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Expression of an active spinach acyl carrier protein-I/protein-A gene fusion
Authors:Phillip D Beremand  Donita Doyle Elmore  Katarzyna Dziewanowska  Daniel J Guerra
Institution:(1) Plant Biochemistry Unit, Agricultural Research Service, U.S. Department of Agriculture, Northern Regional Research Center, 1815 N. University St., 61604 Peoria, IL, USA;(2) Seed Biosynthesis Research Unit, Agricultural Research Service, U.S. Department of Agriculture, Northern Regional Research Center, 1815 N. University St., 61604 Peoria, IL, USA;(3) Department of Biochemistry, University of Warsaw, Warsaw, Poland;(4) Institute of Biological Chemistry, Washington State University, 99164-6340 Pullman, WA, USA
Abstract:A synthetic gene encoding spinach acyl carrier protein I (ACP-I) was fused to a gene encoding the Fc-binding portion of staphylococcal protein A. This gene fusion, under the control of the lambdaPR promoter, was expressed at high levels in Escherichia coli producing a 42 kDa fusion protein. This fusion protein was phosphopantethenylated in E. coli. In vitro the ACP portion of the fusion protein was able to participate in acyl ACP synthetase reactions, plant malonyl-CoA:ACP transacylase (MCT) reactions, and plant fatty acid synthetase (FAS) reactions. Inhibitory effects of high ACP concentrations on in vitro plant FAS were observed with the unfused ACP-1 but not with the fusion protein. As with unfused ACP-I, the fusion protein was a poor substrate for E. coli FAS reactions. When injected into rabbits, the fusion protein was also able to generate antiserum to spinach ACP-I.
Keywords:acyl carrier protein  fatty acid synthesis  gene expression  gene fusion  protein A  spinach
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