The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae

Alexander Faulkner, Xiaoming Chen, Jeffrey Rush, Bruce F Horazdovsky, Charles J. Waechter, George M. Carman, Paul C. Sternweis

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Two genes in Saccharomyces cerevisiae, LPP1 and DPP1, with homology to a mammalian phosphatidic acid (PA) phosphatase were identified and disrupted. Neither single nor combined deletions resulted in growth or secretion phenotypes. As observed previously (Toke, D. A., Bennett, W. L., Dillon, D. A., Wu, W.-I., Chen, X., Ostrander, D. B., Oshiro, J., Cremesti, A., Voelker, D. R., Fischl, A. S., and Carman, G. M. (1998) J. Biol. Chem. 273, 3278- 3284; Toke, D. A., Bennett, W. L., Oshiro, J., Wu, W.-I., Voelker, D. R., and Carman, G. M. (1998) J. Biol. Chem. 273, 14331-14338), the disruption of DPP1 and LPP1 produced profound losses of Mg2+-independent PA phosphatase activity. The coincident attenuation of hydrolyric activity against diacylglycerol pyrophosphate prompted an examination of the effects of these disruptions on hydrolysis of isoprenoid pyrophosphates. Disruption of either LPP1 or DPP1 caused respective decreases of about 25 and 75% in Mg2+- independent hydrolysis of several isoprenoid phosphates by particulate fractions isolated from these cells. The particulate and cytosolic fractions from the double disruption (lpp1Δ dpp1Δ) showed essentially complete loss of Mg2+-independent hydrolyric activity toward dolichyl phosphate (dolichyl-P), dolichyl pyrophosphate (dolichyl-P-P), farnesyl pyrophosphate (farnesyl-P-P), and geranylgeranyl pyrophosphate (geranylgeranyl-P-P). However, a modest Mg2+-stimulated activity toward PA and dolichyl-P was retained in cytosol from lpp1Δ dpp1Δ cells. The action of Dpp1p on isoprenyl pyrophosphates was confirmed by characterization of the hydrolysis of geranylgeranyl-P-P by the purified protein. These results indicate that LPP1 and DPP1 account for most of the hydrolytic activities toward dolichyl- P-P, dolichyl-P, farnesyl,P-P, and geranylgeranyl-P-P but also suggest that yeast contain other enzymes capable of dephosphorylating these essential isoprenoid intermediates.

Original languageEnglish (US)
Pages (from-to)14831-14837
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number21
DOIs
StatePublished - May 21 1999
Externally publishedYes

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Polyisoprenyl Phosphates
Phosphatidate Phosphatase
Phosphoric Monoester Hydrolases
Yeast
Saccharomyces cerevisiae
Hydrolysis
Genes
Diphosphates
Terpenes
Phosphatidic Acids
Cytosol
Yeasts
Phenotype
Enzymes
Growth
dolichol monophosphate
geranylgeranyl pyrophosphate
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Faulkner, A., Chen, X., Rush, J., Horazdovsky, B. F., Waechter, C. J., Carman, G. M., & Sternweis, P. C. (1999). The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. Journal of Biological Chemistry, 274(21), 14831-14837. https://doi.org/10.1074/jbc.274.21.14831

The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. / Faulkner, Alexander; Chen, Xiaoming; Rush, Jeffrey; Horazdovsky, Bruce F; Waechter, Charles J.; Carman, George M.; Sternweis, Paul C.

In: Journal of Biological Chemistry, Vol. 274, No. 21, 21.05.1999, p. 14831-14837.

Research output: Contribution to journalArticle

Faulkner, A, Chen, X, Rush, J, Horazdovsky, BF, Waechter, CJ, Carman, GM & Sternweis, PC 1999, 'The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae', Journal of Biological Chemistry, vol. 274, no. 21, pp. 14831-14837. https://doi.org/10.1074/jbc.274.21.14831
Faulkner, Alexander ; Chen, Xiaoming ; Rush, Jeffrey ; Horazdovsky, Bruce F ; Waechter, Charles J. ; Carman, George M. ; Sternweis, Paul C. / The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 21. pp. 14831-14837.
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