Abstract
A phospholipid transfer protein with a broad substrate specificity was isolated from yeast cytosol. The rate of transfer catalyzed by this protein in vitro is highest for phosphatidylserine; phosphatidylethanolamine, cardiolipin, phosphatidic acid and ergosterol are transported at a lower rate. In contrast to the yeast phosphatidylinositol transfer protein (Daum, G. and Paltauf, F. (1984) Biochim. Biophys. Acta 794, 385–391) the phosphatidylserine transfer protein does not catalyze the translocation of phosphatidylinositol or phosphatidylcholine. Using chromatographic methods the phosphatidylserine transfer protein was enriched approximately 3000-fold over yeast cytosol. The protein is inactivated by heat, detergents and proteinases. Divalent cations strongly inhibit the transfer of phosphatidylserine in vitro, and EDTA at low concentrations has a stimulatory effect.
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