Document Detail


The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.
MedLine Citation:
PMID:  17217469     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Pascal Rey; Noëlle Bécuwe; Marie-Bénédicte Barrault; Dominique Rumeau; Michel Havaux; Benoît Biteau; Michel B Toledano
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-01-01
Journal Detail:
Title:  The Plant journal : for cell and molecular biology     Volume:  49     ISSN:  0960-7412     ISO Abbreviation:  Plant J.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-01-24     Completed Date:  2007-06-29     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  9207397     Medline TA:  Plant J     Country:  England    
Other Details:
Languages:  eng     Pagination:  505-14     Citation Subset:  IM    
Affiliation:
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:
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:
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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