A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2.
Identifieur interne : 000894 ( Main/Exploration ); précédent : 000893; suivant : 000895A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2.
Auteurs : Christophe Riondet [France] ; Jean Paul Desouris ; Jocelyne Guilleminot Montoya ; Yvette Chartier ; Yves Meyer ; Jean-Philippe ReichheldSource :
- Plant, cell & environment [ 1365-3040 ] ; 2012.
Descripteurs français
- KwdFr :
- Arabidopsis (enzymologie), Arabidopsis (génétique), Délétion de séquence (MeSH), Fer (métabolisme), Ferrosulfoprotéines (composition chimique), Ferrosulfoprotéines (métabolisme), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Magnoliopsida (enzymologie), Magnoliopsida (génétique), Modèles moléculaires (MeSH), Multimérisation de protéines (MeSH), Mutagenèse dirigée (MeSH), Oxydoréduction (MeSH), Phylogenèse (MeSH), Phénotype (MeSH), Plant (génétique), Plant (métabolisme), Pollinisation (MeSH), Protéines d'Arabidopsis (génétique), Protéines d'Arabidopsis (métabolisme), Protéines recombinantes (MeSH), Stabilité protéique (MeSH), Stress oxydatif (MeSH), Test de complémentation (MeSH).
- MESH :
- composition chimique : Ferrosulfoprotéines.
- enzymologie : Arabidopsis, Magnoliopsida.
- génétique : Arabidopsis, Glutarédoxines, Magnoliopsida, Plant, Protéines d'Arabidopsis.
- métabolisme : Fer, Ferrosulfoprotéines, Glutarédoxines, Plant, Protéines d'Arabidopsis.
- Délétion de séquence, Modèles moléculaires, Multimérisation de protéines, Mutagenèse dirigée, Oxydoréduction, Phylogenèse, Phénotype, Pollinisation, Protéines recombinantes, Stabilité protéique, Stress oxydatif, Test de complémentation.
English descriptors
- KwdEn :
- Arabidopsis (enzymology), Arabidopsis (genetics), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Genetic Complementation Test (MeSH), Glutaredoxins (genetics), Glutaredoxins (metabolism), Iron (metabolism), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (metabolism), Magnoliopsida (enzymology), Magnoliopsida (genetics), Models, Molecular (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Phenotype (MeSH), Phylogeny (MeSH), Pollination (MeSH), Protein Multimerization (MeSH), Protein Stability (MeSH), Recombinant Proteins (MeSH), Seedlings (genetics), Seedlings (metabolism), Sequence Deletion (MeSH).
- MESH :
- chemical , chemistry : Iron-Sulfur Proteins.
- chemical , genetics : Arabidopsis Proteins, Glutaredoxins.
- enzymology : Arabidopsis, Magnoliopsida.
- genetics : Arabidopsis, Magnoliopsida, Seedlings.
- chemical , metabolism : Arabidopsis Proteins, Glutaredoxins, Iron, Iron-Sulfur Proteins, Seedlings.
- Genetic Complementation Test, Models, Molecular, Mutagenesis, Site-Directed, Oxidation-Reduction, Oxidative Stress, Phenotype, Phylogeny, Pollination, Protein Multimerization, Protein Stability, Recombinant Proteins, Sequence Deletion.
Abstract
The major known function of glutaredoxins (Grxs) is to reduce disulphide bridges. Recently, some have also been shown to interact with iron-sulphur clusters. These can be classified in two subgroups: class II Grx are found in all living organisms and are implicated in assembly of iron-sulphur clusters, while class I Grx are represented by only two members known to form a holodimer structure containing a cluster in vitro, but with an unknown function different from class II. Here, we report that in eukaryotic plants, GRXC1 (class I) orthologs are exclusively present in dicotyledonous plants, suggesting a specific function. Indeed, in Arabidopsis thaliana, reducing activity of recombinant GRXC1 is regulated by redox-dependent stability of the cluster. In planta, GRXC1 has been found predominantly in a holodimeric form, indicating the presence of the cluster in vivo. This suggests that GRXC1 acts as a redox sensor, reducing downstream pathways under oxidative conditions. GRXC2, the closest homolog of GRXC1, is unable to form a cluster in vitro. Knock-out mutants in grxc1 or grxc2 are aphenotypic, but the double mutant produces a lethal phenotype at an early stage after pollinization, suggesting that GRXC1 and GRXC2 share redundant and vital functions.
