The Saccharomyces cerevisiae CDC25 Gene Product Binds Specifically to Catalytically Inactive Ras Proteins In Vivo

REFERENCES

• Becker, D. M., and L. Guarente. 1991. High-efficiency transformation of yeast by electroporation. Methods Enzymol. 194:182–187.
   PubMed Web of Science ®Google Scholar
• Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature (London) 349:117–127.
   PubMed Web of Science ®Google Scholar
• Broach, J. R., and R. J. Deschenes. 1990. The function of RAS genes in Saccharomyces cerevisiae. Adv. Cancer Res. 54:79–139.
   PubMedGoogle Scholar
• Broek, D., T. Toda, T. Michaeli, L. Levin, C. Birchmeier, M. Zoller, S. Powers, and M. Wigler. 1987. The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase pathway. Cell 48:789–799.
   PubMed Web of Science ®Google Scholar
• Brünger, A. T., M. V. Milburn, L. Tong, A. M. deVos, J. Jancarik, Z. Yamaizumi, S. Nishimura, E. Ohtsuka, and S.-H. Kim. 1990. Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain. Proc. Natl. Acad. Sci. USA 87:4849–4853.
   PubMed Web of Science ®Google Scholar
• Butt, T. R., E. J. Sternberg, J. A. Gorman, P. Clark, D. Hamer, M. Rosenberg, and S. T. Crooke. 1984. Copper metallothionein of yeast, structure of the gene, and regulation of expression. Proc. Natl. Acad. Sci. USA 81:3332–3336.
   PubMed Web of Science ®Google Scholar
• Buttler, G., and D. J. Thiele. 1991. ACE2, an activator of yeast metallothionein expression which is homologous to SW15. Mol. Cell. Biol. 11:476–485.
   PubMedGoogle Scholar
• Camonis, J. H., and M. Jacquet. 1988. A new RAS mutation that suppresses the CDC25 gene requirement for growth of Saccharomyces cerevisiae. Mol. Cell. Biol. 8:2980–2983.
   PubMedGoogle Scholar
• Cannon, J. F., and K. Tatchell. 1987. Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase. Mol. Cell. Biol. 7:2653–2663.
   PubMedGoogle Scholar
• Casey, G. P., W. Xiao, and G. H. Rank. 1988. A convenient dominant selection marker for gene transfer in industrial strains of Saccharomyces yeast: SMRI encoded resistance to the herbicide sulfometuron methyl. J. Inst. Brew. 94:93–97.
   Web of Science ®Google Scholar
• Cizewski-Culotta, V., T. Hsu, S. Hu, P. Furst, and D. Hamer. 1989. Copper and the ACE1 regulatory protein reversibly induce yeast metallothionein gene transcription in a mouse extract. Proc. Natl. Acad. Sci. USA 86:8377–8381.
   PubMedGoogle Scholar
• Crëchet, J.-B., P. Poullet, J. Camonis, M. Jacquet, and A. Parmeggiani. 1990. Different kinetic properties of the two mutants, RAS2Ile152 and RAS2Val19, that suppress the CDC25 requirement in RAS/adenylate cyclase pathway in Saccharomyces cerevisiae. J. Biol. Chem. 265:1563–1568.
   PubMedGoogle Scholar
• Crechet, J.-B., P. Poullet, M.-Y. Mistou, A. Parmeggiani, J. Camonis, E. Boy-Marcotte, F. Damak, and M. Jacquet. 1990. Enhancement of the GDP-GTP exchange of RAS proteins by the carboxy-terminal domain of SCD25. Science 248:866–868.
   PubMed Web of Science ®Google Scholar
• Damak, F., E. Boy-Marcotte, D. Le-Roscouet, R. Guilbaud, and M. Jacquet. 1991. SDC25, a CDC25-like gene which contains a RAS-activating domain and is a dispensable gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11:202–212.
