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J Biol Chem, Vol. 275, Issue 19, 14446-14456, May 12, 2000

A New Gene Involved in the Transport-dependent Metabolism of Phosphatidylserine, PSTB2/PDR17, Shares Sequence Similarity with the Gene Encoding the Phosphatidylinositol/Phosphatidylcholine Transfer Protein, SEC14*

Wen-I WuDagger , Sheri Routt§, Vytas A. Bankaitis§, and Dennis R. VoelkerDagger

From the Dagger  Department of Medicine, Program in Cell Biology, National Jewish Medical and Research Center, Denver Colorado 80206 and the § Department of Cell Biology, University of Alabama, Birmingham Alabama 35294-0005

A new yeast strain, designated pstB2, that is defective in the conversion of nascent phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn) by PtdSer decarboxylase 2, has been isolated. The pstB2 strain requires ethanolamine for growth. Incubation of cells with [3H]serine followed by analysis of the aminoglycerophospholipids demonstrates a 50% increase in the labeling of PtdSer and a 72% decrease in PtdEtn formation in the mutant relative to the parental strain. The PSTB2 gene was isolated by complementation, and it restores ethanolamine prototrophy and corrects the defective lipid metabolism of the pstB2 strain. The PSTB2 gene is allelic to the pleiotropic drug resistance gene, PDR17, and is homologous to SEC14, which encodes a phosphatidylinositol/phosphatidylcholine transfer protein. The protein, PstB2p, displays phosphatidylinositol but not PtdSer transfer activity, and its overexpression causes suppression of sec14 mutants. However, overexpression of the SEC14 gene fails to suppress the conditional lethality of pstB2 strains. The transport-dependent metabolism of PtdSer to PtdEtn occurs in permeabilized wild type yeast but is dramatically reduced in permeabilized pstB2 strains. Fractionation of permeabilized cells demonstrates that the pstB2 strain accumulates nascent PtdSer in the Golgi apparatus and a novel light membrane fraction, consistent with a defect in lipid transport processes that control substrate access to PtdSer decarboxylase 2.

* This work was supported by National Institutes of Health Research Grants GM32453 (to D. R. V.), GM19162 (to W. W.), and GM44530 (to V. A. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 303-398-1300; Fax: 303-398-1806; E-mail: voelkerd@njc.org.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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