Multiple Genes Coding for Precursors of Rhodotorucine A, a Farnesyl Peptide Mating Pheromone of the Basidiomycetous Yeast Rhodosporidium toruloides

LITERATURE CITED

• Abe, K., I. Kusaka, and S. Fukui. 1975. Morphological change in the early stages of the mating process of Rhodosporidium toruloides. J. Bacteriol. 122:710–718.
   PubMedGoogle Scholar
• Akada, R., K. Minomi, I. Yamashita, T. Miyakawa, and S. Fukui. 1987. Cloning of a gene coding for rhodotorucine A, a farnesyl peptide mating pheromone of Rhodosporidium toruloides. Agriç. Biol. Chem. 51:1211–1215.
   Web of Science ®Google Scholar
• Änderegg, R. J., R. Betz, S. A. Carr, J. W. Crabb, and W. Duntze. 1988. Structure of Saccharomyces cerevisiae mating hormone a-factor: identification of S-farnesyl cysteine as a structural component. J. Biol. Chem. 263:18236–18240.
   PubMed Web of Science ®Google Scholar
• Bailance, D. J.. 1986. Sequences important for gene expression in filamentous fungi. Yeast 2:229–236.
   PubMedGoogle Scholar
• Benoit, R., N. Ling, and F. Esch. 1987. A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites. Science 238:1126–1129.
   PubMed Web of Science ®Google Scholar
• Betz, R., J. W. Crabb, H. E. Meyer, R. Wittig, and W. Duntze. 1987. Amino acid sequences of a-factor mating peptides from Saccharomyces cerevisiae. J. Biol. Chem. 262:546–548.
   PubMedGoogle Scholar
• Birnstiel, M., M. Busslinger, and K. Strub. 1983. Transcription termination and 3′ processing: the end is in site! Cell 41:349–359.
   Google Scholar
• Brake, A. J., C. Brenner, R. Najarian, P. Laybourn, and J. Merryweather. 1985. Structure of genes encoding precursors of the yeast peptide mating pheromone a-factor, p. 103–108. In M.-J. Gething (ed.), Protein transport and secretion. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Brake, A. J., D. J. Julius, and J. Thorner. 1983. A functional prepro-a-factor gene in Saccharomyces yeasts can contain three, four, or five repeats of the mature pheromone sequence. Mol. Cell. Biol. 3:1440–1450.
   PubMed Web of Science ®Google Scholar
• Buss, J. E., and B. M. Sefton. 1986. Direct identification of palmitic acid as the lipid attached to p21rv. Mol. Cell. Biol. 6:116–122.
   PubMed Web of Science ®Google Scholar
• Chamberlain, J. P.. 1979, Fluorographic detection of radioactivity in Polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132–135.
   PubMed Web of Science ®Google Scholar
• Denhardt, D. T.. 1966. A membrane filter technique for the detection of complementary DNA. Biochem. Biophys. Res. Commun. 23:641–646.
   PubMed Web of Science ®Google Scholar
• Domdey, H., B. Apostol, R.-J. Lin, A. Newman, E. Brody, and J. Abelson. 1984. Lariat structures are in vivo intermediates in yeast pre-mRNA splicing. Cell 39:611–621.
   PubMed Web of Science ®Google Scholar
• Douglass, J., O. Civelli, and E. Herbert. 1984. Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Annu. Rev. Biochem. 53:665–715.
   PubMed Web of Science ®Google Scholar
• Dretzen, G., M. Bellard, P. Sassone-Corsi, and P. Chambon. 1981. A reliable method for the recovery of DNA fragments from agarose and acrylamide gels. Anal. Biochem. 112:295–298.
   PubMed Web of Science ®Google Scholar
• Feinberg, A. P., and B. Vogelstein. 1983. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132:6–13.
   PubMed Web of Science ®Google Scholar
• Fujiyama, A., K. Matsumoto, and F. Tamanoi. 1987. A novel yeast mutant defective in the processing of ras proteins: assessment of the effect of the mutation on processing steps. EMBO J. 6:223–228.
   PubMed Web of Science ®Google Scholar
• Fuller, R., A. Brake, R. Sterne, R. Kunisawa, D. Barnes, M. Flessel, and J. Thorner. 1986. Post-translational processing events in the maturation of yeast pheromone precursors, p. 461–476. In J. Hicks (ed.). Yeast cell biology. Alan R. Liss. Inc., New York.
