Plant Physiology Preview
Published on February 24, 2002; 10.1104/pp.010621
Received July 13, 2001
Returned for revision September 21, 2001
Accepted November 27, 2001
The Endoplasmic Reticulum-Associated Maize GL8 Protein Is a
Component of the Acyl-Coenzyme A Elongase Involved in the Production of
Cuticular Waxes
Xiaojie Xu , Charles R. Dietrich , Rene Lessire , Basil J. Nikolau , and Patrick S. Schnable *
Department of Zoology and Genetics (X.X., C.R.D., P.S.S.), Interdepartmental Molecular, Cellular and Developmental Biology Program, (X.X.), Interdepartmental Plant Physiology Program (C.R.D), Department of Agronomy (P.S.S.), Department of Biochemistry Biophysics and Molecular Biology (B.J.N.), and Center for Plant Genomics (B.J.N., P.S.S.), Iowa State University, Ames, Iowa 50011; and Laboratoire de Biogenese Membranaire, Centre National de la Recherche Scientifique UMR 5544, Universite V. Segalen, Bordeaux 2, 146, 33076 Bordeaux cedex (R.L.)
* Corresponding author; email: schnable{at}iastate.edu.
The gl8 gene is required for the normal accumulation of cuticular waxes on maize (Zea mays) seedling leaves. The predicted GL8 protein exhibits significant sequence similarity to a class of enzymes that catalyze the reduction of a ketone group to a hydroxyl group. Polyclonal antibodies raised against the recombinant Escherichia coli-expressed GL8 protein were used to investigate the function of this protein in planta. Subcellular fractionation experiments indicate that the GL8 protein is associated with the endoplasmic reticulum membranes. Furthermore, polyclonal antibodies raised against the partially purified leek (Allium porrum) microsomal acyl-coenzyme A (CoA) elongase can react with the E. coli-expressed GL8 protein. In addition, anti-GL8 immunoglobulin G inhibited the in vitro elongation of stearoyl-CoA by leek and maize microsomal acyl-CoA elongase. In combination, these findings indicate that the GL8 protein is a component of the acyl-CoA elongase. In addition, the finding that anti-GL8 immunoglobulin G did not significantly inhibit the 3-ketoacyl-CoA synthase, 3-ketoacyl-CoA dehydrase, and (E) 2,3-enoyl-CoA reductase partial reactions of leek or maize acyl-CoA elongase lends further support to our previous hypothesis that the GL8 protein functions as a ß-ketoacyl reductase during the elongation of very long-chain fatty acids required for the production of cuticular waxes.
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