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J. Biol. Chem., Vol. 278, Issue 34, 31495-31503, August 22, 2003

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Regulation of the Yeast DPP1-encoded Diacylglycerol Pyrophosphate Phosphatase by Transcription Factor Gis1p^*

June Oshiro  , Gil-Soo Han , Wendy M. Iwanyshyn , Kristi Conover  and George M. Carman   ¶

From the Graduate Program in Microbiology and Molecular Genetics and the Department of Food Science, Rutgers University, New Brunswick, New Jersey 08901

The Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase catalyzes the dephosphorylation of diacylglycerol pyrophosphate to form phosphatidate and P_i. The enzyme also dephosphorylates phosphatidate to form diacylglycerol and P_i. Because diacylglycerol pyrophosphate, phosphatidate, and diacylglycerol have roles as lipid signal molecules in higher eukaryotic cells, it is important to understand how diacylglycerol pyrophosphate phosphatase is regulated. Analysis of DPP1 expression using P_DPP1-lacZ reporter genes with a series of deletions from the 5' end of the promoter indicated sequences responsible for enzyme expression. Three binding sites (URS_PDS) for transcription factor Gis1p were identified in the DPP1 promoter (consensus sequence of 5'-T(A/T)AGGGAT-3'). A gis1 mutant exhibited elevated levels of DPP1 expression and diacylglycerol pyrophosphate phosphatase activity. Direct interaction between Gis1p and DPP1 promoter elements was demonstrated by electrophoretic mobility shift assays. Mutations in the three URS_PDS elements within the DPP1 promoter abolished Gis1p-DNA interactions in vitro and abolished the regulation of DPP1 in vivo. These data indicated that Gis1p was a repressor of DPP1 expression. Phospholipid composition analysis of the gis1 mutant showed that Gis1p played a role in regulating the cellular level of diacylglycerol pyrophosphate, as well as the levels of the major phospholipids phosphatidylethanolamine and phosphatidylcholine.

Received for publication, May 23, 2003

^* This work was supported in part by United States Public Health Service Grant GM-28140 from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Dept. of Food Science, Rutgers University, 65 Dudley Rd., New Brunswick, NJ 08901. Tel.: 732-932-9611 (ext. 217); Fax: 732-932-6776; E-mail: carman{at}aesop.rutgers.edu.

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