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J Biol Chem, Vol. 273, Issue 6, 3278-3284, February 6, 1998
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From the Diacylglycerol pyrophosphate (DGPP) is involved
in a putative novel lipid signaling pathway. DGPP phosphatase (DGPP
phosphohydrolase) is a membrane-associated 34-kDa enzyme from
Saccharomyces cerevisiae which catalyzes the
dephosphorylation of DGPP to yield phosphatidate (PA)
and then catalyzes the dephosphorylation of PA to yield diacylglycerol. Amino acid sequence information derived from DGPP phosphatase was used
to identify and isolate the DPP1
(diacylglycerol pyrophosphate phosphatase) gene encoding the enzyme. Multicopy plasmids
containing the DPP1 gene directed a 10-fold overexpression
of DGPP phosphatase activity in S. cerevisiae. The
heterologous expression of the S. cerevisiae DPP1 gene in
Sf-9 insect cells resulted in a 500-fold overexpression of DGPP
phosphatase activity over that expressed in wild-type S. cerevisiae. DGPP phosphatase possesses a
Mg2+-independent PA phosphatase activity, and its
expression correlated with the overexpression of DGPP phosphatase
activity in S. cerevisiae and in insect cells. DGPP
phosphatase was predicted to be an integral membrane protein with six
transmembrane-spanning domains. The enzyme contains a novel phosphatase
sequence motif found in a superfamily of phosphatases. A
dpp1 Department of Food Science, Cook College,
New Jersey Agricultural Experiment Station, Rutgers University, New
Brunswick, New Jersey 08903, § Lord and Taylor Laboratory
for Lung Biochemistry and the Anna Perahia Adatto Clinical Research
Center, National Jewish Center for Immunology and Respiratory Medicine,
Denver, Colorado 80206, and the ¶ Department of Food Science and
Nutrition, University of Rhode Island,
West Kingston, Rhode Island 02892
mutant was constructed by deletion of the
chromosomal copy of the DPP1 gene. The dpp1
mutant was viable and did not exhibit any obvious growth defects. The mutant was devoid of DGPP phosphatase activity and accumulated (4-fold)
DGPP. Analysis of the mutant showed that the DPP1 gene was
not responsible for all of the Mg2+-independent PA
phosphatase activity in S. cerevisiae.
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