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Published on November 16, 2007; 10.1104/pp.107.106831

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Received August 3, 2007
Accepted November 2, 2007

Physiological roles of {beta}-substituted alanine synthase gene (Bsas) family in Arabidopsis thaliana

Mutsumi Watanabe , Miyako Kusano , Akira Oikawa , Atsushi Fukushima , Masaaki Noji , and Kazuki Saito *

Graduate School of Pharmaceutical Sciences, Chiba University, Yayoi-cho 1-33, Inage-ku, Chiba 263-8522, Japan; RIKEN Plant Science Center, Suehiro-cho 1-7-22, Tsurumi-ku, Yokohama, 230-0045, Japan; Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro-cho, Tokushima, 770-8514, Japan

* Corresponding author; email: ksaito{at}faculty.chiba-u.jp.

The {beta}-substituted alanine synthase (Bsas) family in the large super family of pyridoxal 5'-phosphate-dependent enzymes comprises cysteine (Cys) synthase (CSase) [O-acetylserine (thiol) lyase] and {beta}-cyanoalanine synthase (CASase) in plants. Nine genomic sequences encode putative Bsas proteins in Arabidopsis thaliana. The physiological roles of these Bsas isoforms in vivo were investigated by the characterization of T-DNA insertion mutants. The analyses of gene expression, activities of CSase and CASase, and levels of Cys and glutathione in the bsas mutants indicated that cytosolic Bsas1;1, plastidic Bsas2;1, and mitochondrial Bsas2;2 play major roles in Cys biosynthesis. Cytosolic Bsas1;1 has the most dominant contribution both in leaf and root, and mitochondrial Bsas2;2 plays a significant role in root. Mitochondrial Bsas3;1 is a genuine CASase. Non-targeted metabolome analyses of knockout mutants were carried out by a combination of gas chromatography time-of-flight mass spectrometry and capillary electrophoresis time-of-flight mass spectrometry. The level of {gamma}-glutamyl-{beta}-cyanoalanine decreased in the mutant bsas3;1, indicating the crucial role of Bsas3;1 in {beta}-cyanoalanine metabolism in vivo.




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