An atypical catalytic mechanism involving three cysteines of thioredoxin.
Identifieur interne : 003997 ( Main/Exploration ); précédent : 003996; suivant : 003998An atypical catalytic mechanism involving three cysteines of thioredoxin.
Auteurs : Cha San Koh [France] ; Nicolas Navrot ; Claude Didierjean ; Nicolas Rouhier ; Masakazu Hirasawa ; David B. Knaff ; Gunnar Wingsle ; Razip Samian ; Jean-Pierre Jacquot ; Catherine Corbier ; Eric GelhayeSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2008.
Descripteurs français
- KwdFr :
- Catalyse (MeSH), Clonage moléculaire (MeSH), Cristallographie aux rayons X (MeSH), Cystéine (composition chimique), Dithiothréitol (composition chimique), Données de séquences moléculaires (MeSH), Glutarédoxines (composition chimique), Mutation (MeSH), Protéines végétales (composition chimique), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Spectrométrie de masse ESI (MeSH), Séquence d'acides aminés (MeSH), Thioredoxin-disulfide reductase (composition chimique), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Cystéine, Dithiothréitol, Glutarédoxines, Protéines végétales, Thioredoxin-disulfide reductase, Thiorédoxines.
- métabolisme : Thiorédoxines.
- Catalyse, Clonage moléculaire, Cristallographie aux rayons X, Données de séquences moléculaires, Mutation, Similitude de séquences d'acides aminés, Sites de fixation, Spectrométrie de masse ESI, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Catalysis (MeSH), Cloning, Molecular (MeSH), Crystallography, X-Ray (MeSH), Cysteine (chemistry), Dithiothreitol (chemistry), Glutaredoxins (chemistry), Molecular Sequence Data (MeSH), Mutation (MeSH), Plant Proteins (chemistry), Sequence Homology, Amino Acid (MeSH), Spectrometry, Mass, Electrospray Ionization (MeSH), Thioredoxin-Disulfide Reductase (chemistry), Thioredoxins (chemistry), Thioredoxins (metabolism).
- MESH :
- chemical , chemistry : Cysteine, Dithiothreitol, Glutaredoxins, Plant Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , metabolism : Thioredoxins.
- Amino Acid Sequence, Binding Sites, Catalysis, Cloning, Molecular, Crystallography, X-Ray, Molecular Sequence Data, Mutation, Sequence Homology, Amino Acid, Spectrometry, Mass, Electrospray Ionization.
Abstract
Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys(4)) and two (Cys(58) and Cys(61)) in the classical thioredoxin active site ((57)WCGPC(61)). The property of a mutant in which Cys(58) was replaced by serine demonstrates that it is responsible for the initial nucleophilic attack during the catalytic cycle. The observation that the C4S mutant is inactive in the presence of Grx but fully active when dithiothreitol is used as a reductant indicates that Cys(4) is required for the regeneration of PtTrxh4 by Grx. Biochemical and x-ray crystallographic studies indicate that two intramolecular disulfide bonds involving Cys(58) can be formed, linking it to either Cys(61) or Cys(4). We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form.
DOI: 10.1074/jbc.M802093200
PubMed: 18552403
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Knaff</name></author><author><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name></author><author><name sortKey="Samian, Razip" sort="Samian, Razip" uniqKey="Samian R" first="Razip" last="Samian">Razip Samian</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="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18552403</idno><idno type="pmid">18552403</idno><idno type="doi">10.1074/jbc.M802093200</idno><idno type="wicri:Area/Main/Corpus">003861</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003861</idno><idno type="wicri:Area/Main/Curation">003861</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">003861</idno><idno type="wicri:Area/Main/Exploration">003861</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">An atypical catalytic mechanism involving three cysteines of thioredoxin.</title><author><name sortKey="Koh, Cha San" sort="Koh, Cha San" uniqKey="Koh C" first="Cha San" last="Koh">Cha San Koh</name><affiliation wicri:level="4"><nlm:affiliation>Equipe Biocristallographie, UMR 7036 CNRS-Université Henri Poincaré, URAFPA, Equipe PB2P, Faculté des Sciences et Techniques, Nancy Université, BP 239, 54506 Vandoeuvre Cedex France.</nlm:affiliation><orgName type="university">Université Henri Poincaré</orgName><country>France</country><placeName><settlement type="city">Nancy</settlement><region type="region" nuts="2">Grand Est</region><region type="old region" nuts="2">Lorraine (région)</region></placeName></affiliation></author><author><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</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><author><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name></author><author><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name></author><author><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name></author><author><name sortKey="Samian, Razip" sort="Samian, Razip" uniqKey="Samian R" first="Razip" last="Samian">Razip Samian</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="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name></author><author><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Binding Sites (MeSH)</term><term>Catalysis (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Crystallography, X-Ray (MeSH)</term><term>Cysteine (chemistry)</term><term>Dithiothreitol (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (MeSH)</term><term>Plant Proteins (chemistry)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Spectrometry, Mass, Electrospray Ionization (MeSH)</term><term>Thioredoxin-Disulfide Reductase (chemistry)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalyse (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cristallographie aux rayons X (MeSH)</term><term>Cystéine (composition chimique)</term><term>Dithiothréitol (composition chimique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (composition chimique)</term><term>Mutation (MeSH)</term><term>Protéines végétales (composition chimique)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Spectrométrie de masse ESI (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thioredoxin-disulfide reductase (composition chimique)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Dithiothreitol</term><term>Glutaredoxins</term><term>Plant Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Dithiothréitol</term><term>Glutarédoxines</term><term>Protéines