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Originally published In Press as doi:10.1074/jbc.M202045200 on March 26, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19609-19617, May 31, 2002
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Multiple Regulatory Roles of a Novel Saccharomyces cerevisiae Protein, Encoded by YOL002c, in Lipid and Phosphate Metabolism*

Igor V. KarpichevDagger , Lizbeth CornivelliDagger , and Gillian M. Small§

From the Department of Biology, City College of the City University of New York, New York, New York 10031

The yeast open reading frame YOL002c encodes a putative membrane protein. This protein is evolutionarily conserved across species, including humans, although the function of each of these proteins remains unknown. YOL002c is highly expressed in yeast cells that are grown in the presence of saturated fatty acids such as myristate. Furthermore, cells in which the YOL002c gene is disrupted grow poorly on this carbon source. These mutant cells are also resistant to the polyene antibiotic, nystatin. Gene chip analysis on yol002cDelta cells revealed that a variety of genes encoding proteins involved in fatty acid metabolism and in the phosphate signaling pathway are induced in this mutant strain. In addition, our studies demonstrated that in the disruption strain acid phosphatase activity is expressed constitutively, and the cells accumulate polyphosphate to much higher levels than wild-type cells. A homologous human protein is able to partially rescue these defects in phosphate metabolism. We propose that YOL002c encodes a Saccharomyces cerevisiae protein that plays a key role in metabolic pathways that regulate lipid and phosphate metabolism.


* This work was supported by National Institutes of Health Grants RO1DK54976 and RCMI Grant G12 RR03060.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.

Dagger Both authors contributed equally to this work.

§ To whom correspondence should be addressed. Tel.: 212-794-5417; Fax: 212-794-5378; E-mail: gmsbh@cunyvm.cuny.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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