DOI: 10.1111/j.1365-3040.2011.02355.x
PubMed: 21767278
Affiliations:
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xml:lang="en"><term>Genetic Complementation Test</term><term>Models, Molecular</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Phenotype</term><term>Phylogeny</term><term>Pollination</term><term>Protein Multimerization</term><term>Protein Stability</term><term>Recombinant Proteins</term><term>Sequence Deletion</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de séquence</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Mutagenèse dirigée</term><term>Oxydoréduction</term><term>Phylogenèse</term><term>Phénotype</term><term>Pollinisation</term><term>Protéines recombinantes</term><term>Stabilité protéique</term><term>Stress oxydatif</term><term>Test de complémentation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The major known function of glutaredoxins (Grxs) is to reduce disulphide bridges. Recently, some have also been shown to interact with iron-sulphur clusters. These can be classified in two subgroups: class II Grx are found in all living organisms and are implicated in assembly of iron-sulphur clusters, while class I Grx are represented by only two members known to form a holodimer structure containing a cluster in vitro, but with an unknown function different from class II. Here, we report that in eukaryotic plants, GRXC1 (class I) orthologs are exclusively present in dicotyledonous plants, suggesting a specific function. Indeed, in Arabidopsis thaliana, reducing activity of recombinant GRXC1 is regulated by redox-dependent stability of the cluster. In planta, GRXC1 has been found predominantly in a holodimeric form, indicating the presence of the cluster in vivo. This suggests that GRXC1 acts as a redox sensor, reducing downstream pathways under oxidative conditions. GRXC2, the closest homolog of GRXC1, is unable to form a cluster in vitro. Knock-out mutants in grxc1 or grxc2 are aphenotypic, but the double mutant produces a lethal phenotype at an early stage after pollinization, suggesting that GRXC1 and GRXC2 share redundant and vital functions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21767278</PMID><DateCompleted><Year>2014</Year><Month>06</Month><Day>06</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-3040</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>2</Issue><PubDate><Year>2012</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant, cell & environment</Title><ISOAbbreviation>Plant Cell Environ</ISOAbbreviation></Journal><ArticleTitle>A dicotyledon-specific glutaredoxin GRXC1 family with dimer-dependent redox regulation is functionally redundant with GRXC2.</ArticleTitle><Pagination><MedlinePgn>360-73</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1365-3040.2011.02355.x</ELocationID><Abstract><AbstractText>The major known function of glutaredoxins (Grxs) is to reduce disulphide bridges. Recently, some have also been shown to interact with iron-sulphur clusters. These can be classified in two subgroups: class II Grx are found in all living organisms and are implicated in assembly of iron-sulphur clusters, while class I Grx are represented by only two members known to form a holodimer structure containing a cluster in vitro, but with an unknown function different from class II. Here, we report that in eukaryotic plants, GRXC1 (class I) orthologs are exclusively present in dicotyledonous plants, suggesting a specific function. Indeed, in Arabidopsis thaliana, reducing activity of recombinant GRXC1 is regulated by redox-dependent stability of the cluster. In planta, GRXC1 has been found predominantly in a holodimeric form, indicating the presence of the cluster in vivo. This suggests that GRXC1 acts as a redox sensor, reducing downstream pathways under oxidative conditions. GRXC2, the closest homolog of GRXC1, is unable to form a cluster in vitro. Knock-out mutants in grxc1 or grxc2 are aphenotypic, but the double mutant produces a lethal phenotype at an early stage after pollinization, suggesting that GRXC1 and GRXC2 share redundant and vital functions.</AbstractText><CopyrightInformation>© 2011 Blackwell Publishing Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Riondet</LastName><ForeName>Christophe</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Laboratoire Génome et Développement des Plantes, UMR 5096 CNRS-UPVD, 58 Avenue de Villeneuve - Bat T, 66860 Perpignan Cedex, France. christophe.riondet@univperp.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Desouris</LastName><ForeName>Jean Paul</ForeName><Initials>JP</Initials></Author><Author ValidYN="Y"><LastName>Montoya</LastName><ForeName>Jocelyne Guilleminot</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Chartier</LastName><ForeName>Yvette</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Meyer</LastName><ForeName>Yves</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Reichheld</LastName><ForeName>Jean-Philippe</ForeName><Initials>JP</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>2011</Year><Month>07</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Cell Environ</MedlineTA><NlmUniqueID>9309004</NlmUniqueID><ISSNLinking>0140-7791</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis 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MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></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="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019684" MajorTopicYN="N">Magnoliopsida</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054817" MajorTopicYN="N">Pollination</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055550" MajorTopicYN="N">Protein Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D036226" MajorTopicYN="N">Seedlings</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017384" MajorTopicYN="N">Sequence Deletion</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>7</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>6</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21767278</ArticleId><ArticleId IdType="doi">10.1111/j.1365-3040.2011.02355.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Languedoc-Roussillon</li><li>Occitanie (région administrative)</li></region><settlement><li>Perpignan</li></settlement></list><tree><noCountry><name sortKey="Chartier, Yvette" sort="Chartier, Yvette" uniqKey="Chartier Y" first="Yvette" last="Chartier">Yvette Chartier</name><name sortKey="Desouris, Jean Paul" sort="Desouris, Jean Paul" uniqKey="Desouris J" first="Jean Paul" last="Desouris">Jean Paul Desouris</name><name sortKey="Meyer, Yves" sort="Meyer, Yves" uniqKey="Meyer Y" first="Yves" last="Meyer">Yves Meyer</name><name sortKey="Montoya, Jocelyne Guilleminot" sort="Montoya, Jocelyne Guilleminot" uniqKey="Montoya J" first="Jocelyne Guilleminot" last="Montoya">Jocelyne Guilleminot Montoya</name><name sortKey="Reichheld, Jean Philippe" sort="Reichheld, Jean Philippe" uniqKey="Reichheld J" first="Jean-Philippe" last="Reichheld">Jean-Philippe Reichheld</name></noCountry><country name="France"><region name="Occitanie (région administrative)"><name sortKey="Riondet, Christophe" sort="Riondet, Christophe" uniqKey="Riondet C" first="Christophe" last="Riondet">Christophe Riondet</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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