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J. Biol. Chem., Vol. 282, Issue 25, 18116-18128, June 22, 2007

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AtPLAI Is an Acyl Hydrolase Involved in Basal Jasmonic Acid Production and Arabidopsis Resistance to Botrytis cinerea^*

Wenyu Yang, Shivakumar P. Devaiah, Xiangqing Pan, Giorgis Isaac^¶, Ruth Welti^¶, and Xuemin Wang¹

From the Department of Biology, University of Missouri, St. Louis, Missouri 63121, the Donald Danforth Plant Science Center, St. Louis, Missouri 63132, and the ^¶Kansas Lipidomics Research Center, Division of Biology, Kansas State University, Manhattan, Kansas 66506

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.

Received for publication, January 16, 2007 , and in revised form, May 2, 2007.

^* This work was supported by the National Science Foundation Grants MCB-0455318 and IOB-0454866. The Kansas Lipidomics Research Center Analytical Laboratory was supported by National Science Foundation EPSCoR program Grant EPS-0236913 with matching support from the State of Kansas through the Kansas Technology Enterprise Corporation and Kansas State University. The Kansas Lipidomics Research Center also received Core Facility support from K-IDeA Networks of Biomedical Research Excellence (INBRE) through National Institutes of Health Grant P20RR16475 from the INBRE program of the National Center for Research Resources. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Tel.: 314-587-1419; Fax: 314-587-1519; E-mail: wangxue{at}umsl.edu.

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