Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B.
Identifieur interne : 000C56 ( Main/Exploration ); précédent : 000C55; suivant : 000C57Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B.
Auteurs : Christina Vieira Dos Santos [France] ; Edith Laugier ; Lionel Tarrago ; Vincent Massot ; Emmanuelle Issakidis-Bourguet ; Nicolas Rouhier ; Pascal ReySource :
- FEBS letters [ 0014-5793 ] ; 2007.
Descripteurs français
- KwdFr :
- Cystéine (génétique), Cystéine (métabolisme), Facteurs temps (MeSH), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Methionine Sulfoxide Reductases (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Plastes (enzymologie), Plastes (métabolisme), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Spécificité du substrat (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Transport d'électrons (MeSH).
- MESH :
- enzymologie : Plastes.
- génétique : Cystéine, Glutarédoxines, Oxidoreductases, Protéines d'Arabidopsis, Protéines recombinantes, Thiorédoxines.
- métabolisme : Cystéine, Glutarédoxines, Oxidoreductases, Plastes, Protéines d'Arabidopsis, Protéines recombinantes, Thiorédoxines.
- Facteurs temps, Methionine Sulfoxide Reductases, Mutagenèse dirigée, Oxydoréduction, Spécificité du substrat, Transport d'électrons.
English descriptors
- KwdEn :
- Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Cysteine (genetics), Cysteine (metabolism), Electron Transport (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Methionine Sulfoxide Reductases (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plastids (enzymology), Plastids (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Substrate Specificity (MeSH), Thioredoxins (genetics), Thioredoxins (metabolism), Time Factors (MeSH).
- MESH :
- chemical , genetics : Arabidopsis Proteins, Cysteine, Glutaredoxins, Oxidoreductases, Recombinant Proteins, Thioredoxins.
- chemical , metabolism : Arabidopsis Proteins, Cysteine, Glutaredoxins, Oxidoreductases, Recombinant Proteins, Thioredoxins.
- enzymology : Plastids.
- metabolism : Plastids.
- Electron Transport, Methionine Sulfoxide Reductases, Mutagenesis, Site-Directed, Oxidation-Reduction, Substrate Specificity, Time Factors.
Abstract
Methionine sulfoxide reductases (MSRs) A and B reduce methionine sulfoxide (MetSO) S- and R-diastereomers, respectively, back to Met using electrons generally supplied by thioredoxin. The physiological reductants for MSRBs remain unknown in plants, which display a remarkable variety of thioredoxins (Trxs) and glutaredoxins (Grxs). Using recombinant proteins, we show that Arabidopsis plastidial MSRB1 and MSRB2, which differ regarding the number of presumed redox-active cysteines, possess specific reductants. Most simple-module Trxs, especially Trx m1 and Trx y2, are preferential and efficient electron donors towards MSRB2, while the double-module CDSP32 Trx and Grxs can reduce only MSRB1. This study identifies novel types of reductants, related to Grxs and peculiar Trxs, for MSRB proteins displaying only one redox-active cysteine.
