Human peroxiredoxin 5 gene organization, initial characterization of its promoter and identification of alternative forms of mRNA.

Peroxiredoxin 5 (PRDX5) is a mammalian thioredoxin peroxidase ubiquitously expressed in tissues. Its role as antioxidant enzyme has been previously supported in different pathological situations. In this study, we determined the complete human PRDX5 genomic organization and isolated the 5'-flanking region of the gene.

Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat.

Human peroxiredoxin 5 is a recently discovered mitochondrial, peroxisomal and cytosolic thioredoxin peroxidase able to reduce hydrogen peroxide and alkyl hydroperoxides. To gain insight into peroxiredoxin 5 antioxidant role in cell protection, we investigated the resistance of yeast cells expressing human peroxiredoxin 5 in mitochondria or in the cytosol against oxidative stress induced by paraquat. The herbicide paraquat is a redox active drug known to generate superoxide anions in mitochondria and the cytosol of yeast and mammalian cells leading to the formation of several reactive oxygen species.

Alkyl hydroperoxide reductase 1 protects Saccharomyces cerevisiae against metal ion toxicity and glutathione depletion.

Alkyl hydroperoxide reductase 1 (Ahp1p) is a thioredoxin peroxidase of the peroxiredoxin family expressed by Saccharomyces cerevisiae. Recently, disruption of the AHP1 gene has shown that the gene is not essential for yeast growth on glucose medium but revealed a high sensitivity of null mutants to organic peroxides, suggesting that Ahp1p is an important enzyme implicated in oxidative stress protection in S. cerevisiae.