Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins.
Identifieur interne : 000A90 ( Main/Exploration ); précédent : 000A89; suivant : 000A91Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins.
Auteurs : Lionel Tarrago [France] ; Edith Laugier ; Mirko Zaffagnini ; Christophe Marchand ; Pierre Le Maréchal ; Nicolas Rouhier ; Stéphane D. Lemaire ; Pascal ReySource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2009.
Descripteurs français
- KwdFr :
- Arabidopsis (métabolisme), Catalyse (MeSH), Cinétique (MeSH), Cystéine (composition chimique), Glutarédoxines (métabolisme), Glutathion (composition chimique), Methionine Sulfoxide Reductases (MeSH), Modèles biologiques (MeSH), Mutagenèse dirigée (MeSH), Mutation (MeSH), Oxidoreductases (composition chimique), Phénomènes physiologiques des plantes (MeSH), Régénération (MeSH), Structure tertiaire des protéines (MeSH), Thiols (composition chimique), Thiorédoxines (composition chimique).
- MESH :
- composition chimique : Cystéine, Glutathion, Oxidoreductases, Thiols, Thiorédoxines.
- métabolisme : Arabidopsis, Glutarédoxines.
- Catalyse, Cinétique, Methionine Sulfoxide Reductases, Modèles biologiques, Mutagenèse dirigée, Mutation, Phénomènes physiologiques des plantes, Régénération, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Arabidopsis (metabolism), Catalysis (MeSH), Cysteine (chemistry), Glutaredoxins (metabolism), Glutathione (chemistry), Kinetics (MeSH), Methionine Sulfoxide Reductases (MeSH), Models, Biological (MeSH), Mutagenesis, Site-Directed (MeSH), Mutation (MeSH), Oxidoreductases (chemistry), Plant Physiological Phenomena (MeSH), Protein Structure, Tertiary (MeSH), Regeneration (MeSH), Sulfhydryl Compounds (chemistry), Thioredoxins (chemistry).
- MESH :
- chemical , chemistry : Cysteine, Glutathione, Oxidoreductases, Sulfhydryl Compounds, Thioredoxins.
- metabolism : Arabidopsis, Glutaredoxins.
- Catalysis, Kinetics, Methionine Sulfoxide Reductases, Models, Biological, Mutagenesis, Site-Directed, Mutation, Plant Physiological Phenomena, Protein Structure, Tertiary, Regeneration.
Abstract
Methionine oxidation leads to the formation of S- and R-diastereomers of methionine sulfoxide (MetSO), which are reduced back to methionine by methionine sulfoxide reductases (MSRs) A and B, respectively. MSRBs are classified in two groups depending on the conservation of one or two redox-active Cys; 2-Cys MSRBs possess a catalytic Cys-reducing MetSO and a resolving Cys, allowing regeneration by thioredoxins. The second type, 1-Cys MSRBs, possess only the catalytic Cys. The biochemical mechanisms involved in activity regeneration of 1-Cys MSRBs remain largely elusive. In the present work we used recombinant plastidial Arabidopsis thaliana MSRB1 and MSRB2 as models for 1-Cys and 2-Cys MSRBs, respectively, to delineate the Trx- and glutaredoxin-dependent reduction mechanisms. Activity assays carried out using a series of cysteine mutants and various reductants combined with measurements of free thiols under distinct oxidation conditions and mass spectrometry experiments show that the 2-Cys MSRB2 is reduced by Trx through a dithiol-disulfide exchange involving both redox-active Cys of the two partners. Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated. The deglutathionylation of MSRB1 is achieved by both mono- and dithiol glutaredoxins and involves only their N-terminal conserved catalytic Cys. This study proposes a detailed mechanism of the regeneration of 1-Cys MSRB activity by glutaredoxins, which likely constitute physiological reductants for this type of MSR.
