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Plant and Cell Physiology, 1999, Vol. 40, No. 5 477-481
© 1999

Molecular Cloning and Expression of Arabidopsis Fatty Acid Hydroperoxide Lyase

Kenji Matsui1, Jack Wilkinson2, Bill Hiatt2, Vic Knauf2 and Tadahiko Kajiwara1

1 Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University Yamaguchi, 753-8515 Japan
2 Calgene, LLC. 1920 Fifth Street, Davis, CA 95616 U.S.A.

Kenji Matsui, fax; +81-839-33-5820, e-mail; matsui{at}agr.yamaguchi-u.ac.jp

Fatty acid hydroperoxide lyase (HPOL), an enzyme of the octadecanoid pathway that forms carbon-6 aldehydes such as n-hexanal or (Z)-3-hexenal, was cloned from Arabidopsis thaliana as a full-length cDNA. The HPOL activity obtained by expressing the cDNA in Escherichia coli formed n-hexanal from linoleic acid 13-hydroperoxide, whereas linoleic acid 9-hydroperoxide was not a substrate for the enzyme. The HPOL mRNA is expressed at low level in leaves; however, its accumulation can be found in the inflorescence. Wounding or methyl jasmonate treatments increase the mRNA level in leaves. These results indicate that the HPOL gene is up-regulated in leaves in response to wounding and that the enzyme may be an active component of the octadecanoid defense response.

(Received October 7, 1998; Accepted February 19, 1999)
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