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First published online July 25, 2002; 10.1104/pp.003251

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Plant Physiol, August 2002, Vol. 129, pp. 1700-1709

Fatty Acid Export from the Chloroplast. Molecular Characterization of a Major Plastidial Acyl-Coenzyme A Synthetase from Arabidopsis1

Judy A. Schnurr, Jay M. Shockey, Gert-Jan de Boer, and John A. Browse*

Institute of Biological Chemistry, Washington State University, P.O. Box 646340, Pullman, Washington 99164-6340 (J.A.S., J.M.S., J.A.B.); and Department of Plant Biology, Carnegie Institution of Washington, 260 Panama Street, Stanford, California 94305 (G.-J.d.B.)

Acyl-coenzyme A (CoA) synthetases (ACSs, EC 6.2.1.3) catalyze the formation of fatty acyl-CoAs from free fatty acid, ATP, and CoA. Essentially all de novo fatty acid synthesis occurs in the plastid. Fatty acids destined for membrane glycerolipid and triacylglycerol synthesis in the endoplasmic reticulum must be first activated to acyl-CoAs via an ACS. Within a family of nine ACS genes from Arabidopsis, we identified a chloroplast isoform, LACS9. LACS9 is highly expressed in developing seeds and young rosette leaves. Both in vitro chloroplast import assays and transient expression of a green fluorescent protein fusion indicated that the LACS9 protein is localized in the plastid envelope. A T-DNA knockout mutant (lacs9-1) was identified by reverse genetics and these mutant plants were indistinguishable from wild type in growth and appearance. Analysis of leaf lipids provided no evidence for compromised export of acyl groups from chloroplasts. However, direct assays demonstrated that lacs9-1 plants contained only 10% of the chloroplast long-chain ACS activity found for wild type. The residual long-chain ACS activity in mutant chloroplasts was comparable with calculated rates of fatty acid synthesis. Although another isozyme contributes to the activation of fatty acids during their export from the chloroplast, LACS9 is a major chloroplast ACS.

1 This work was supported by The Dow Chemical Company/Dow AgroSciences, by the U.S. National Science Foundation (grant no. IBN-0084329), by the Agricultural Research Center, Washington State University, and by the U.S. Department of Energy (to G.-J.d.B. under grant no. DE-FG02-94ER20133 to Chris Somerville [Carnegie Institution of Washington]).

* Corresponding author; e-mail jab{at}wsu.edu; fax 509-335-7643.

© 2002 American Society of Plant Physiologists


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