The Two Forms of Karyogamy Transcription Factor Kar4p Are Regulated by Differential Initiation of Transcription, Translation, and Protein Turnover

REFERENCES

• Apanovitch, D. M., K. C. Slep, P. B. Sigler, and J. Dohlman 1998. Sst2 is a GTPase-activating protein for Gpa1: purification and characterization of a cognate RGS-Gα protein pair in yeast. Biochemistry 37:4815–4822.
   PubMedGoogle Scholar
• Ausubel, F. M. 1987. Current protocols in molecular biology. Greene Publishing Associates, Brooklyn, N.Y.
   Google Scholar
• Bachmair, A., D. Finley, and J. Varshavsky 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179–186.
   PubMed Web of Science ®Google Scholar
• Beh, C. T., V. Brizzio, and J. Rose 1997. KAR5 encodes a novel pheromone-inducible protein required for homotypic nuclear fusion. J. Cell Biol. 139:1063–1076.
   PubMedGoogle Scholar
• Beltzer, J. P., S. R. Morris, and J. Kohlhaw 1988. Yeast LEU4 encodes mitochondrial and nonmitochondrial forms of alpha-isopropylmalate synthase. J. Biol. Chem. 263:368–374.
   PubMedGoogle Scholar
• Boguta, M., L. A. Hunter, W.-C. Shen, E. C. Gillman, N. C. Martin, and J. Hopper 1994. Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol. Mol. Cell. Biol. 14:2298–2306.
   PubMed Web of Science ®Google Scholar
• Byers, B., and J. Goetsch 1975. Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae. J. Bacteriol. 124:511–523.
   PubMed Web of Science ®Google Scholar
• Chatton, B., P. Walter, J. P. Ebel, F. Lacroute, and J. Fasiolo 1988. The yeast VAS1 gene encodes both mitochondrial and cytoplasmic valyl-tRNA synthetases. J. Biol. Chem. 263:52–57.
   PubMed Web of Science ®Google Scholar
• Cigan, A. M., E. K. Pabich, and J. Donahue 1988. Mutational analysis of the HIS4 translational initiator region in Saccharomyces cerevisiae. Mol. Cell. Biol. 8:2964–2975.
   PubMed Web of Science ®Google Scholar
• Donahue, T. F., and J. Cigan 1988. Genetic selection for mutations that reduce or abolish ribosomal recognition of the HIS4 translational initiator region. Mol. Cell. Biol. 8:2955–2963.
   PubMedGoogle Scholar
• Errede, B., R. M. Cade, B. M. Yashar, Y. Kamada, D. E. Levin, K. Irie, and J. Matsumoto 1995. Dynamics and organization of MAP kinase signal pathways. Mol. Reprod. Dev. 42:477–485.
   PubMed Web of Science ®Google Scholar
• Gammie, A. E., and J. Crosa 1991. Co-operative autoregulation of a replication protein gene. Mol. Microbiol. 5:3015–3023.
   PubMedGoogle Scholar
• Gammie, A. E., L. J. Kurihara, R. B. Vallee, and J. Rose 1995. DNM1, a dynamin-related gene, participates in endosomal trafficking in yeast. J. Cell Biol. 130:553–566.
   PubMedGoogle Scholar
• Gill, G., and J. Ptashne 1988. Negative effect of the transcriptional activator GAL4. Nature 334:721–724.
   PubMed Web of Science ®Google Scholar
• Hershko, A. 1997. Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr. Opin. Cell Biol. 9:788–799.
   PubMed Web of Science ®Google Scholar
• Herskowitz, I. 1995. MAP kinase pathways in yeast: for mating and more. Cell 80:187–197.
   PubMed Web of Science ®Google Scholar
• Hicke, L., and J. Riezman 1996. Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell 84:277–287.
   PubMed Web of Science ®Google Scholar
• Hicke, L., B. Zanolari, and J. Riezman 1998. Cytoplasmic tail phosphorylation of the α-factor receptor is required for its ubiquitination and internalization. J. Cell Biol. 141:349–358.
   PubMed Web of Science ®Google Scholar
• Hinnebusch, A. G., and J. Liebman 1991. Protein synthesis and translational control in Saccharomyces cerevisiae The molecular and cellular biology of the yeast Saccharomyces: genome dynamics, protein synthesis, and energetics In J. R. Broach, J. R. Pringle, E. W. Jones (ed.), 1:627–735 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Hochstrasser, M. 1992. Ubiquitin and intracellular protein degradation. Curr. Opin. Cell Biol. 4:1024–1031.
   PubMedGoogle Scholar
• Hochstrasser, M. 1996. Ubiquitin-dependent protein degradation. Annu. Rev. Genet. 30:405–439.
   PubMed Web of Science ®Google Scholar
• Hochstrasser, M., M. J. Ellison, V. Chau, and J. Varshavsky 1991. The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl. Acad. Sci. USA 88:4606–4610.
   PubMed Web of Science ®Google Scholar
• Kassir, Y., and J. Simchen 1991. Monitoring meiosis and sporulation in Saccharomyces cerevisiae. Methods Enzymol. 194:94–110.
