Characterization of a non-specific lipid transfer protein associated with the peroxisomal membrane of the yeast, Saccharomyces cerevisiae.

A lipid transfer protein with a broad substrate specificity is associated with the peroxisomal membrane of the yeast Saccharomyces cerevisiae. The protein catalyzes in vitro the transfer of various phospholipids, phosphatidylinositol and phosphatidylserine being translocated at the highest rates. The transfer protein can be released from peroxisomal membranes by treatment with 0.25 M KCl and highly enriched using conventional chromatographic techniques. It is inactivated by heat, detergents, divalent cations and proteinases. During various steps of purification this lipid transfer protein co-fractionated with peroxisomal acyl-CoA oxidase (Pox1p). In a pox1 disruptant peroxisomal lipid transfer activity was still present, although at a reduced level. The peroxisomal lipid transfer protein from the pox1 mutant exhibited different chromatographic properties as compared to the wild-type strain suggesting that acyl-CoA oxidase and the peroxisomal lipid transfer protein may from a complex.