title: The Endoplasmic reticulum-associated maize GL8 protein is a component of the acyl-coenzyme A elongase involved in the production of cuticular waxes.
abstract: 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 beta-ketoacyl reductase during the elongation of very long-chain fatty acids required for the production of cuticular waxes.
authors.affiliation: Laboratoire de Biogenese Membranaire, Centre National de la Recherche Scientifique UMR 5544, Universite V. Segalen, Bordeaux 2, 146, 33076 Bordeaux cedex.
authors.forename: Xiaojie
authors.initials: X
authors.lastname: Xu
authors.forename: Charles R
authors.initials: CR
authors.lastname: Dietrich
authors.forename: Rene
authors.initials: R
authors.lastname: Lessire
authors.forename: Basil J
authors.initials: BJ
authors.lastname: Nikolau
authors.forename: Patrick S
authors.initials: PS
authors.lastname: Schnable
mesh_terms: D015094:3-Hydroxyacyl CoA Dehydrogenases / Q000378:metabolism; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000378:metabolism; D051080:Acyl-Carrier Protein S-Malonyltransferase; D044942:Acyl-CoA Dehydrogenase, Long-Chain / Q000378:metabolism; D000217:Acyltransferases / Q000378:metabolism; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D054889:Fatty Acid Synthase, Type II; D015870:Gene Expression; D015151:Immunoblotting; D009154:Mutation; D018515:Plant Leaves / Q000201:enzymology / Q000378:metabolism; D010940:Plant Proteins; D014885:Waxes / Q000378:metabolism*; D003313:Zea mays / Q000201:enzymology* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D010940:Plant Proteins; D014885:Waxes; D000429:Alcohol Oxidoreductases; C108981:glossy8 protein, Zea mays; D015094:3-Hydroxyacyl CoA Dehydrogenases; C023744:acetoacetyl-CoA reductase; D044942:Acyl-CoA Dehydrogenase, Long-Chain; D000217:Acyltransferases; D051080:Acyl-Carrier Protein S-Malonyltransferase; C494968:fabD protein, E coli; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; D054889:Fatty Acid Synthase, Type II