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ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

Arabidopsis PPR40 Connects Abiotic Stress Responses to Mitochondrial Electron Transport^1,[W],[OA]

Institute of Plant Biology (L.Z., G.R., G.S., K.Ö., C.K., L.S.), and Proteomics Research Group (Z.D., K.F.M.), Biological Research Centre, Hungarian Academy of Sciences, 6726–Szeged, Hungary; Department of Applied Biotechnology and Food Science, Laboratory of Biochemistry and Molecular Biology, Budapest University of Technology and Economics, 1111–Budapest, Hungary (A.S.); Pathobiochemistry Research Group, Hungarian Academy of Sciences and Semmelweis University, 1111–Budapest, Hungary (A.S.); Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143–0446 (K.F.M.); and Max-Planck-Institut für Züchtungsforschung, D–50829 Cologne, Germany (C.K., Z.K.)

Oxidative respiration produces adenosine triphosphate through the mitochondrial electron transport system controlling the energy supply of plant cells. Here we describe a mitochondrial pentatricopeptide repeat (PPR) domain protein, PPR40, which provides a signaling link between mitochondrial electron transport and regulation of stress and hormonal responses in Arabidopsis (Arabidopsis thaliana). Insertion mutations inactivating PPR40 result in semidwarf growth habit and enhanced sensitivity to salt, abscisic acid, and oxidative stress. Genetic complementation by overexpression of PPR40 complementary DNA restores the ppr40 mutant phenotype to wild type. The PPR40 protein is localized in the mitochondria and found in association with Complex III of the electron transport system. In the ppr40-1 mutant the electron transport through Complex III is strongly reduced, whereas Complex IV is functional, indicating that PPR40 is important for the ubiqinol-cytochrome c oxidoreductase activity of Complex III. Enhanced stress sensitivity of the ppr40-1 mutant is accompanied by accumulation of reactive oxygen species, enhanced lipid peroxidation, higher superoxide dismutase activity, and altered activation of several stress-responsive genes including the alternative oxidase AOX1d. These results suggest a close link between regulation of oxidative respiration and environmental adaptation in Arabidopsis.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: László Szabados (szabados{at}brc.hu).

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www.plantphysiol.org/cgi/doi/10.1104/pp.107.111260

^* Corresponding author; e-mail szabados{at}brc.hu.

Received October 20, 2007; accepted February 20, 2008; published February 27, 2008.

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