| The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response. | |
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MedLine Citation:
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PMID: 17217469 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The 2-cysteine peroxiredoxins (2-Cys-Prxs) are antioxidants that reduce peroxides through a thiol-based mechanism. During catalysis, these ubiquitous enzymes are occasionally inactivated by the substrate-dependent oxidation of the catalytic cysteine to the sulfinic acid (-SO2H) form, and are reactivated by reduction by sulfiredoxin (Srx), an enzyme recently identified in yeast and in mammal cells. In plants, 2-Cys-Prxs constitute the most abundant Prxs and are located in chloroplasts. Here we have characterized the unique Srx gene in Arabidopsis thaliana (AtSrx) from a functional point of view, and analyzed the phenotype of two AtSrx knockout (AtSrx-) mutant lines. AtSrx is a chloroplastic enzyme displaying sulfinic acid reductase activity, as shown by the ability of the recombinant AtSrx to reduce the overoxidized 2-Cys-Prx form in vitro, and by the accumulation of the overoxidized Prx in mutant lines lacking Srx in vivo. Furthermore, AtSrx mutants exhibit an increased tolerance to photooxidative stress generated by high light combined with low temperature. These data establish that, as in yeast and in mammals, plant 2-Cys-Prxs are subject to substrate-mediated inactivation reversed by Srx, and suggest that the 2-Cys-Prx redox status and sulfiredoxin are parts of a signaling mechanism participating in plant responses to oxidative stress. |
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Authors:
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Pascal Rey; Noëlle Bécuwe; Marie-Bénédicte Barrault; Dominique Rumeau; Michel Havaux; Benoît Biteau; Michel B Toledano |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2007-01-01 |
Journal Detail:
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Title: The Plant journal : for cell and molecular biology Volume: 49 ISSN: 0960-7412 ISO Abbreviation: Plant J. Publication Date: 2007 Feb |
Date Detail:
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Created Date: 2007-01-24 Completed Date: 2007-06-29 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 9207397 Medline TA: Plant J Country: England |
Other Details:
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Languages: eng Pagination: 505-14 Citation Subset: IM |
Affiliation:
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CEA, DSV, DEVM, LEMP, Laboratoire d'Ecophysiologie Moléculaire des Plantes, UMR 6191 CNRS-CEA-Université de la Méditerranée, 13108 Saint-Paul-lez-Durance, Cedex, France. pascal.rey@cea.fr |
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| MeSH Terms | |
Descriptor/Qualifier:
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Adaptation, Physiological Amino Acid Sequence Arabidopsis / enzymology* Arabidopsis Proteins / metabolism* Chloroplasts / enzymology* Gene Expression Homozygote Light Molecular Sequence Data Mutagenesis, Insertional Mutation Oxidation-Reduction Oxidoreductases Acting on Sulfur Group Donors / metabolism* Peroxidases / metabolism* Peroxiredoxins Phenotype Sequence Homology, Amino Acid Temperature |
| Chemical | |
Reg. No./Substance:
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0/Arabidopsis Proteins; EC 1.11.1.-/Peroxidases; EC 1.11.1.15/Peroxiredoxins; EC 1.8.-/Oxidoreductases Acting on Sulfur Group Donors; EC 1.8.98.2/sulfiredoxin protein, Arabidopsis |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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