A FAD2 homologue from Lesquerella lindheimeri has predominantly fatty acid hydroxylase activity

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DOIResolve DOI: http://doi.org/10.1016/j.plantsci.2007.03.015
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Journal titlePlant Science
Subjectlesquerella lindheimeri; fatty acid hydroxylase; ricinoleic acid; hydroxy fatty acid; seed oil content; single seed TLC
AbstractA genomic sequence encoding a polypeptide with 91% sequence identity to the Lesquerella fendleri bifunctional oleate 12-hydroxylase:desaturase was amplified by PCR from Lesquerella lindheimeri. Expression of the gene in the yeast Saccharomyces cerevisiae resulted in the synthesis of ricinoleic acid and very low levels of di-unsaturated fatty acids. Comparison of the amino acid sequences of the L. lindheimeri and castor bean oleate 12-hydroxylase enzymes to those of the L. fendleri bifunctional oleate 12-hydroxylase:desaturase and oleate 12-desaturase enzymes from 32 diverse species identified a single amino acid (M295) that was conserved in the hydroxylases and different but also conserved in the desaturases and the bifunctional enzyme. Site-directed mutagenesis indicated that this residue was most likely not involved in determining the catalytic outcome of the hydroxylation/desaturation reaction. Transformation of an Arabidopsis fad2/fae1 mutant line with the L. lindheimeri hydroxylase gave further evidence that this enzyme, like the castor oleate 12-hydroxylase, is primarily a fatty acid hydroxylase and should not be considered bifunctional. Total hydroxy fatty acid content of up to 18% of seed fatty acids was measured in homozygous transformants. Lines with the highest hydroxy fatty acid content showed significant reduction in total oil content.
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AffiliationNRC Plant Biotechnology Institute; National Research Council Canada
Peer reviewedYes
NPARC number23002566
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Record identifier6c69af17-0d37-475c-8c4f-2d34d1cde352
Record created2017-11-30
Record modified2017-12-04
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