title: The Arabidopsis thaliana sulfiredoxin is a plastidic cysteine-sulfinic acid reductase involved in the photooxidative stress response.
abstract: 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.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
authors.forename: Pascal
authors.initials: P
authors.lastname: Rey
authors.forename: Noëlle
authors.initials: N
authors.lastname: Bécuwe
authors.forename: Marie-Bénédicte
authors.initials: MB
authors.lastname: Barrault
authors.forename: Dominique
authors.initials: D
authors.lastname: Rumeau
authors.forename: Michel
authors.initials: M
authors.lastname: Havaux
authors.forename: Benoît
authors.initials: B
authors.lastname: Biteau
authors.forename: Michel B
authors.initials: MB
authors.lastname: Toledano
mesh_terms: D000222:Adaptation, Physiological; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000378:metabolism*; D002736:Chloroplasts / Q000201:enzymology*; D015870:Gene Expression; D006720:Homozygote; D008027:Light; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D009154:Mutation; D010084:Oxidation-Reduction; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D054464:Peroxiredoxins; D010641:Phenotype; D017386:Sequence Homology, Amino Acid; D013696:Temperature
chemical_list: D029681:Arabidopsis Proteins; D010544:Peroxidases; D054464:Peroxiredoxins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C520419:sulfiredoxin protein, Arabidopsis