   PubMedGoogle Scholar
• DeFeo-Jones, D., K. Tatchell, L. C. Robinson, I. Sigal, W. C. Vass, D. R. Lowy, and Ε. Μ. Scolnick. 1985. Mammalian and yeast ras gene products: biological function in their heterologous system. Science 228:179–184.
   PubMed Web of Science ®Google Scholar
• Engelberg, D., G. Simchen, and A. Levitzki. 1990. In vitro reconstitution of CDC25 regulated S. cerevisiae adenylyl cyclase and its kinetic properties. EMBO J. 9:641–651.
   PubMedGoogle Scholar
• Fedor-Chaiken, M., R. J. Deschenes, and J. R. Broach. 1990. SRV2, a gene required for RAS activation of adenylate cyclase in yeast. Cell 61:329–340.
   PubMed Web of Science ®Google Scholar
• Feig, L. Α., and G. M. Cooper. 1988. Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol. Cell. Biol. 8:3235–3243.
   PubMed Web of Science ®Google Scholar
• Feig, L. Α., B.-T. Pan, T. M. Roberis, and G. M. Cooper. 1986. Isolation of ras GTP-binding mutants using an in situ colony-binding assay. Proc. Natl. Acad. Sci. USA 83:4607–4611.
   PubMedGoogle Scholar
• Field, J., A. Vojtek, R. Ballester, G. Bolger, J. Colicelli, K. Ferguson, J. Gerst, T. Kataoka, T. Michaeli, S. Powers, M. Riggs, L. Rodgers, I. Wieland, B. Wheland, and M. Wigler. 1990. Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein. Cell 61:319–327.
   PubMed Web of Science ®Google Scholar
• Field, J., H.-P. Xu, T. Michaeli, R. Ballester, P. Sass, M. Wigler, and J. Colicelli. 1990. Mutations of the adenylate cyclase gene that block RAS function in Saccharomyces cerevisiae. Science 247:464–467.
   PubMedGoogle Scholar
• Fields, S., and O.-K. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature (London) 340:245–246.
   PubMed Web of Science ®Google Scholar
• Fogel, S., and J. W. Welch. 1982. Tandem gene amplification mediates copper resistance in yeast. Proc. Natl. Acad. Sci. USA 79:5342–5346.
   PubMed Web of Science ®Google Scholar
• Fürst, P., S. Hu, R. Hackett, and D. Hamer. 1988. Copper activates metallothionein gene transcription by altering the conformation of a specific DNA binding protein. Cell 55:705–717.
   PubMed Web of Science ®Google Scholar
• Gerst, J. E., K. Ferguson, A. Vojtek, M. Wigler, and J. Field. 1991. CAP is a bifunctional component of the Saccharomyces cerevisiae adenylyl cyclase complex. Mol. Cell. Biol. 11:1248–1257.
   PubMed Web of Science ®Google Scholar
• Gibbs, J. B., and M. S. Marshall. 1989. The ras oncogene—an important regulatory element in lower eucaryotic organisms. Microbiol. Rev. 53:171–185.
   PubMedGoogle Scholar
• Gibbs, J. B., M. D. Schaber, M. S. Marshall, Ε. Μ. Scolnick, and I. S. Sigal. 1987. Identification of guanine nucleotides bound to ras-encoded proteins in growing yeast cells. J. Biol. Chem. 262:10426–10429.
   PubMedGoogle Scholar
• Goody, R. S., M. Frech, and A. Wittinghofer. 1991. Affinity of guanine nucleotide binding proteins for their ligands: facts and artefacts. Trends Biochem. Sci. 16:327–328. (Letter.)
   PubMedGoogle Scholar
• Hamer, D. 1986. Metallothionein. Annu. Rev. Biochem. 55:913–951.
   PubMed Web of Science ®Google Scholar
• Herskowitz, I. 1987. Functional inactivation of genes by dominant negative mutations. Nature (London) 329:219–222.
   PubMed Web of Science ®Google Scholar
• Johnsson, N., G. Marriott, and K. Weber. 1988. p36, the major cytoplasmic substrate of sre tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO J. 7:2435–2442.
