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First published online May 8, 2008; 10.1104/pp.108.117168 Plant Physiology 147:1325-1333 (2008) © 2008 American Society of Plant Biologists OPEN ACCESS ARTICLE
An Oleate Hydroxylase from the Fungus Claviceps purpurea: Cloning, Functional Analysis, and Expression in Arabidopsis[OA]Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, Saskatchewan, Canada S7N 5A8 (D.M., X.Q.); and Bioriginal Food and Science Corporation, Saskatoon, Saskatchewan, Canada S7N 0W9 (D.M.)
Claviceps purpurea, a fungal pathogen responsible for ergot diseases in many agriculturally important cereal crops, produces high levels of ricinoleic acid (12-hydroxyoctadec-cis-9-enoic acid) in its sclerotia. It has been believed for many years that the biosynthesis of this fatty acid in C. purpurea involves a hydration process with linoleic acid as the substrate. Using degenerate polymerase chain reaction, we cloned a gene from the sclerotia encoding an enzyme (CpFAH) that has high sequence similarity to the C. purpurea oleate desaturase, but only low similarity to plant oleate hydroxylases. Functional analysis of CpFAH in yeast (Saccharomyces cerevisiae) indicated it acted predominantly as a hydroxylase, introducing hydroxyl groups at the 12-position of oleic acid and palmitoleic acid. As well, it showed
The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Xiao Qiu (xiao.qiu{at}usask.ca). [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.108.117168 * Corresponding author; e-mail xiao.qiu{at}usask.ca. Received January 31, 2008; accepted April 28, 2008; published May 8, 2008.
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