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J Biol Chem, Vol. 274, Issue 8, 4537-4544, February 19, 1999
,§,§
From the To isolate new antioxidant genes, we have
searched for activities that would rescue the tert-butyl
hydroperoxide (t-BOOH)-hypersensitive phenotype of a
Saccharomyces cerevisiae strain deleted for the gene
encoding the oxidative stress response regulator Skn7. We report the
characterization of AHP1, which encodes a 19-kDa protein similar to the AhpC/TSA protein family within a small region
encompassing Cys-62 of Ahp1p and the highly conserved N-terminal
catalytic AhpC/TSA cysteine. Ahp1p contains a peroxisomal sorting
signal, suggesting a peroxisomal localization. AHP1 exerts
strong antioxidant protective functions, as demonstrated both by gene
overexpression and deletion analyses, and is inducible by peroxides in
an Yap1- and Skn7-dependent manner. Similar to yeast Tsa1p,
Ahp1p forms a disulfide-linked homodimer upon oxidation and in
vivo requires the presence of the thioredoxin system but not of
glutathione to perform its antioxidant protective function.
Furthermore, in contrast to Tsa1p, which is specific for
H2O2, Ahp1p is specific for organic peroxides.
Therefore, with respect to substrate specificity, Ahp1p differs from
Tsa1p and is similar to prokaryotic alkyl hydroperoxide reductase AhpC.
These data suggest that Ahp1p is a yeast orthologue of prokaryotic AhpC
and justifies its name of yeast alkyl hydroperoxide reductase.
Department of Pharmacology and Toxicology,
College of Pharmacy, Rutgers University, Piscataway, New Jersey
08855 and § Service de Biochimie et Génétique
Moléculaire, Bât 142, CEA-Saclay,
F-91191 Gif-sur-Yvette Cedex, France
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