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J. Biol. Chem., Vol. 282, Issue 23, 17002-17013, June 8, 2007

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Arabidopsis thaliana Squalene Epoxidase 1 Is Essential for Root and Seed Development^*

Jeanne M. Rasbery¹, Hui Shan, Renee J. LeClair², Michael Norman³, Seiichi P. T. Matsuda, and Bonnie Bartel⁴

From the Department of Biochemistry and Cell Biology and the Department of Chemistry, Rice University, Houston, Texas, 77005

Squalene epoxidase converts squalene into oxidosqualene, the precursor of all known angiosperm cyclic triterpenoids, which include membrane sterols, brassinosteroid phytohormones, and non-steroidal triterpenoids. In this work, we have identified six putative Arabidopsis squalene epoxidase (SQE) enzymes and used heterologous expression in yeast to demonstrate that three of these enzymes, SQE1, SQE2, and SQE3, can epoxidize squalene. We isolated and characterized Arabidopsis sqe1 mutants and discovered severe developmental defects, including reduced root and hypocotyl elongation. Adult sqe1–3 and sqe1–4 plants have diminished stature and produce inviable seeds. The sqe1–3 mutant accumulates squalene, consistent with a block in the triterpenoid biosynthetic pathway. Therefore, SQE1 function is necessary for normal plant development, and the five SQE-like genes remaining in this mutant are not fully redundant with SQE1.

Received for publication, December 26, 2006 , and in revised form, March 29, 2007.

^* This work was supported by grants from the National Science Foundation (MCB-0209769) and the Robert A. Welch Foundation (C-1323 and C-1309). 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 Fig. 1.

¹ Supported, in part, by a training grant from the National Institutes of Health (T32-GM08362).

² Present address: Maine Medical Ctr. Research Institute, 81 Research Dr., Scarborough, ME 04074.

³ Present address: Dept. of Chemistry, Box 90354, Duke University, Durham, NC 27708.

⁴ To whom correspondence should be addressed: Dept. of Biochemistry and Cell Biology, 6100 Main St., Houston, TX, 77005. Tel.: 713-348-5602; Fax: 713-348-5154; E-mail: bartel{at}rice.edu.

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