Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from saccharomyces cerevisiae

doi:10.1074/jbc.M311779200

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Papers In Press, published online ahead of print November 20, 2003
J. Biol. Chem, 10.1074/jbc.M311779200
Submitted on October 27, 2003
Revised on November 18, 2003
Accepted on November 18, 2003

Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase catalytic site from saccharomyces cerevisiae

Gil-Soo Han, Celeste N. Johnston, and George M. Carman

Department of Food Science, Rutgers University, New Brunswick, NJ 08901-8520

Corresponding Author: carman{at}aesop.rutgers.edu

The Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase is a vacuole membrane-associated enzyme that catalyzes the removal of the b-phosphate from diacylglycerol pyrophosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol. The enzyme has six putative transmembrane domains and a hydrophilic region that contains a phosphatase motif required for its catalytic activity. In this work, we examined the topography of diacylglycerol pyrophosphate phosphatase catalytic site within the transverse plane of the vacuole membrane. Results of protease protection analysis using endoproteinase Lys-C and labeling of cysteine residues using sulfhydryl reagents were consistent with a model where the catalytic site of diacylglycerol pyrophosphate phosphatase was oriented to the cytosolic face of the vacuole membrane. In addition, diacylglycerol pyrophosphate phosphatase activity was found with intact vacuoles. The phospholipids diacylglycerol pyrophosphate (0.6 mol%) and phosphatidate (1.4 mol%) were found in the vacuole membrane, and their levels decreased to an undetectable level and by 79%, respectively, when cells were depleted for zinc. The reduced levels of diacylglycerol pyrophosphate and phosphatidate correlated with the induced expression of diacylglycerol pyrophosphate phosphatase. This work suggested that diacylglycerol pyrophosphate phosphatase functions to regulate the levels of diacylglycerol pyrophosphate and phosphatidate on the cytosolic face of the vacuole membrane.

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				G.-S. Han, S. Siniossoglou, and G. M. Carman The Cellular Functions of the Yeast Lipin Homolog Pah1p Are Dependent on Its Phosphatidate Phosphatase Activity J. Biol. Chem., December 21, 2007; 282(51): 37026 - 37035. [Abstract] [Full Text] [PDF]

				M.-G. Choi and G. M. Carman Phosphorylation of Human CTP Synthetase 1 by Protein Kinase A: IDENTIFICATION OF Thr455 AS A MAJOR SITE OF PHOSPHORYLATION J. Biol. Chem., February 23, 2007; 282(8): 5367 - 5377. [Abstract] [Full Text] [PDF]

				M. C. Kersting and G. M. Carman Regulation of the Saccharomyces cerevisiae EKI1-encoded Ethanolamine Kinase by Zinc Depletion J. Biol. Chem., May 12, 2006; 281(19): 13110 - 13116. [Abstract] [Full Text] [PDF]

				G.-S. Han, W.-I Wu, and G. M. Carman The Saccharomyces cerevisiae Lipin Homolog Is a Mg2+-dependent Phosphatidate Phosphatase Enzyme J. Biol. Chem., April 7, 2006; 281(14): 9210 - 9218. [Abstract] [Full Text] [PDF]

				W. M. Iwanyshyn, G.-S. Han, and G. M. Carman Regulation of Phospholipid Synthesis in Saccharomyces cerevisiae by Zinc J. Biol. Chem., May 21, 2004; 279(21): 21976 - 21983. [Abstract] [Full Text] [PDF]