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ENVIRONMENTAL STRESS AND ADAPTATION

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 Stress¹

Department of Applied Biological Chemistry, Osaka Prefecture University, Sakai 599–8531, Japan (A.G., Y.N.); and Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nakamachi, Nara 631–8505, Japan (K.Y., M.T., T.T., S.S.)

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-2) 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 O₂ and the level of lipid peroxidation in the wild-type and each type of mutant cell after the application of t-butyl hydroperoxide or H₂O₂. 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.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.044842.

^* Corresponding author; e-mail shigeoka{at}nara.kindai.ac.jp; fax 81–742–43–2252.

Received April 25, 2004; returned for revision July 7, 2004; accepted July 7, 2004.

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