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J Biol Chem, Vol. 273, Issue 44, 28590-28596, October 30, 1998
,
From the A recently cloned cDNA from sunflower codes
for a fusion protein composed of an N-terminal cytochrome
b5 and a domain similar to membrane-bound acyl
lipid desaturases. For a functional identification, homologous
cDNAs from Brassica napus and Arabidopsis
thaliana were expressed in Saccharomyces cerevisiae,
and sphingolipid long chain bases were analyzed. The expression of the
heterologous enzyme results in significant proportions of new
Institut für Allgemeine Botanik,
Universität Hamburg, Ohnhorststraße 18, D-22609 Hamburg, Germany
and § Laborgruppe Immunchemie, Forschungszentrum Borstel,
Parkallee 22, D-23845 Borstel, Germany
8,9-cis/trans-phytosphingenines
that accompany the residual C18-phytosphinganine predominating in wild-type yeast cells. These results represent the
first identification of a gene coding for a sphingolipid desaturase and
for a stereounselective desaturase showing
trans-activity from any organism. Furthermore, this fusion
protein is a new member of the cytochrome b5
superfamily. The formation of the two regioisomeric phytosphingenines in the transformed yeast sheds new light on the
factors controlling regioselectivity.
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