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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TypeArticle
Journal titlePlant Science
ISSN0168-9452
1873-2259
Volume173
Issue1
Pages4349
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.
Publication date
PublisherElsevier
LanguageEnglish
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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