Abstract
We have isolated fatty acid elongation 1 (FAE1) genomic clones from high erucic acid (HEA) B. napus, B. rapa and B. oleracea, and low erucic acid (LEA) B. napus. Nucleotide sequences corresponding to open reading frames of 1523 bp were translated and proteins of 506 a.a. were deduced. Comparative study of FAE1 protein sequences from HEA and LEA Brassicas revealed the one crucial amino acid difference: the serine residue at position 282 of the HEA FAE1 sequences is substituted by phenylalanine in LEA B. napus. Using site directed mutagenesis the phenylalanine282 residue was substituted with a serine residue in FAE1 polypeptide from LEA B. napus, the mutated gene was expressed in yeast, and GC analysis showed presence of very long chain mono-unsaturated fatty acids indicating that the elongase activity was restored in the LEA FAE1 enzyme. Thus, for the first time, the low erucic acid trait in B. napus has been attributed to a single amino acid substitution which prevents the biosynthesis of very long chain mono-unsaturated fatty acids.
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© 2003 Springer Science+Business Media Dordrecht
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Katavic, V., Mietkiewska, E., Barton, D.L., Giblin, E.M., Reed, D.W., Taylor, D.C. (2003). Substitution of Phe282 with Ser in Lea B. napus c.v. Westar Restores FAE1 Enzyme Activity. In: Murata, N., Yamada, M., Nishida, I., Okuyama, H., Sekiya, J., Hajime, W. (eds) Advanced Research on Plant Lipids. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0159-4_20
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DOI: https://doi.org/10.1007/978-94-017-0159-4_20
Publisher Name: Springer, Dordrecht
Print ISBN: 978-90-481-6210-9
Online ISBN: 978-94-017-0159-4
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