Protéines végétales (composition chimique), Protéines végétales (métabolisme).
- MESH :
- analyse : Cystéine.
- composition chimique : Oxidoreductases, Protéines recombinantes, Protéines végétales.
- enzymologie : Cytosol, Escherichia coli, Plastes, Populus.
- génétique : Escherichia coli.
- isolement et purification : Oxidoreductases.
- métabolisme : Oxidoreductases, Protéines recombinantes, Protéines végétales.
- Cinétique, Clonage moléculaire, Cristallographie aux rayons X, Données de séquences moléculaires, Methionine Sulfoxide Reductases, Mutagenèse.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Cysteine (analysis), Cytosol (enzymology), Escherichia coli (enzymology), Escherichia coli (genetics), Kinetics (MeSH), Methionine Sulfoxide Reductases (MeSH), Molecular Sequence Data (MeSH), Mutagenesis (MeSH), Oxidoreductases (chemistry), Oxidoreductases (isolation & purification), Oxidoreductases (metabolism), Plant Proteins (chemistry), Plant Proteins (metabolism), Plastids (enzymology), Populus (enzymology), Recombinant Proteins (chemistry), Recombinant Proteins (metabolism).
- MESH :
- chemical , analysis : Cysteine.
- chemical , chemistry : Oxidoreductases, Plant Proteins, Recombinant Proteins.
- enzymology : Cytosol, Escherichia coli, Plastids, Populus.
- genetics : Escherichia coli.
- chemical , isolation & purification : Oxidoreductases.
- chemical , metabolism : Oxidoreductases, Plant Proteins, Recombinant Proteins.
- Cloning, Molecular, Crystallography, X-Ray, Kinetics, Methionine Sulfoxide Reductases, Molecular Sequence Data, Mutagenesis.
Abstract
The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys(46) is the catalytic cysteine, and the two C-terminal cysteines, Cys(196) and Cys(202), are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys(202), but not Cys(196), is the first recycling cysteine that forms a disulfide bond with the catalytic Cys(46). Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys(202) is located closer to Cys(46) compared with Cys(196) and is included in a (202)CYG(204) signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine.
DOI: 10.1074/jbc.M605007200
PubMed: 17135266
Affiliations:
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first="Nicolas" last="Rouhier">Nicolas Rouhier</name><affiliation wicri:level="3"><nlm:affiliation>UMR 1136 INRA-UHP, Nancy Universités, Interactions Arbres Microorganismes, IFR 110, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-anacy.fr</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 1136 INRA-UHP, Nancy Universités, Interactions Arbres Microorganismes, IFR 110, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex</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="Kauffmann, Brice" sort="Kauffmann, Brice" uniqKey="Kauffmann B" first="Brice" last="Kauffmann">Brice Kauffmann</name></author><author><name sortKey="Tete Favier, Frederique" sort="Tete Favier, Frederique" uniqKey="Tete Favier F" 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moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (analyse)</term><term>Cytosol (enzymologie)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (enzymologie)</term><term>Escherichia coli (génétique)</term><term>Methionine Sulfoxide Reductases (MeSH)</term><term>Mutagenèse (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (isolement et purification)</term><term>Oxidoreductases (métabolisme)</term><term>Plastes (enzymologie)</term><term>Populus (enzymologie)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (composition chimique)</term><term>Protéines végétales (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Cysteine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" 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xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term><term>Protéines recombinantes</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Kinetics</term><term>Methionine Sulfoxide Reductases</term><term>Molecular Sequence Data</term><term>Mutagenesis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Methionine Sulfoxide Reductases</term><term>Mutagenèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys(46) is the catalytic cysteine, and the two C-terminal cysteines, Cys(196) and Cys(202), are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys(202), but not Cys(196), is the first recycling cysteine that forms a disulfide bond with the catalytic Cys(46). Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys(202) is located closer to Cys(46) compared with Cys(196) and is included in a (202)CYG(204) signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17135266</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>10</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>282</Volume><Issue>5</Issue><PubDate><Year>2007</Year><Month>Feb</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Functional and structural aspects of poplar cytosolic and plastidial type a methionine sulfoxide reductases.