   Google Scholar
• Herbert, E., and M. Uhler. 1982. Biosynthesis and polyprotein precursors to regulatory peptides. Cell 30:1–2.
   PubMed Web of Science ®Google Scholar
• Huynh, T. V., R. A. Young, and R. W. Davis. 1985. Constructing and screening cDNA libraries in XgtlO and Xgtll, p. 49–78. In D. M. Glover (ed.), DNA cloning, a practical approach, vol. 1. IRL Press, Oxford.
   Google Scholar
• Ishibashi, Y., Y. Sakagami, A. Isogai, and A. Suzuki. 1984. Structure of tremerogens A-9291-I and A-9291-VIII: peptidyl sex hormones of Tremella hrasiliensis. Biochemistry 23:1399–1404.
   Google Scholar
• Jensen, R., G. F. Sprague, Jr., and I. Herskowitz. 1983. Regulation of yeast mating-type interconversion: feedback control of HO gene expression by the mating-type locus. Proc. Natl. Acad. Sci. USA 80:3035–3039.
   PubMed Web of Science ®Google Scholar
• Julius, D., L. Blair, A. Brake, G. Sprague, and J. Thorner. 1983. Yeast α factor is processed from a larger precursor polypeptide: the essential role of a membrane-bound dipeptidyl aminopeptidase. Cell 32:839–852.
   PubMed Web of Science ®Google Scholar
• Julius, D., A. Brake, L. Blair, R. Kunisawa, and J. Thorner. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-a-factor. Cell 37:1075–1089.
   PubMed Web of Science ®Google Scholar
• Julius, D., R. Schekman, and J. Thorner. 1984. Glycosylation and processing of prepro-a-factor through the yeast secretory pathway. Cell 36:309–318.
   PubMed Web of Science ®Google Scholar
• Kamiya, Y., A. Sakurai, S. Tamura, N. Takahashi, K. Abe, E. Tsuchiya, S. Fukui, C. Kitada, and M. Fujino. 1978. Structure of rhodotorucine A, a novel lipopeptide, inducing mating tube formation in Rlodosporidium toridoides. Biochem. Biophys. Res. Commun. 83:1077–1083.
   PubMedGoogle Scholar
• Kamps, M. P., J. E. Buss, and B. M. Sefton. 1986. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptides substrates without inducing transformation. Cell 45:105–112.
   PubMedGoogle Scholar
• Kozak, M.. 1984. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 12:857–872.
   PubMed Web of Science ®Google Scholar
• Kurjan, J., and I. Herskowitz. 1982. Structure of a yeast pheromone gene (A/Fα): a putative α-factor precursor contains four tandem copies of mature α-factor. Cell 30:933–943.
   PubMed Web of Science ®Google Scholar
• Lerner, R. A., N. Green, H. Alexander, F.-T. Liu, J. G. Sutcliffe, and T. M. Shinnick. 1981. Chemically synthesized peptides predicted from the nucleotide sequence of the hepatitis B virus genome elicit antibodies reactive with the native envelope protein of Dane particles. Proc. Natl. Acad. Sci. USA 78:3403–3407.
   PubMed Web of Science ®Google Scholar
• March, C. J., B. Mosley, A. Larsen, D. P. Cerretti, G. Braedt, V. Price, S. Gillis, C. S. Henney, S. R. Kronheim, K. Grabstein, P. J. Conlon, T. P. Hopp, and D. Cosman. 1985. Cloning, sequence and expression of two distinct human interleukin-1 complementary DNAs. Nature (London) 315:641–647.
   PubMed Web of Science ®Google Scholar
• Marglin, A., and R. B. Merrifield. 1970. Chemical synthesis of peptides and proteins. Annu. Rev. Biochem. 39:841–866.
   PubMedGoogle Scholar
• McMaster, G. K., and G. G. Carmichael. 1977. Analysis of single- and double-stranded nucleic acids on Polyacrylamide and agarose gels by using glyoxal and acridine orange. Proc. Natl. Acad. Sci. USA 74:4835–4838.
   PubMed Web of Science ®Google Scholar
• Miyakawa, T., R. Miyama, M. Tabata, E. Tsuchiya, and S. Fukui. 1985. A study on the biosynthesis of tremerogen, 4-10. a polyisoprenyl peptide mating pheromone of Tremella mesenterica, using an inhibitor of mevalonate synthesis. Agric. Biol. Chem. 49:1343–1347.
