Yeast α Mating Factor Structure-Activity Relationship Derived from Genetically Selected Peptide Agonists and Antagonists of Ste2p

REFERENCES

• Ammerer, G. 1983. Expression of genes in yeast using the ADCI promoter. Methods Enzymol. 101:192–201.
   PubMed Web of Science ®Google Scholar
• 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
• Blumer, K. J., and J. Thorner. 1990. β and γ subunits of a yeast guanine nucleotide-binding protein are not essential for membrane association of the α subunit but are required for receptor coupling. Proc. Natl. Acad. Sci. USA 87:4363–4367.
   PubMedGoogle Scholar
• Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164–175.
   PubMed Web of Science ®Google Scholar
• Bourbonnais, Y., D. Bolin, and D. Shields. 1988. Secretion of somatostatin by Saccharomyces cerevisiae. Correct proteolytic processing of pro- α-factor-somatostatin hybrids requires the products of the KEX2 and STE13 genes. J. Biol. Chem. 263:15342–15347.
   PubMed Web of Science ®Google Scholar
• Brake, A. J., J. P. Merryweather, D. G. Coit, U. A. Heberlein, F. R. Masiarz, G. T. Mullenbach, M. S. Urdea, P. Valenzuela, and P. J. Barr. 1984. a-Fac-tor-directed synthesis and secretion of mature foreign proteins in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 81:4642–4646.
   PubMed Web of Science ®Google Scholar
• Brenner, C., and R. S. Fuller. 1992. Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted, soluble Kex2 protease. Proc. Natl. Acad. Sci. USA 89:922–926.
   PubMedGoogle Scholar
• Christianson, T. W., R. S. Sikorski, M. Dante, J. H. Shero, and P. Hieter. 1992. Multifunctional yeast high-copy-number shuttle vectors. Gene 110:119–122.
   PubMed Web of Science ®Google Scholar
• Ciejek, D., and J. Thorner. 1979. Recovery of S. cerevisiae a cells from G1 arrest by α-factor pheromone requires endopeptidase action. Cell 18:623–635.
   PubMed Web of Science ®Google Scholar
• Eriotou-Bargiota, E., C.-B. Xue, F. Naider, and J. M. Becker. 1992. Antagonistic and synergistic peptide analogues of the tridecapeptide mating pheromone of Saccharomyces cerevisiae. Biochemistry 31:551–557.
   PubMedGoogle Scholar
• Garbow, J. R., M. Breslav, O. Antohi, and F. Naider. 1994. Conformational analysis of the Saccharomyces cerevisiae tridecapeptide mating pheromone by 13C., 15N rotational-echo double resonance nuclear magnetic resonance spectroscopy. Biochemistry 33:10094–10099.
   PubMedGoogle Scholar
• Gounarides, J. S., M. S. Broido, J. M. Becker, and F. R. Naider. 1993. Conformational analysis of [D-Ala9]-α-factor and [L-Ala9]-α-factor in solution in the presence of lipid. Biochemistry 32:908–917.
   PubMedGoogle Scholar
• Jelicks, L. A., M. S. Broido, J. M. Becker, and F. R. Naider. 1989. Interaction of the Saccharomyces cerevisiae α-factor with phospholipid vesicles as revealed by proton and phosphorus NMR. Biochemistry 28:4233–4240.
   PubMedGoogle Scholar
• Jelicks, L. A., F. R. Naider, P. Shenbagamurthi, J. M. Becker, and M. S. Broido. 1988. A type II β-turn in a flexible peptide: proton assignment and conformational analysis of the α-factor from Saccharomyces cerevisiae in solution. Biopolymers 27:431–449.
   PubMed Web of Science ®Google Scholar
• King, K., H. G. Dohlman, J. Thorner, M. G. Caron, and R. L. Lefkowitz. 1990. Control of yeast mating signal transduction by a mammalian β2-adrenergic receptor and Gs α subunit. Science 250:121–123.
   PubMedGoogle Scholar
• Klopotowski, T., and A. Wiater. 1965. Synergism of aminotriazole and phosphate on the inhibition of yeast imidazoleglycerolphosphate dehydratase. Arch. Biochem. Biophys. 112:562–566.
   PubMedGoogle Scholar
• Kron, S. J., and N. A. R. Gow. 1995. Budding yeast morphogenesis: signaling, cytoskeleton and cell cycle. Curr. Opin. Cell Biol. 7:845–855.
   PubMedGoogle Scholar
• Levin, Y., R. K. Khare, G. Abel, D. Hill, E. Eriotou-Bargiota, J. M. Becker, and F. Naider. 1993. Histidine of the α-factor of Saccharomyces cerevisiae is not essential for binding to its receptor or for biological activity. Biochemistry 32:8199–8206.
   PubMedGoogle Scholar
• Masui, Y., T. Tanaka, N. Chino, K. Kita, and S. Sakakibara. 1979. Amino acid substitution of mating factor of Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 86:982–987.
   PubMed Web of Science ®Google Scholar
• Naider, F., J. Gounarides, C.-B. Xue, E. Bargiota, and J. M. Becker. 1992. Studies on the yeast α-mating factor: a model for mammalian peptide hormones. Biopolymers 32:335–339.
   PubMedGoogle Scholar
• Price, L. A., E. M. Kajkowski, J. R. Hadcock, B. A. Ozenberger, and M. H. Pausch. 1995. Functional coupling of a mammalian somatostatin receptor to the yeast pheromone response pathway. Mol. Cell. Biol. 15:6188–6195.
   PubMed Web of Science ®Google Scholar
• Raths, S. K., F. Naider, and J. M. Becker. 1988. Peptide analogues compete with the binding of α-factor to its receptor in Saccharomyces cerevisiae. J. Biol. Chem. 263:17333–17341.
   PubMedGoogle Scholar
• Samokhin, G. P., L. V. Lizlova, J. D. Bespalova, M. I. Titov, and V. N. Smirnov. 1981. The effect of α-factor on the rate of cell-cycle initiation in Saccharomyces cerevisiae: α-factor modulates transition probability in yeast. Exp. Cell Res. 131:267–275.
   PubMedGoogle Scholar
• Sapperstein, S., C. Berkower, and S. Michaelis. 1994. Nucleotide sequence of the yeast STE14 gene, which encodes farnesylcysteine carboxyl methyl-transferase, and demonstration of its essential role in α-factor export. Mol. Cell. Biol. 14:1438–1449.
   PubMedGoogle Scholar
• Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3–21.
   PubMed Web of Science ®Google Scholar
• Sprague, G. F., Jr., and J. W. Thorner. 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae, p. 657–744. In E. W. Jones, J. R. Pringle, and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces: gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Stevenson, B. J., N. Rhodes, B. Errede, and G. F. Sprague, Jr. 1992. Constitutive mutants of the protein kinase STE11 activate the yeast pheromone response pathway in the absence of the G protein. Genes Dev. 6:1293–1304.
   PubMed Web of Science ®Google Scholar
• Struhl, K., and R. W. Davis. 1977. Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazoleglycerolphosphate dehydratase (his3). Proc. Natl. Acad. Sci. USA 74:5255–5259.
   PubMedGoogle Scholar
• Taylor, W. R. 1986. The classification of amino acid conservation. J. Theor. Biol. 119:205–218.
   PubMed Web of Science ®Google Scholar
• Xue, C.-B., E. Eriotou-Bargiota, D. Miller, J. M. Becker, and F. Naider. 1989. A covalently constrained congener of the Saccharomyces cerevisiae tridecapeptide mating pheromone is an agonist. J. Biol. Chem. 264:19161–19168.
   PubMedGoogle Scholar