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J. Biol. Chem., Vol. 278, Issue 24, 21370-21377, June 13, 2003

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Arabidopsis Mutants in Short- and Medium-chain Acyl-CoA Oxidase Activities Accumulate Acyl-CoAs and Reveal That Fatty Acid -Oxidation Is Essential for Embryo Development^*

Elizabeth L. Rylott, Caroline A. Rogers, Alison D. Gilday, Teresa Edgell, Tony R. Larson and Ian A Graham 

From the CNAP, Department of Biology, University of York, York YO10 5YW, United Kingdom

The short-chain acyl-CoA oxidase (ACX4) is one of a family of ACX genes that together catalyze the first step of peroxisomal fatty acid -oxidation during early, postgerminative growth in oilseed species. Here we have isolated and characterized an Arabidopsis thaliana mutant containing a T-DNA insert in ACX4. In acx4 seedlings, short-chain acyl-CoA oxidase activity was reduced by greater than 98%, whereas medium-chain activity was unchanged from wild type levels. Despite the almost complete loss of short-chain activity, lipid catabolism and seedling growth and establishment were unaltered in the acx4 mutant. However, the acx4 seedlings accumulated high levels (31 mol %) of short-chain acyl-CoAs and showed resistance to 2,4-dichlorophenoxybutyric acid, which is converted to the herbicide and auxin analogue 2,4-dichlorophenoxyacetic acid by -oxidation. A mutant in medium-chain length acyl-CoA activity (acx3) (1) shows a similar phenotype to acx4, and we show here that acx3 seedlings accumulate medium-chain length acyl-CoAs (16.4 mol %). The acx3 and acx4 mutants were crossed together, and remarkably, the acx3acx4 double mutants aborted during the first phase of embryo development. We propose that acx3acx4 double mutants are nonviable because they have a complete block in short-chain acyl-CoA oxidase activity. This is the first demonstration of the effects of eliminating (short-chain) -oxidation capacity in plants and shows that a functional -oxidation cycle is essential in the early stages of embryo development.

Received for publication, January 24, 2003 , and in revised form, April 2, 2003.

^* 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.

To whom all correspondence should be sent: CNAP, Dept. of Biology, University of York, P.O. Box 373, York YO10 5YW, UK. Tel.: 44-01904-328750; Fax: 44-01904-328762; E-mail: iag1{at}york.ac.uk.

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