DOI: 10.1074/jbc.M109.015487
PubMed: 19457862
PubMed Central: PMC2707211
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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MSRBs are classified in two groups depending on the conservation of one or two redox-active Cys; 2-Cys MSRBs possess a catalytic Cys-reducing MetSO and a resolving Cys, allowing regeneration by thioredoxins. The second type, 1-Cys MSRBs, possess only the catalytic Cys. The biochemical mechanisms involved in activity regeneration of 1-Cys MSRBs remain largely elusive. In the present work we used recombinant plastidial Arabidopsis thaliana MSRB1 and MSRB2 as models for 1-Cys and 2-Cys MSRBs, respectively, to delineate the Trx- and glutaredoxin-dependent reduction mechanisms. Activity assays carried out using a series of cysteine mutants and various reductants combined with measurements of free thiols under distinct oxidation conditions and mass spectrometry experiments show that the 2-Cys MSRB2 is reduced by Trx through a dithiol-disulfide exchange involving both redox-active Cys of the two partners. Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated. The deglutathionylation of MSRB1 is achieved by both mono- and dithiol glutaredoxins and involves only their N-terminal conserved catalytic Cys. This study proposes a detailed mechanism of the regeneration of 1-Cys MSRB activity by glutaredoxins, which likely constitute physiological reductants for this type of MSR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19457862</PMID><DateCompleted><Year>2009</Year><Month>09</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>284</Volume><Issue>28</Issue><PubDate><Year>2009</Year><Month>Jul</Month><Day>10</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Regeneration mechanisms of Arabidopsis thaliana methionine sulfoxide reductases B by glutaredoxins and thioredoxins.</ArticleTitle><Pagination><MedlinePgn>18963-71</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M109.015487</ELocationID><Abstract><AbstractText>Methionine oxidation leads to the formation of S- and R-diastereomers of methionine sulfoxide (MetSO), which are reduced back to methionine by methionine sulfoxide reductases (MSRs) A and B, respectively. MSRBs are classified in two groups depending on the conservation of one or two redox-active Cys; 2-Cys MSRBs possess a catalytic Cys-reducing MetSO and a resolving Cys, allowing regeneration by thioredoxins. The second type, 1-Cys MSRBs, possess only the catalytic Cys. The biochemical mechanisms involved in activity regeneration of 1-Cys MSRBs remain largely elusive. In the present work we used recombinant plastidial Arabidopsis thaliana MSRB1 and MSRB2 as models for 1-Cys and 2-Cys MSRBs, respectively, to delineate the Trx- and glutaredoxin-dependent reduction mechanisms. Activity assays carried out using a series of cysteine mutants and various reductants combined with measurements of free thiols under distinct oxidation conditions and mass spectrometry experiments show that the 2-Cys MSRB2 is reduced by Trx through a dithiol-disulfide exchange involving both redox-active Cys of the two partners. Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated. The deglutathionylation of MSRB1 is achieved by both mono- and dithiol glutaredoxins and involves only their N-terminal conserved catalytic Cys. This study proposes a detailed mechanism of the regeneration of 1-Cys MSRB activity by glutaredoxins, which likely constitute physiological reductants for this type of MSR.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tarrago</LastName><ForeName>Lionel</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Commissariat à l'Energie Atomique (Cadarache, France), Direction des Sciences du Vivant, Institut de Biologie Environnementale et Biotechnologie, Laboratoire d'Ecophysiologie Moléculaire des Plantes, 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>Zaffagnini</LastName><ForeName>Mirko</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Marchand</LastName><ForeName>Christophe</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Le Maréchal</LastName><ForeName>Pierre</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Rouhier</LastName><ForeName>Nicolas</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Lemaire</LastName><ForeName>Stéphane D</ForeName><Initials>SD</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>2009</Year><Month>05</Month><Day>20</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="D013438">Sulfhydryl Compounds</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>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</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="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018521" MajorTopicYN="N">Plant Physiological Phenomena</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012038" MajorTopicYN="Y">Regeneration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>5</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>5</Month><Day>22</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2009</Year><Month>9</Month><Day>2</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19457862</ArticleId><ArticleId 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Lemaire</name><name sortKey="Marchand, Christophe" sort="Marchand, Christophe" uniqKey="Marchand C" first="Christophe" last="Marchand">Christophe Marchand</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="Zaffagnini, Mirko" sort="Zaffagnini, Mirko" uniqKey="Zaffagnini M" first="Mirko" last="Zaffagnini">Mirko Zaffagnini</name></noCountry><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Tarrago, Lionel" sort="Tarrago, Lionel" uniqKey="Tarrago L" first="Lionel" last="Tarrago">Lionel Tarrago</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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