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...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 94; no. 4; pp. 1142 - 1147 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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 Access | Get full text |
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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. |
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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 |