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Published on November 18, 2005; 10.1104/pp.105.070391

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Received August 24, 2005
Returned for revision September 28, 2005
Accepted October 4, 2005

Protection against Photooxidative Injury of Tobacco Leaves by 2-Alkenal Reductase. Detoxication of Lipid Peroxide-Derived Reactive Carbonyls

Jun'ichi Mano *, Enric Belles-Boix , Elena Babiychuk , Dirk Inzé , Yoshimitsu Torii , Eiji Hiraoka , Koichi Takimoto , Luit Slooten , Kozi Asada , and Sergei Kushnir

Science Research Center, Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8515, Japan; Faculty of Agriculture, Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8515, Japan
Department of Plant Systems Biology, Flanders Interuniversity Institute for Biotechnology, Ghent University, B-9052 Ghent, Belgium
Faculty of Agriculture, Yamaguchi University, Yoshida 1677-1, Yamaguchi 753-8515, Japan
Vrije Universiteit Brussel, Laboratorium voor Biofysica, 1050 Brussels, Belgium
Faculty of Life Science and Biotechnology, Fukuyama University, Fukuyama 729-0292, Japan

* Corresponding author; email: mano{at}yamaguchi-u.ac.jp.

Degradation of lipid peroxides leads to the formation of cytotoxic 2-alkenals and oxenes (collectively designated reactive carbonyls). The novel NADPH-dependent oxidoreductase 2-alkenal reductase (AER; EC 1.3.1.74) from Arabidopsis (Arabidopsis thaliana), which is encoded by the gene At5g16970, catalyzes the reduction of the {alpha},{beta}-unsaturated bond of reactive carbonyls, and hence is presumed to function in antioxidative defense in plants. Here we show that Arabidopsis AER (At-AER) has a broad substrate spectrum to biologically relevant reactive carbonyls. Besides 2-alkenals, the enzyme recognized as substrates the lipid peroxide-derived oxenes 9-oxo-octadeca-(10E),(12Z)-dienoic acid and 13-oxo-octadeca-(9E),(11Z)-dienoic acid, as well as the potent genotoxin 4-oxo-(2E)-nonenal, altogether suggesting AER has a key role in the detoxification of reactive carbonyls. To validate this conclusion by in vivo studies, transgenic tobacco (Nicotiana tabacum) plants that had 100- to 250-fold higher AER activity levels than control plants were generated. The engineered plants exhibited significantly less damage from either (1) the exogenously administered 4-hydroxy-(2E)-nonenal, (2) treatment with methyl viologen plus light, or (3) intense light. We further show that the At-AER protein fused with the Aequorea victoria green fluorescent protein localizes in cytosol and the nucleus in Bright-Yellow 2 cells. These results indicate that reactive carbonyls mediate photooxidative injury in leaf cells, and At-AER in the cytosol protects the cells by reducing the {alpha},{beta}-unsaturated bond of the photoproduced reactive carbonyls.




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