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Journal of Experimental Botany, Vol. 52, No. 360, pp. 1581-1585, July 1, 2001
© 2001 Oxford University Press

Short Communications

Mutagenesis and heterologous expression in yeast of a plant {Delta}6-fatty acid desaturase

Olga Sayanova1, Frédéric Beaudoin1, Balázs Libisch1,2, Aude Castel1,3, Peter R. Shewry1 and Johnathan A. Napier1,4

1 IACR-Long Ashton Research Station, Department of Agricultural Sciences, University of Bristol, Long Ashton, Bristol BS41 9AF, UK
2 Department of Plant Anatomy, Eötvös Loránd University, Budapest, Hungary
3 University Paris Sud, CNRS, F-91405 Orsay, France

Abstract

Membrane-bound microsomal fatty acid desaturases are known to have three conserved histidine boxes, comprising a total of up to eight histidine residues. Recently, a number of deviations from this consensus have been reported, with the substitution of a glutamine for the first histidine residue of the third histidine box being present in the so called ‘front end’ desaturases. These enzymes are also characterized by the presence of a cytochrome b5 domain at the protein N-terminus. Site-directed mutagenesis has been used to probe the functional importance of a number of amino acid residues which comprise the third histidine box of a ‘front end’ desaturase, the borage {Delta}6-fatty acid desaturase. This showed that the variant glutamine in the third histidine box is essential for enzyme activity and that histidine is not able to substitute for this residue.

Key words: Microsomal fatty acid desaturase, ‘front end’ desaturation, borage.


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