   PubMedGoogle Scholar
• Jones, S., M.-L. Vignais, and J. R. Broach. 1991. The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine nucleotides bound to Ras. Mol. Cell. Biol. 11:2641–2646.
   PubMed Web of Science ®Google Scholar
• Kataoka, T., S. Powers, S. Cameron, O. Fasano, M. Goldfarb, J. Broach, and M. Wigler. 1985. Functional homology of mammalian and yeast RAS protein. Cell 40:19–26.
   PubMed Web of Science ®Google Scholar
• Krengel, U., I. Schlichting, A. Scherer, R. Schumann, M. Frech, J. John, W. Kabsch, E. F. Pai, and A. Wittinghofer. 1990. Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules. Cell 62:539–548.
   PubMed Web of Science ®Google Scholar
• Kunisawa, R., T. N. Davis, M. S. Urdea, and J. Thorner. 1987. Complete nucleotide sequence of the gene encoding the regulatory subunit of 3′,5′-cyclic AMP-dependent protein kinase from the yeast Saccharomyces cerevisiae. Nucleic Acids Res. 15:368–369.
   PubMedGoogle Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Marshall, M. S., J. B. Gibbs, E. M. Scolnick, and I. S. Sigal. 1987. Regulatory function of the Saccharomyces cerevisiae RAS C terminus. Mol. Cell. Biol. 7:2309–2315.
   PubMedGoogle Scholar
• Meyhack, B., A. Hinnen, and J. Heim. 1989. Heterologous gene expression in Saccharomyces cerevisiae, p. 311–321. In C. L. Hershberger, S. W. Queener, and G. Hegeman (ed.), Genetics and molecular biology of industrial microorganisms. American Society for Microbiology, Washington, D.C.
   Google Scholar
• Michaeli, T., J. Field, R. Ballester, K. O’Neill, and M. Wigler. 1989. Mutants of H-ras that interfere with RAS effector function in Saccharomyces cerevisiae. EMBO J. 8:3039–3044.
   PubMedGoogle Scholar
• Milburn, M. V., L. Tong, A. M. deVos, A. Brünger, Z. Yamaizumi, S. Nishimura, and S.-H. Kim. 1990. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247:939–945.
   PubMed Web of Science ®Google Scholar
• Mitts, M. R., J. Bradshaw-Rouse, and W. Heideman. 1991. Interactions between adenylate cyclase and the yeast GTPase-activating protein IRAL Mol. Cell. Biol. 11:4591–4598.
   Google Scholar
• Munder, T., and H. Kuntzel. 1989. Glucose-induced cAMP signaling in Saccharomyces cerevisiae is mediated by the CDC25 protein. FEBS Lett. 242:341–345.
   PubMedGoogle Scholar
• Munder, Τ., Μ. Mink, and H. Küntzel. 1988. Domains of the Saccharomyces cerevisiae CDC25 gene controlling mitosis and meiosis. Mol. Gen. Genet. 214:271–277.
   PubMedGoogle Scholar
• Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351–2359.
   PubMed Web of Science ®Google Scholar
• Powers, S., K. O’Neill, and M. Wigler. 1989. Dominant yeast and mammalian RAS mutants that interfere with the CDC25-dependent activation of wild-type RAS in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:390–395.
   PubMed Web of Science ®Google Scholar
• Pringle, J. R., and L. H. Hartwell. 1981. The Saccharomyces cerevisiae cell cycle, p. 97–142. In J. N. Strathern, E. W. Jones, and J. R. Broach (ed.), The molecular biology of the yeast Saccharomyces: life cycle and inheritance. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Robinson, L. C., J. B. Gibbs, M. S. Marshall, I. S. Sigal, and K. Tatchell. 1987. CDC25: a component of the RAS-adenylate cyclase pathway in Saccharomyces cerevisiae. Science 235:1218–1221.
   PubMed Web of Science ®Google Scholar
• Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–211.
