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J Biol Chem, Vol. 273, Issue 44, 28590-28596, October 30, 1998

A Sphingolipid Desaturase from Higher Plants
IDENTIFICATION OF A NEW CYTOCHROME b₅ FUSION PROTEIN

Petra Sperling, Ulrich Zähringer^§, and Ernst Heinz

From the  Institut für Allgemeine Botanik, Universität Hamburg, Ohnhorststraße 18, D-22609 Hamburg, Germany and ^§ Laborgruppe Immunchemie, Forschungszentrum Borstel, Parkallee 22, D-23845 Borstel, Germany

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 ^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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