DOI: 10.1016/j.febslet.2007.07.081
PubMed: 17761174
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(genetics)</term><term>Glutaredoxins (metabolism)</term><term>Methionine Sulfoxide Reductases (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Plastids (enzymology)</term><term>Plastids (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Substrate Specificity (MeSH)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cystéine (génétique)</term><term>Cystéine (métabolisme)</term><term>Facteurs temps (MeSH)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Methionine Sulfoxide Reductases (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Plastes (enzymologie)</term><term>Plastes (métabolisme)</term><term>Protéines d'Arabidopsis (génétique)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Arabidopsis Proteins</term><term>Cysteine</term><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>Cysteine</term><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Recombinant Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plastes</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plastids</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cystéine</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Protéines d'Arabidopsis</term><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plastids</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cystéine</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Plastes</term><term>Protéines d'Arabidopsis</term><term>Protéines recombinantes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Methionine Sulfoxide Reductases</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Substrate Specificity</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Facteurs temps</term><term>Methionine Sulfoxide Reductases</term><term>Mutagenèse dirigée</term><term>Oxydoréduction</term><term>Spécificité du substrat</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Methionine sulfoxide reductases (MSRs) A and B reduce methionine sulfoxide (MetSO) S- and R-diastereomers, respectively, back to Met using electrons generally supplied by thioredoxin. The physiological reductants for MSRBs remain unknown in plants, which display a remarkable variety of thioredoxins (Trxs) and glutaredoxins (Grxs). Using recombinant proteins, we show that Arabidopsis plastidial MSRB1 and MSRB2, which differ regarding the number of presumed redox-active cysteines, possess specific reductants. Most simple-module Trxs, especially Trx m1 and Trx y2, are preferential and efficient electron donors towards MSRB2, while the double-module CDSP32 Trx and Grxs can reduce only MSRB1. This study identifies novel types of reductants, related to Grxs and peculiar Trxs, for MSRB proteins displaying only one redox-active cysteine.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17761174</PMID><DateCompleted><Year>2008</Year><Month>01</Month><Day>07</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>581</Volume><Issue>23</Issue><PubDate><Year>2007</Year><Month>Sep</Month><Day>18</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Specificity of thioredoxins and glutaredoxins as electron donors to two distinct classes of Arabidopsis plastidial methionine sulfoxide reductases B.</ArticleTitle><Pagination><MedlinePgn>4371-6</MedlinePgn></Pagination><Abstract><AbstractText>Methionine sulfoxide reductases (MSRs) A and B reduce methionine sulfoxide (MetSO) S- and R-diastereomers, respectively, back to Met using electrons generally supplied by thioredoxin. The physiological reductants for MSRBs remain unknown in plants, which display a remarkable variety of thioredoxins (Trxs) and glutaredoxins (Grxs). Using recombinant proteins, we show that Arabidopsis plastidial MSRB1 and MSRB2, which differ regarding the number of presumed redox-active cysteines, possess specific reductants. Most simple-module Trxs, especially Trx m1 and Trx y2, are preferential and efficient electron donors towards MSRB2, while the double-module CDSP32 Trx and Grxs can reduce only MSRB1. This study identifies novel types of reductants, related to Grxs and peculiar Trxs, for MSRB proteins displaying only one redox-active cysteine.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Vieira Dos Santos</LastName><ForeName>Christina</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>CEA, DSV, IBEB, SBVME, Laboratoire d'Ecophysiologie Moléculaire des Plantes (LEMP), UMR 6191, 13108 Saint-Paul-lez-Durance Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Laugier</LastName><ForeName>Edith</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Tarrago</LastName><ForeName>Lionel</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Massot</LastName><ForeName>Vincent</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Issakidis-Bourguet</LastName><ForeName>Emmanuelle</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Rey</LastName><ForeName>Pascal</ForeName><Initials>P</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>2007</Year><Month>08</Month><Day>14</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 UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</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="D029681" MajorTopicYN="N">Arabidopsis 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Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018087" MajorTopicYN="N">Plastids</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate 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PubStatus="medline"><Year>2008</Year><Month>1</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>9</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17761174</ArticleId><ArticleId IdType="pii">S0014-5793(07)00842-3</ArticleId><ArticleId IdType="doi">10.1016/j.febslet.2007.07.081</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Saint-Paul-lez-Durance</li></settlement></list><tree><noCountry><name sortKey="Issakidis Bourguet, Emmanuelle" sort="Issakidis Bourguet, Emmanuelle" uniqKey="Issakidis Bourguet E" first="Emmanuelle" last="Issakidis-Bourguet">Emmanuelle Issakidis-Bourguet</name><name sortKey="Laugier, Edith" sort="Laugier, Edith" uniqKey="Laugier E" first="Edith" last="Laugier">Edith Laugier</name><name sortKey="Massot, Vincent" sort="Massot, Vincent" uniqKey="Massot V" first="Vincent" last="Massot">Vincent Massot</name><name sortKey="Rey, Pascal" sort="Rey, Pascal" uniqKey="Rey P" first="Pascal" last="Rey">Pascal Rey</name><name sortKey="Rouhier, Nicolas" sort="Rouhier, Nicolas" uniqKey="Rouhier N" first="Nicolas" last="Rouhier">Nicolas Rouhier</name><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Vieira Dos Santos, Christina" sort="Vieira Dos Santos, Christina" uniqKey="Vieira Dos Santos C" first="Christina" last="Vieira Dos Santos">Christina Vieira Dos Santos</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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