</ArticleTitle><Pagination><MedlinePgn>3367-78</MedlinePgn></Pagination><Abstract><AbstractText>The genome of Populus trichocarpa contains five methionine sulfoxide reductase A genes. Here, both cytosolic (cMsrA) and plastidial (pMsrA) poplar MsrAs were analyzed. The two recombinant enzymes are active in the reduction of methionine sulfoxide with either dithiothreitol or poplar thioredoxin as a reductant. In both enzymes, five cysteines, at positions 46, 81, 100, 196, and 202, are conserved. Biochemical and enzymatic analyses of the cysteine-mutated MsrAs support a catalytic mechanism involving three cysteines at positions 46, 196, and 202. Cys(46) is the catalytic cysteine, and the two C-terminal cysteines, Cys(196) and Cys(202), are implicated in the thioredoxin-dependent recycling mechanism. Inspection of the pMsrA x-ray three-dimensional structure, which has been determined in this study, strongly suggests that contrary to bacterial and Bos taurus MsrAs, which also contain three essential Cys, the last C-terminal Cys(202), but not Cys(196), is the first recycling cysteine that forms a disulfide bond with the catalytic Cys(46). Then Cys(202) forms a disulfide bond with the second recycling cysteine Cys(196) that is preferentially reduced by thioredoxin. In agreement with this assumption, Cys(202) is located closer to Cys(46) compared with Cys(196) and is included in a (202)CYG(204) signature specific for most plant MsrAs. The tyrosine residue corresponds to the one described to be involved in substrate binding in bacterial and B. taurus MsrAs. In these MsrAs, the tyrosine residue belongs to a similar signature as found in plant MsrAs but with the first C-terminal cysteine instead of the last C-terminal cysteine.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>UMR 1136 INRA-UHP, Nancy Universités, Interactions Arbres Microorganismes, IFR 110, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre Cedex, France. nrouhier@scbiol.uhp-anacy.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kauffmann</LastName><ForeName>Brice</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Tete-Favier</LastName><ForeName>Frédérique</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Palladino</LastName><ForeName>Pasquale</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Gans</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Branlant</LastName><ForeName>Guy</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Boschi-Muller</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AAS46231</AccessionNumber><AccessionNumber>AAS46232</AccessionNumber></AccessionNumberList></DataBank><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2J89</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2006</Year><Month>11</Month><Day>29</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="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.-</RegistryNumber><NameOfSubstance UI="D051150">Methionine Sulfoxide Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.11</RegistryNumber><NameOfSubstance UI="C027219">methionine sulfoxide reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051150" MajorTopicYN="N">Methionine Sulfoxide Reductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016296" MajorTopicYN="N">Mutagenesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018087" MajorTopicYN="N">Plastids</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>12</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>4</Month><Day>11</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>12</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17135266</ArticleId><ArticleId IdType="pii">M605007200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M605007200</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="Boschi Muller, Sandrine" sort="Boschi Muller, Sandrine" uniqKey="Boschi Muller S" first="Sandrine" last="Boschi-Muller">Sandrine Boschi-Muller</name><name sortKey="Branlant, Guy" sort="Branlant, Guy" uniqKey="Branlant G" first="Guy" last="Branlant">Guy Branlant</name><name sortKey="Gans, Pierre" sort="Gans, Pierre" uniqKey="Gans P" first="Pierre" last="Gans">Pierre Gans</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Kauffmann, Brice" sort="Kauffmann, Brice" uniqKey="Kauffmann B" first="Brice" last="Kauffmann">Brice Kauffmann</name><name sortKey="Palladino, Pasquale" sort="Palladino, Pasquale" uniqKey="Palladino P" first="Pasquale" last="Palladino">Pasquale Palladino</name><name sortKey="Tete Favier, Frederique" sort="Tete Favier, Frederique" uniqKey="Tete Favier F" first="Frédérique" last="Tete-Favier">Frédérique Tete-Favier</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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