691
Entry URI http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u18024555i
Entry name Watanabe Mutsumi et al. 2008 Jan. Plant Physiol. 146(1):310-20.
Title Physiological roles of the beta-substituted alanine synthase gene family in Arabidopsis.
Authors Fukushima Atsushi|Kusano Miyako|Noji Masaaki|Oikawa Akira|Saito Kazuki|Watanabe Mutsumi
Abstract The beta-substituted alanine (Ala) synthase (Bsas) family in the large superfamily of pyridoxal 5'-phosphate-dependent enzymes comprises cysteine (Cys) synthase (CSase) [O-acetyl-serine (thiol) lyase] and beta-cyano-Ala 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. 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. Nontargeted 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-cyano-Ala decreased in the mutant bsas3;1, indicating the crucial role of Bsas3;1 in beta-cyano-Ala metabolism in vivo.
Pubmed ID 18024555
Journal Plant physiology
Volume 146
Issue 1
Pages 310-20
Publication date 2008 Jan
Num of phenotype gene 0