   Web of Science ®Google Scholar
• Miyakawa, T., M. Nishihara, E. Tsuchiya, and S. Fukui. 1982. Role of metabolism of the mating pheromone in sexual differentiation of the heterobasidiomycete Rlwdosporidium toruloides. J. Bacteriol. 151:1184–1194.
   PubMedGoogle Scholar
• Nasmyth, K.. 1983. Molecular analysis of a cell lineage. Nature (London) 302:670–676.
   PubMed Web of Science ®Google Scholar
• Omary, M. B., and I. S. Trowbridge. 1981. Covalent binding of fatty acid to the transferrin receptor in cultured human cells. J. Biol. Chem. 256:4715–4718.
   PubMed Web of Science ®Google Scholar
• Powers, S., S. Michaelis, D. Broek, S. S. Anna-A, J. Field, I. Herskowitz, and M. Wigler. 1986. RAM. a gene of yeast required for a functional modification of RAS proteins and for production of mating pheromone a-factor. Cell 47:413–422.
   PubMedGoogle Scholar
• Rigby, P. W. J., M. Dieckmann, C. Rhodes, and P. Berg. 1977. Labeling deoxyribonucleic acid to high specific activity in vitro bv nick translation with DNA polymerase I. J. Mol. Biol. 113:237–251.
   PubMed Web of Science ®Google Scholar
• Rothblatt, J. A., J. R. Webb, G. Ammerer, and D. I. Meyer. 1987. Secretion in yeast: structural features influencing the post-translational translocation of prepro-α-factor in vitro. EMBO J. 6:3455–3463.
   PubMedGoogle Scholar
• Sakagami, V., A. Isogai, A. Suzuki, C. Kitada, and M. Fujino. 1979. Structure of tremerogen A-10, a peptidal hormone inducing conjugation tube formation in Tremella mesenterial. Agric. Biol. Chem. 43:2643–2645.
   Web of Science ®Google Scholar
• Sakagami, Y., M. Yoshida, A. Isogai, and A. Suzuki. 1981. Structure of tremerogen <7-13, a peptidal sex hormone of Tremella mesenterial. Agric. Biol. Chem. 45:1045–1047.
   Web of Science ®Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Schaefer, M., M. R. Picciotto, T. Kreiner, R.-R. Kaldany, R. Taussig, and R. H. Scheller. 1985. Aplysia neurons express a gene encoding multiple FMRFamide neuropeptides. Cell 41:457–467.
   PubMed Web of Science ®Google Scholar
• Schlesinger, M. J.. 1983. Fatty acid acylation of eukaryotic cell proteins. Methods Enzymol. 96:795–801.
   PubMedGoogle Scholar
• Schultz, A. M., L. E. Henderson, S. Oroszlan, E. A. Garber, and H. Hanafusa. 1985. Amino terminal myristylation of the protein kinase p60.s/r. a retroviral transforming protein. Science 227:427–429.
   PubMed Web of Science ®Google Scholar
• Schwartz, T. W.. 1986. The processing of peptide precursors, ‘proline-directed arginyl cleavage’ and other monobasic processing mechanisms. FEBS Lett. 200:1–10.
   PubMed Web of Science ®Google Scholar
• Singh, A., E. Y. Chen, J. M. Lugovoy, C. N. Chang, R. A. Hitzeman, and P. H. Seeburg. 1983. Saccharomyces cerevisiae contains two discrete genes coding for the α-factor pheromone. Nucleic Acids Res. 11:4049–4063.
   PubMed Web of Science ®Google Scholar
• Stark, G. R., and G. M. Wahl. 1984. Gene amplification. Annu. Rev. Biochem. 53:447–491.
   PubMed Web of Science ®Google Scholar
• Swank, R. T., and K. D. Munkres. 1971. Molecular weight analysis of oligopeptides by electrophoresis in Polyacrylamide gel with sodium dodecyl sulfate. Anal. Biochem. 39:462–477.
   PubMed Web of Science ®Google Scholar
• Thomas, P. S.. 1980. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77:5201–5205.
   PubMed Web of Science ®Google Scholar
• Tomiyoshi, Y., T. Miyakawa, E. Tsuchiya, and S. Fukui. 1981. Preparation and characterization of antisera directed against the peptide moiety of tremerogen A-10, a mating hormone of Tremella mesenterial. Agric. Biol. Chem. 45:1917–1919.
   Web of Science ®Google Scholar
• Willumsen, B. M., and A. Christensen. 1984. The p21 ras C-terminus is required for transformation and membrane association. Nature (London) 310:583–586.
   PubMed Web of Science ®Google Scholar