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Originally published In Press as doi:10.1074/jbc.M207234200 on September 25, 2002

J. Biol. Chem., Vol. 277, Issue 48, 46051-46058, November 29, 2002
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Identification of a Jasmonate-regulated Allene Oxide Synthase That Metabolizes 9-Hydroperoxides of Linoleic and Linolenic Acids*

Aya ItohDagger §, Anthony L. SchilmillerDagger §||, Bonnie C. McCaigDagger , and Gregg A. HoweDagger ||**

From the Dagger  Department of Energy Plant Research Laboratory and || Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 48824-1312

Allene oxide synthase (AOS) is a cytochrome P-450 (CYP74A) that catalyzes the first step in the conversion of 13-hydroperoxy linolenic acid to jasmonic acid and related signaling molecules in plants. Here, we report the molecular cloning and characterization of a novel AOS-encoding cDNA (LeAOS3) from Lycopersicon esculentum whose predicted amino acid sequence classifies it as a member of the CYP74C subfamily of enzymes that was hitherto not known to include AOSs. Recombinant LeAOS3 expressed in Escherichia coli showed spectral characteristics of a P-450. The enzyme transformed 9- and 13-hydroperoxides of linoleic and linolenic acid to alpha -ketol, gamma -ketol, and cyclopentenone compounds that arise from spontaneous hydrolysis of unstable allene oxides, indicating that the enzyme is an AOS. Kinetic assays demonstrated that LeAOS3 was approx 10-fold more active against 9-hydroperoxides than the corresponding 13-isomers. LeAOS3 transcripts accumulated in roots, but were undetectable in aerial parts of mature plants. In contrast to wild-type plants, LeAOS3 expression was undetectable in roots of a tomato mutant that is defective in jasmonic acid signaling. These findings suggest that LeAOS3 plays a role in the metabolism of 9-lipoxygenase-derived hydroperoxides in roots, and that this branch of oxylipin biosynthesis is regulated by the jasmonate signaling cascade.

* This work was supported by grants from the Division of Energy Biosciences, the United States Department of Energy (DE-FG02-91ER20021), and Michigan Life Science Corridor (78341) (to G. A. H.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF454634.

§ These authors contributed equally to this work.

Present address: Dept. of Environmental Information and Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997-0017, Japan.

** To whom correspondence should be addressed: MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824-1312. Tel.: 517-355-5159; Fax: 517-353-9168; E-mail: howeg@msu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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