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Mutations in a protein tyrosine phosphatase gene (PTP2) and a protein serine/threonine phosphatase gene (PTC1) cause a synthetic growth defect in Saccharomyces cerevisiae.

Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, Massachusetts.

ABSTRACT

Two protein tyrosine phosphatase genes, PTP1 and PTP2, are known in Saccharomyces cerevisiae. However, the functions of these tyrosine phosphatases are unknown, because mutations in either or both phosphatase genes have no clear phenotypic effects. In this report, we demonstrate that although ptp2 has no obvious phenotype by itself, it has a profound effect on cell growth when combined with mutations in a novel protein phosphatase gene. Using a colony color sectoring assay, we isolated 25 mutants in which the expression of PTP1 or PTP2 is required for growth. Complementation tests of the mutants showed that they have a mutation in one of three genes. Cloning and sequence determination of one of these gene, PTC1, indicated that it encodes a homolog of the mammalian protein serine/threonine phosphatase 2C (PP2C). The amino acid sequence of the PTC1 product is approximately 35% identical to PP2C. Disruption of PTC1 indicated that the PTC1 function is nonessential. In contrast, ptc1 ptp2 double mutants showed a marked growth defect. To examine whether PTC1 encodes an active protein phosphatase, a glutathione S-transferase (GST)-PTC1 fusion gene was constructed and expressed in Escherichia coli. Purified GST-PTC1 fusion protein hydrolyzed a serine phosphorylated substrate in the presence of the divalent cation Mg2+ or Mn2+. GST-PTC1 also had weak (approximately 0.5% of its serine phosphatase activity) protein tyrosine phosphatase activity.

