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Entry URI http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u17475618i
Entry name Yang Wenyu et al. 2007 Jun. J. Biol. Chem. 282(25):18116-28.
Title AtPLAI is an acyl hydrolase involved in basal jasmonic acid production and Arabidopsis resistance to Botrytis cinerea.
Authors Devaiah Shivakumar P|Isaac Giorgis|Pan Xiangqing|Wang Xuemin|Welti Ruth|Yang Wenyu
Abstract Intracellular phospholipase A2 (PLA2) plays an important role in regulating oxylipin biosynthesis in mammals, but the molecular and biochemical nature of intracellular PLA2 is not well understood in plants. Arabidopsis thaliana gene At1g61850 (AtPLAI) encodes a 140-kDa protein that is most similar to mammalian calcium-independent PLA2, and additionally contains leucine-rich repeats and Armadillo repeats. AtPLAI hydrolyzes phospholipids at both the sn-1 and sn-2 positions, but prefers galactolipids to phospholipids as substrates. Profiling of lipid species altered in response to the necrotrophic fungus Botrytis cinerea revealed decreases in the levels of phosphatidylglycerol and digalactosyldiacylglycerol, suggesting that hydrolysis of plastidic polar lipids might provide precursors for pathogen-induced jasmonic acid (JA) production. Disruption of AtPLAI by T-DNA insertion reduced the basal level of JA, but did not impede pathogen-induced production of JA, free linolenic acid, or hydrolysis of plastidic lipids. Still, AtPLAI-deficient plants exhibited more damage than wild type plants after B. cinerea infection, and pretreatment of plants with methyl jasmonate alleviated pathogen damage to the mutant plants. The study shows that AtPLAI is an acyl hydrolase, rather than a specific phospholipase A. AtPLAI is involved in basal JA production and Arabidopsis resistance to the necrotrophic fungus B. cinerea.
Pubmed ID 17475618
Journal The Journal of biological chemistry
Volume 282
Issue 25
Pages 18116-28
Publication date 2007 Jun
Num of phenotype gene 0