   PubMed Web of Science ®Google Scholar
• Rymond, B. C., R. S. Zitomer, D. Schiimperli, and M. Rosenberg. 1983. The expression in yeast of the Escherichia coli gal Κ gene on CYC1.gal Κ fusion plasmids. Gene 25:249–262.
   PubMedGoogle Scholar
• Sanger, F., S. Nicklen, and A. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Sigal, I. S., J. B. Gibbs, J. S. D’Alonzo, G. L. Temeles, B. S. Wolanski, S. H. Socher, and Ε. Μ. Scolnick. 1986. Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects. Proc. Natl. Acad. Sci. USA 83:952–956.
   PubMed Web of Science ®Google Scholar
• Stacey, D. W., L. A. Feig, and J. B. Gibbs. 1991. Dominant inhibitory Ras mutants selectively inhibit the activity of either cellular or oncogenic Ras. Mol. Cell. Biol. 11:4053–4064.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., B. K. Lin, D. R. Wood, and F. Tamanoi. 1991. IRA2, an upstream negative regulator of RAS in yeast, is a RAS GTPase-activating protein. Proc. Natl. Acad. Sci. USA 88:468–472.
   PubMedGoogle Scholar
• Tanaka, Κ., Κ. Matsumoto, and A. Toh-e. 1989. IRA1, an inhibitory regulator of the RAS-cyclic AMP pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 9:757–768.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., M. Nakafuku, T. Satoh, M. S. Marshall, J. B. Gibbs, K. Matsumoto, Y. Kaziro, and A. Toh-e. 1990. S. cerevisiae genes IRA1 and IRA2 encode proteins that may be functionally equivalent to mammalian ras GTPase activating protein. Cell 60:803–807.
   PubMed Web of Science ®Google Scholar
• Tanaka, K., M. Nakafuku, F. Tamanoi, Y. Kaziro, K. Matsumoto, and A. Toh-e. 1990. IRA2, a second gene of Saccharomyces cerevisiae that encodes a protein with a domain homologous to mammalian ras GTPase-activating protein. Mol. Cell. Biol. 10:4303–4313.
   PubMed Web of Science ®Google Scholar
• Taylor, S. S., J. A. Buechler, and W. Yonemoto. 1990. cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59:971–1005.
   PubMedGoogle Scholar
• Thevelein, J. M. 1991. Fermentable sugars and intracellular acidification as specific activators of the RAS-adenylate cyclase signalling pathway in yeast: the relationship to nutrient-induced cell cycle control. Mol. Microbiol. 5:1301–1307.
   PubMedGoogle Scholar
• Thiele, D. J. 1988. ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene. Mol. Cell. Biol. 8:2745–2752.
   PubMed Web of Science ®Google Scholar
• Toda, T., S. Cameron, P. Sass, M. Zoller, J. D. Scott, B. McMullen, M. Hurwitz, E. G. Krebs, and M. Wigler. 1987. Cloning and characterization of BCY1, a locus encoding a regulatory subunit of the cyclic AMP-dependent protein kinase in Saccharomyces cerevisiae. Mol. Cell. Biol. 7:1371–1377.
   PubMed Web of Science ®Google Scholar
• Welch, J., S. Fogel, C. Buchman, and M. Karin. 1989. The CUP2 gene product regulates the expression of the CUP1 gene, coding for yeast metallothionein. EMBO J. 8:255–260.
   PubMed Web of Science ®Google Scholar
• Wigler, M., J. Field, S. Powers, D. Broek, T. Toda, S. Cameron, J. Nikawa, T. Michaeli, J. Colicelli, and K. Ferguson. 1988. Studies of RAS function in the yeast Saccharomyces cerevisiae. Cold Spring Harbor Symp. Quant. Biol. 53:649–655.
   PubMedGoogle Scholar
• Yang, W., W. Gahl, and D. Hamer. 1991. Role of heat shock transcription factor in yeast metallothionein gene expression. Mol. Cell. Biol. 11:3676–3681.
   PubMed Web of Science ®Google Scholar