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PLANT PHYSIOLOGY , Vol 105, Issue 2 635-641, Copyright © 1994 by American Society of Plant Biologists

METABOLISM AND ENZYMOLOGY

Cloning of a Higher-Plant Plastid [omega]-6 Fatty Acid Desaturase cDNA and Its Expression in a Cyanobacterium

W. D. Hitz, T. J. Carlson, J. R. Booth Jr, A. J. Kinney, K. L. Stecca and N. S. Yadav
Central Research and Development (W.D.H., T.J.C.) and Agricultural Products (J.R.B., A.J.K., K.L.S., N.S.Y), E.I. duPont de Nemours & Co., Experimental Station, P.O. Box 80402, Wilmington, Delaware 19880-0402

Oligomers based on amino acids conserved between known plant [omega]-3 and cyanobacterium [omega]-6 fatty acid desaturases were used to screen an Arabidopsis cDNA library for related sequences. An identified clone encoding a novel desaturase-like polypeptide was used to isolate its homologs from Glycine max and Brassica napus. The plant deduced amino acid sequences showed less than 27% similarity to known plant [omega]-6 and [omega]-3 desaturases but more than 48% similarity to cyanobacterial [omega]-6 desaturase, and they contained putative plastid transit sequences. Thus, we deduce that the plant cDNAs encode the plastid [omega]-6 desaturase. The identity was supported by expression of the B. napus cDNA cyanobacterium. Synechococcus transformed with a chimeric gene that contains a prokaryotic promoter fused to the rapeseed cDNA encoding all but the first 73 amino acids partially converted its oleic acid fatty acid to linoleic acid, and the 16:1(9c) fatty acid was converted primarily to 16:2(9c,12) in vivo. Thus, the plant [omega]-6 desaturase, which utilizes 16:1(7c) in plants, can utilize 16:1(9c) in the cyanobacterium. The plastid and cytosolic homologs of plant [omega]-6 desaturases are much more distantly related than those of [omega]-3 desaturases.


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