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Published on September 3, 2004; 10.1104/pp.104.044842

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Received April 25, 2004
Returned for revision July 7, 2004
Accepted July 7, 2004

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

Ahmed Gaber , Kazuya Yoshimura , Masahiro Tamoi , Toru Takeda , Yoshihisa Nakano , and Shigeru Shigeoka *

Department of Applied Biological Chemistry, Osaka Prefecture University, Sakai 599-8531, Japan
Department of Food and Nutrition, Faculty of Agriculture, Kinki University, Nakamachi, Nara 631-8505, Japan

* Corresponding author; email: shigeoka{at}nara.kindai.ac.jp.

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{Delta}) 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.




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