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Synechocystis PCC 6803 contains two types of glutathione peroxidase-like proteins (GPX-1 and GPX-2) that utilize NADPH but not reduced glutathione and unsaturated fatty acid hydroperoxides or alkyl hydroperoxides. The steady-state transcript level of gpx-1 gradually increased under oxidative stress conditions imposed by high light intensity, high salinity, or application of methylviologen or t-butyl hydroperoxide in the wild-type and GPX-2 knock-out mutant (gpx-2Delta) cells. To examine the ability of GPX-1, GPX-2, and thioredoxin peroxidase to scavenge lipid hydroperoxide in vivo, we measured the photosynthetic evolution of O(2) and the level of lipid peroxidation in the wild-type and each type of mutant cell after the application of t-butyl hydroperoxide or H(2)O(2). The data reported here indicate that GPX-1 and GPX-2 are essential for the removal of lipid hydroperoxides under normal and stress conditions, leading to the protection of membrane integrity.

plant physiology

Induction and Functional Analysis of Two Reduced Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutathione Peroxidase-Like Proteins in <i>Synechocystis</i> PCC 6803 during the Progression of Oxidative Stress

Induction and Functional Analysis of Two Reduced Nicotinamide Adenine Dinucleotide Phosphate-Dependent Glutathione Peroxidase-Like Proteins in Synechocystis PCC 6803 during the Progression of Oxidative Stress