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• Contamine, V., Picard, M. (2000). Maintenance and Integrity of the Mitochondrial Genome: a Plethora of Nuclear Genes in the Budding Yeast. Microbiol. Mol. Biol. Rev. 64: 281-315 [Abstract] [Full Text]  
• Mattison, C. P., Ota, I. M. (2000). Two protein tyrosine phosphatases, Ptp2 and Ptp3, modulate the subcellular localization of the Hog1 MAP kinase in yeast. Genes Dev. 14: 1229-1235 [Abstract] [Full Text]  
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• Cheng, A., Ross, K. E., Kaldis, P., Solomon, M. J. (1999). Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases. Genes Dev. 13: 2946-2957 [Abstract] [Full Text]  
• Zhan, X.-L., Guan, K.-L. (1999). A specific protein-protein interaction accounts for the in vivo substrate selectivity of Ptp3 towards the Fus3 MAP kinase. Genes Dev. 13: 2811-2827 [Abstract] [Full Text]  
• Gaits, F., Russell, P. (1999). Vacuole Fusion Regulated by Protein Phosphatase 2C in Fission Yeast. Mol. Biol. Cell 10: 2647-2654 [Abstract] [Full Text]  
• Kaufman, R. J. (1999). Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13: 1211-1233 [Full Text]  
• Reiser, V., Ruis, H., Ammerer, G. (1999). Kinase Activity-dependent Nuclear Export Opposes Stress-induced Nuclear Accumulation and Retention of Hog1 Mitogen-activated Protein Kinase in the Budding Yeast Saccharomyces cerevisiae. Mol. Biol. Cell 10: 1147-1161 [Abstract] [Full Text]  
• Kapranov, P., Jensen, T. J., Poulsen, C., de Bruijn, F. J., Szczyglowski, K. (1999). A protein phosphatase 2C gene, LjNPP2C1, from Lotus japonicus induced during root nodule development. Proc. Natl. Acad. Sci. USA 96: 1738-1743 [Abstract] [Full Text]  
• Gustin, M. C., Albertyn, J., Alexander, M., Davenport, K. (1998). MAP Kinase Pathways in the Yeast Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 62: 1264-1300 [Abstract] [Full Text]  
• Hansen, D., Pilgrim, D. (1998). Molecular Evolution of a Sex Determination Protein: FEM-2 (PP2C) in Caenorhabditis. Genetics 149: 1353-1362 [Abstract] [Full Text]  
• Mamoun, C. B., Sullivan Jr., D. J., Banerjee, R., Goldberg, D. E. (1998). Identification and Characterization of an Unusual Double Serine/Threonine Protein Phosphatase 2C in the Malaria Parasite Plasmodium falciparum. J. Biol. Chem. 273: 11241-11247 [Abstract] [Full Text]  
• Welihinda, A. A., Tirasophon, W., Green, S. R., Kaufman, R. J. (1998). Protein Serine/Threonine Phosphatase Ptc2p Negatively Regulates the Unfolded-Protein Response by Dephosphorylating Ire1p Kinase. Mol. Cell. Biol. 18: 1967-1977 [Abstract] [Full Text]  
• Roeder, A. D., Hermann, G. J., Keegan, B. R., Thatcher, S. A., Shaw, J. M. (1998). Mitochondrial Inheritance Is Delayed in Saccharomyces cerevisiae Cells Lacking the Serine/Threonine Phosphatase PTC1. Mol. Biol. Cell 9: 917-930 [Abstract] [Full Text]  
• Meskiene, I., Bogre, L., Glaser, W., Balog, J., Brandstotter, M., Zwerger, K., Ammerer, G., Hirt, H. (1998). MP2C, a plant protein phosphatase 2C, functions as a negative regulator of mitogen-activated protein kinase pathways in yeast and plants. Proc. Natl. Acad. Sci. USA 95: 1938-1943 [Abstract] [Full Text]  
• Sheen, J. (1998). Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants. Proc. Natl. Acad. Sci. USA 95: 975-980 [Abstract] [Full Text]  
• Jacoby, T., Flanagan, H., Faykin, A., Seto, A. G., Mattison, C., Ota, I. (1997). Two Protein-tyrosine Phosphatases Inactivate the Osmotic Stress Response Pathway in Yeast by Targeting the Mitogen-activated Protein Kinase, Hog1. J. Biol. Chem. 272: 17749-17755 [Abstract] [Full Text]  
• Gaits, F., Shiozaki, K., Russell, P. (1997). Protein Phosphatase 2C Acts Independently of Stress-activated Kinase Cascade to Regulate the Stress Response in Fission Yeast. J. Biol. Chem. 272: 17873-17879 [Abstract] [Full Text]  
• Ernsting, B. R., Dixon, J. E. (1997). The PPS1 Gene of Saccharomyces cerevisiae Codes for a Dual Specificity Protein Phosphatase with a Role in the DNA Synthesis Phase of the Cell Cycle. J. Biol. Chem. 272: 9332-9343 [Abstract] [Full Text]  
• Chin-Sang, I D, Spence, A M (1996). Caenorhabditis elegans sex-determining protein FEM-2 is a protein phosphatase that promotes male development and interacts directly with FEM-3.. Genes Dev. 10: 2314-2325 [Abstract]  
• Wang, Y., Santini, F., Qin, K., Huang, C. Y. (1995). A Mg[IMAGE]-dependent, Ca[IMAGE]-inhibitable Serine/Threonine Protein Phosphatase from Bovine Brain. J. Biol. Chem. 270: 25607-25612 [Abstract] [Full Text]  
• Wilson, L. K., Benton, B. M., Zhou, S., Thorner, J., Martin, G. S. (1995). The Yeast Immunophilin Fpr3 Is a Physiological Substrate of the Tyrosine-specific Phosphoprotein Phosphatase Ptp1. J. Biol. Chem. 270: 25185-25193 [Abstract] [Full Text]  
• Ostanin, K., Pokalsky, C., Wang, S., Van Etten, R. L. (1995). Cloning and Characterization of a Saccharomyces cerevisiae Gene Encoding the Low Molecular Weight Protein-tyrosine Phosphatase. J. Biol. Chem. 270: 18491-18499 [Abstract] [Full Text]  
• Stone, J., Collinge, M., Smith, R., Horn, M., Walker, J. (1994). Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science 266: 793-795 [Abstract]  
• Leung, J, Bouvier-Durand, M, Morris, P., Guerrier, D, Chefdor, F, Giraudat, J (1994). Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science 264: 1448-1452 [Abstract]