Identification of an Animal ω -3 Fatty Acid Desaturase by Heterologous Expression in Arabidopsis

In animals, fatty acid desaturases catalyze key reactions in the synthesis of arachidonic acid and other polyunsaturated fatty acids. A search of the Caenorhabditis elegans DNA databases, using the sequences of Arabidopsis genes, identified several putative desaturases. Here we describe the characte...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 94; no. 4; pp. 1142 - 1147
Main Authors Spychalla, James P., Kinney, Anthony J., Browse, John
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences of the United States of America 18.02.1997
National Acad Sciences
National Academy of Sciences
The National Academy of Sciences of the USA
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:In animals, fatty acid desaturases catalyze key reactions in the synthesis of arachidonic acid and other polyunsaturated fatty acids. A search of the Caenorhabditis elegans DNA databases, using the sequences of Arabidopsis genes, identified several putative desaturases. Here we describe the characterization of the first of these genes, fat-1. The predicted protein encoded by a fat-1 cDNA showed 32-35% identity with both FAD2 and FAD3 of Arabidopsis. When expressed in transgenic plants, fat-1 resulted in a 90% increase in the proportion of α -linolenic acid in root lipids. Wild-type Arabidopsis incorporated ω -6 fatty acids (Δ 8,11,14-20:3 and Δ 5,8,11,14-20:4) into membrane lipids but did not desaturate them. By contrast, fat-1 transgenic plants efficiently desaturated both of these fatty acids to the corresponding ω -3 products. These findings indicate that the C. elegans fat-1 gene encodes the first animal representative of a class of glycerolipid desaturases that have previously been characterized in plants and cyanobacteria. The FAT-1 protein is an ω -3 fatty acyl desaturase that recognizes a range of 18- and 20-carbon ω -6 substrates.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
To whom reprint requests should be addressed.
Christopher Somerville, Carnegie Institution of Washington, Stanford, CA
Present address: Spychalla Farms, Inc., N3974 Highway 52, Antigo, WI 54409.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.4.1142