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J. Biol. Chem., Vol. 281, Issue 44, 33511-33520, November 3, 2006

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Identification of a Peroxisomal Acyl-activating Enzyme Involved in the Biosynthesis of Jasmonic Acid in Arabidopsis^*

Abraham J. K. Koo, Hoo Sun Chung, Yuichi Kobayashi^¶, and Gregg A. Howe¹

From the Department of Energy-Plant Research Laboratory, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824 and the ^¶Department of Biological Engineering, Tokyo Institute of Technology, 4259-B52 Nagatsuta-cho, Midori-ku, Yokohama 226-8501, Japan

Jasmonic acid (JA) is a lipid-derived signal that regulates a wide variety of developmental and defense-related processes in higher plants. JA is synthesized from linolenic acid via an enzymatic pathway that initiates in the plastid and terminates in peroxisomes. The C18 JA precursor 12-oxo-phytodienoic acid (OPDA) is converted in the peroxisome to 3-oxo-2-(2'-[Z]-pentenyl)cyclopentane-1-octanoic acid (OPC-8:0), which subsequently undergoes three rounds of -oxidation to yield JA. Although most JA biosynthetic enzymes have been identified, several key steps in the pathway remain to be elucidated. To address this knowledge gap, we employed co-expression analysis to identify genes that are coordinately regulated with known JA biosynthetic components in Arabidopsis. Among the candidate genes uncovered by this approach was a 4-coumarate-CoA ligase-like member of the acyl-activating enzyme (AAE) gene family, which we have named OPC-8:0 CoA Ligase1 (OPCL1). In response to wounding, opcl1 null mutants exhibited reduced levels of JA and hyperaccumulation of OPC-8:0. Recombinant OPCL1 was active against both OPDA and OPC-8:0, as well as medium-to-long straight-chain fatty acids. Subcellular localization studies with green fluorescent protein-tagged OPCL1 showed that the protein is targeted to peroxisomes. These findings establish a physiological role for OPCL1 in the activation of JA biosynthetic precursors in leaf peroxisomes, and further indicate that OPC-8:0 is a physiological substrate for the activation step. The results also demonstrate the utility of co-expression analysis for identification of factors that contribute to jasmonate homeostasis.

Received for publication, August 16, 2006 , and in revised form, September 7, 2006.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) EF014466 [GenBank] .

^* This work was supported in part by National Institutes of Health Grant R01GM57795 and United States Department of Energy Grant DE-FG02-91ER20021 (to G. A. H.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables S1 and S2 and Figs. S1 and S2.

This article was selected as a Paper of the Week.

¹ To whom correspondence should be addressed: Dept. of Energy-Plant Research Laboratory, Michigan State University, East Lansing, MI 48824-1312. Tel.: 517-355-5159; Fax: 517-353-9168; E-mail: howeg{at}msu.edu.

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