végétales</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Catalysis</term><term>Cloning, Molecular</term><term>Crystallography, X-Ray</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Sequence Homology, Amino Acid</term><term>Spectrometry, Mass, Electrospray Ionization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Clonage moléculaire</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Mutation</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Spectrométrie de masse ESI</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys(4)) and two (Cys(58) and Cys(61)) in the classical thioredoxin active site ((57)WCGPC(61)). The property of a mutant in which Cys(58) was replaced by serine demonstrates that it is responsible for the initial nucleophilic attack during the catalytic cycle. The observation that the C4S mutant is inactive in the presence of Grx but fully active when dithiothreitol is used as a reductant indicates that Cys(4) is required for the regeneration of PtTrxh4 by Grx. Biochemical and x-ray crystallographic studies indicate that two intramolecular disulfide bonds involving Cys(58) can be formed, linking it to either Cys(61) or Cys(4). We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18552403</PMID><DateCompleted><Year>2008</Year><Month>10</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>283</Volume><Issue>34</Issue><PubDate><Year>2008</Year><Month>Aug</Month><Day>22</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>An atypical catalytic mechanism involving three cysteines of thioredoxin.</ArticleTitle><Pagination><MedlinePgn>23062-72</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M802093200</ELocationID><Abstract><AbstractText>Unlike other thioredoxins h characterized so far, a poplar thioredoxin of the h type, PtTrxh4, is reduced by glutathione and glutaredoxin (Grx) but not NADPH:thioredoxin reductase (NTR). PtTrxh4 contains three cysteines: one localized in an N-terminal extension (Cys(4)) and two (Cys(58) and Cys(61)) in the classical thioredoxin active site ((57)WCGPC(61)). The property of a mutant in which Cys(58) was replaced by serine demonstrates that it is responsible for the initial nucleophilic attack during the catalytic cycle. The observation that the C4S mutant is inactive in the presence of Grx but fully active when dithiothreitol is used as a reductant indicates that Cys(4) is required for the regeneration of PtTrxh4 by Grx. Biochemical and x-ray crystallographic studies indicate that two intramolecular disulfide bonds involving Cys(58) can be formed, linking it to either Cys(61) or Cys(4). We propose thus a four-step disulfide cascade mechanism involving the transient glutathionylation of Cys(4) to convert this atypical thioredoxin h back to its active reduced form.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Koh</LastName><ForeName>Cha San</ForeName><Initials>CS</Initials><AffiliationInfo><Affiliation>Equipe Biocristallographie, UMR 7036 CNRS-Université Henri Poincaré, URAFPA, Equipe PB2P, Faculté des Sciences et Techniques, Nancy Université, BP 239, 54506 Vandoeuvre Cedex France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Navrot</LastName><ForeName>Nicolas</ForeName><Initials>N</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><Author ValidYN="Y"><LastName>Hirasawa</LastName><ForeName>Masakazu</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Knaff</LastName><ForeName>David B</ForeName><Initials>DB</Initials></Author><Author ValidYN="Y"><LastName>Wingsle</LastName><ForeName>Gunnar</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Samian</LastName><ForeName>Razip</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Jacquot</LastName><ForeName>Jean-Pierre</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Corbier</LastName><ForeName>Catherine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Gelhaye</LastName><ForeName>Eric</ForeName><Initials>E</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>2008</Year><Month>06</Month><Day>14</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="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></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="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004229" MajorTopicYN="N">Dithiothreitol</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021241" MajorTopicYN="N">Spectrometry, Mass, Electrospray Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>6</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>10</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>6</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18552403</ArticleId><ArticleId IdType="pii">M802093200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M802093200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Grand Est</li><li>Lorraine (région)</li></region><settlement><li>Nancy</li></settlement><orgName><li>Université Henri Poincaré</li></orgName></list><tree><noCountry><name sortKey="Corbier, Catherine" sort="Corbier, Catherine" uniqKey="Corbier C" first="Catherine" last="Corbier">Catherine Corbier</name><name sortKey="Didierjean, Claude" sort="Didierjean, Claude" uniqKey="Didierjean C" first="Claude" last="Didierjean">Claude Didierjean</name><name sortKey="Gelhaye, Eric" sort="Gelhaye, Eric" uniqKey="Gelhaye E" first="Eric" last="Gelhaye">Eric Gelhaye</name><name sortKey="Hirasawa, Masakazu" sort="Hirasawa, Masakazu" uniqKey="Hirasawa M" first="Masakazu" last="Hirasawa">Masakazu Hirasawa</name><name sortKey="Jacquot, Jean Pierre" sort="Jacquot, Jean Pierre" uniqKey="Jacquot J" first="Jean-Pierre" last="Jacquot">Jean-Pierre Jacquot</name><name sortKey="Knaff, David B" sort="Knaff, David B" uniqKey="Knaff D" first="David B" last="Knaff">David B. Knaff</name><name sortKey="Navrot, Nicolas" sort="Navrot, Nicolas" uniqKey="Navrot N" first="Nicolas" last="Navrot">Nicolas Navrot</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Samian, Razip" sort="Samian, Razip" uniqKey="Samian R" first="Razip" last="Samian">Razip Samian</name><name sortKey="Wingsle, Gunnar" sort="Wingsle, Gunnar" uniqKey="Wingsle G" first="Gunnar" last="Wingsle">Gunnar Wingsle</name></noCountry><country name="France"><region name="Grand Est"><name sortKey="Koh, Cha San" sort="Koh, Cha San" uniqKey="Koh C" first="Cha San" last="Koh">Cha San Koh</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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