First published online February 24, 2002; 10.1104/pp.010621
Plant Physiol, March 2002, Vol. 128, pp. 924-934
The Endoplasmic Reticulum-Associated Maize GL8 Protein Is a
Component of the Acyl-Coenzyme A Elongase Involved in the Production of
Cuticular Waxes1
Xiaojie
Xu,2
Charles R.
Dietrich,3
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.)
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  -ketoacyl reductase
during the elongation of very long-chain fatty acids required for the production of cuticular waxes.
1
This study was supported by the National Science
Foundation (grant nos. IBM-9316832 and IBN-9808559 to P.S.S. and
B.J.N.). C.R.D. was funded in part by a U.S. Department of Agriculture National Needs Fellowship in Plant Biotechnology. This is Journal Paper
no. 19,396 of the Iowa Agricultural and Home Economics Experiment Station (Ames, IA). This is project no. 3,409 and was supported by
Hatch Act and State of Iowa funds.
2
Present address: University of Wisconsin-Madison,
Madison, WI 53706.
3
Present address: Donald Danforth Plant Science Center,
St. Louis, MO 63132.
*
Corresponding author; e-mail schnable{at}iastate.edu; fax
515-294-2299.
© 2002 American Society of Plant Physiologists
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