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PLANT PHYSIOLOGY , Vol 109, Issue 3 999-1006, Copyright © 1995 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Cloning of a Coconut Endosperm cDNA Encoding a 1-Acyl-sn-Glycerol-3-Phosphate Acyltransferase That Accepts Medium-Chain-Length Substrates
D. S. Knutzon, K. D. Lardizabal, J. S. Nelsen, J. L. Bleibaum, H. M. Davies and J. G. Metz
Calgene, Inc., 1920 Fifth Street, Davis, California 95616
Immature coconut (Cocos nucifera) endosperm contains a
1-acyl-sn-glycerol-3-phosphate acyltransferase (LPAAT) activity that shows
a preference for medium-chain-length fatty acyl-coenzyme A substrates (H.M.
Davies, D.J. Hawkins, J.S. Nelsen [1995] Phytochemistry 39: 989-996).
Beginning with solubilized membrane preparations, we have used
chromatographic separations to identify a polypeptide with an apparent
molecular mass of 29 kD, whose presence in various column fractions
correlates with the acyltransferase activity detected in those same
fractions. Amino acid sequence data obtained from several peptides
generated from this protein were used to isolate a full-length clone from a
coconut endosperm cDNA library. Clone pCGN5503 contains a 1325-bp cDNA
insert with an open reading frame encoding a 308-amino acid protein with a
calculated molecular mass of 34.8 kD. Comparison of the deduced amino acid
sequence of pCGN5503 to sequences in the data banks revealed significant
homology to other putative LPAAT sequences. Expression of the coconut cDNA
in Escherichia coli conferred upon those cells a novel LPAAT activity whose
substrate activity profile matched that of the coconut enzyme.
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