   PubMedGoogle Scholar
• Kurihara, L. J., C. T. Beh, M. Latterich, R. Schekman, and J. Rose 1994. Nuclear congression and membrane fusion: two distinct events in the yeast karyogamy pathway. J. Cell Biol. 126:911–923.
   PubMedGoogle Scholar
• Kurihara, L. J., B. G. Stewart, A. E. Gammie, and J. Rose 1996. Kar4p, a karyogamy-specific component of the yeast pheromone response pathway. Mol. Cell. Biol. 16:3990–4002.
   PubMedGoogle Scholar
• Leberer, E., D. Y. Thomas, and J. Whiteway 1997. Pheromone signalling and polarized morphogenesis in yeast. Curr. Opin. Genet. Dev. 7:59–66.
   PubMedGoogle Scholar
• Levin, D. E., and J. Errede 1995. The proliferation of MAP kinase signaling pathways in yeast. Curr. Opin. Cell Biol. 7:197–202.
   PubMed Web of Science ®Google Scholar
• Madura, K., and J. Varshavsky 1994. Degradation of G α by the N-end rule pathway. Science 265:1454–1458.
   PubMed Web of Science ®Google Scholar
• Marsh, L., and J. Rose 1997. The pathway of cell and nuclear fusion during mating in S. cerevisiae The molecular and cellular biology of the yeast Saccharomyces: cell cycle and cell biology In J. R. Pringle, J. R. Broach, E. W. Jones (ed.), 3:827–888 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Meluh, P. B., and J. Rose 1990. KAR3, a kinesin-related gene required for yeast nuclear fusion. Cell 60:1029–1041.
   PubMed Web of Science ®Google Scholar
• Miller, R. K., and J. Rose 1998. Kar9p is a novel cortical protein required for cytoplasmic microtubule orientation in yeast. J. Cell Biol. 140:377–390.
   PubMed Web of Science ®Google Scholar
• Natsoulis, G., F. Hilger, and J. Fink 1986. The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae. Cell 46:235–243.
   PubMed Web of Science ®Google Scholar
• Ohashi, A., J. Gibson, I. Gregor, and J. Schatz 1982. Import of proteins into mitochondria. The precursor of cytochrome c1 is processed in two steps, one of them heme-dependent. J. Biol. Chem. 257:13042–13047.
   PubMed Web of Science ®Google Scholar
• Page, B. D., L. L. Satterwhite, M. D. Rose, and J. Snyder 1994. Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein. J. Cell Biol. 124:507–519.
   PubMedGoogle Scholar
• Rose, A. M., P. B. Joyce, A. K. Hopper, and J. Martin 1992. Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nuclei. Mol. Cell. Biol. 12:5652–5658.
   PubMedGoogle Scholar
• Rose, M. D., F. Winston, P. Hieter 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Sambrook, J., E. F. Fritsch, T. Maniatis 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Schneider, B. L., W. Seufert, B. Steiner, Q. H. Yang, and J. Futcher 1995. Use of polymerase chain reaction epitope tagging for protein tagging in Saccharomyces cerevisiae. Yeast 11:1265–1274.
   PubMedGoogle Scholar
• Schwob, E., T. Bohm, M. D. Mendenhall, and J. Nasmyth 1994. The B-type cyclin kinase inhibitor p40SIC1 controls the G1 to S transition in S. cerevisiae. Cell 79:233–244.
   PubMed Web of Science ®Google Scholar
• Sikorski, R. S., and J. Hieter 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
   PubMed Web of Science ®Google Scholar
• Smith, S. E., M. Koegl, and J. Jentsch 1996. Role of the ubiquitin/proteasome system in regulated protein degradation in Saccharomyces cerevisiae. Biol. Chem. 377:437–446.
   PubMed Web of Science ®Google Scholar
• Sprague, G. F., and J. Thorner 1992. Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae The molecular and cellular biology of the yeast Saccharomyces: gene expression In J. R. Broach, J. R. Pringle, E. W. Jones (ed.), 2:657–744 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Taussig, R., and J. Carlson 1983. Nucleotide sequence of the yeast SUC2 gene for invertase. Nucleic Acids Res. 11:1943–1954.
   PubMed Web of Science ®Google Scholar
• Varshavsky, A. 1995. The N-end rule. Cold Spring Harbor Symp. Quant. Biol. 60:461–478.
   PubMedGoogle Scholar
• Varshavsky, A. 1992. The N-end rule. Cell 69:725–735.
   PubMed Web of Science ®Google Scholar
• Wolfe, C. L., Y. C. Lou, A. K. Hopper, and J. Martin 1994. Interplay of heterogeneous transcriptional start sites and translational selection of AUGs dictate the production of mitochondrial and cytosolic/nuclear tRNA nucleotidyltransferase from the same gene in yeast. J. Biol. Chem. 269:13361–13366.
   PubMedGoogle Scholar
• Zitomer, R. S., D. A. Walthall, B. C. Rymond, and J. Hollenberg 1984. Saccharomyces cerevisiae ribosomes recognize non-AUG initiation codons. Mol. Cell. Biol. 4:1191–1197.
   PubMedGoogle Scholar