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A desaturase-like protein from white spruce is a Delta(9) desaturase
Elizabeth-France Marillia1, E Michael Giblin, Patrick S Covello
1National Research Council of Canada, Plant Biotechnology Institute, Seed Oil Biotechnology Group, 110 Gymnasium Place, Saskatoon, SK, Canada S7N 0W9.
Abstract:
Gymnospermae seed lipids are characterized by a high degree of desaturation, most having a Delta(9) double bond. By degenerate polymerase chain reaction (PCR) we have isolated a white spruce (Picea glauca) cDNA clone that encodes an amino acid sequence sharing a high degree of homology with other putative plant acyl-coenzyme A (CoA) Des9 desaturases. Both in vivo and in vitro expression studies in a Delta(9) desaturase-deficient yeast strain demonstrated the desaturation functionality of the white spruce clone, and gas chromatography-mass spectrometry (GC-MS) analyses confirmed the regioselectivity of the encoded enzyme. This is the first report of the functional characterization of a plant membrane-bound acyl-CoA-like protein Delta(9) desaturase by heterologous expression in yeast.