The sail Suppressor Locus in Saccharomyces cerevisiae Encodes a Translation Factor That Functions during tRNA^Met_i Recognition of the Start Codon

References

• Ahmad, M. F., N. Nasrin, M. K. Bagchi, I. Chakravarty, and N. K. Gupta. 1985. A comparative study of the characteristics of eIF-2 and eIF-2-ancillary factor activities from yeast Saccharomyces cerevisiae and rabbit reticulocytes. J. Biol. Chem. 260:6960–6965.
   PubMedGoogle Scholar
• Baim, S. B., D. F. Pietras, D. C. Eustice, and F. Sherman. 1985. A mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c. Mol. Cell. Biol. 5:1839–1846.
   PubMedGoogle Scholar
• Burgin, A. B., K. Parodos, D. J. Lane, and N. R. Pace. 1990. The excision of intervening sequences from Salmonella 23S ribosomal RNA. Cell 60:405–414.
   PubMedGoogle Scholar
• Castilho-Valavicius, B., H. Yoon, and T. F. Donahue. 1990. Genetic characterization of the Saccharomyces cerevisiae translational initiation suppressors sai1, sui2 and SUI3 and their effects on HIS4 expression. Genetics 124:483–495.
   PubMedGoogle Scholar
• Cigan, A. M., L. Feng, and T. F. Donahue. 1988. tRNAMeti functions in directing the scanning ribosome to the site of translation. Science 242:93–97.
   PubMed Web of Science ®Google Scholar
• Cigan, A. M., E. K. Pabich, and T. F. 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
• Cigan, A. M., E. K. Pabich, L. Feng, and T. F. Donahue. 1989. Yeast translation initiation suppressor sui2 encodes the α subunit of eukaryotic initiation factor 2 and shares sequence identity with the human α subunit. Proc. Natl. Acad. Sci. USA 86:2784–2788.
   PubMed Web of Science ®Google Scholar
• de Pater, B. S., and R. Schilperoort, and L. A. M. Hensgens. Unpublished data.
   Google Scholar
• Dieckmann, C. L., and A. Tzagoloff. 1985. Assembly of the mitochondrial membrane system. J. Biol. Chem. 260:1513–1520.
   PubMedGoogle Scholar
• Donahue, T. F., and A. M. 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
• Donahue, T. F., A. M. Cigan, E. K. Pabich, and B. Castilho-Valavicius. 1988. Mutations at a Zn(II) finger motif in the yeast elF-2β gene alter ribosomal start-site selection during the scanning process. Cell 54:621–632.
   PubMed Web of Science ®Google Scholar
• Donahue, T. F., P. J. Farabaugh, and G. R. Fink. 1983. The nucleotide sequence of the HIS4 region of yeast. Gene 18:47–59.
   Google Scholar
• Ernst, H., R. F. Duncan, and J. W. B. Hershey. 1987. Cloning and sequencing of complementary DNAs encoding the α-sub- unit of translation initiation factor elF-2. J. Biol. Chem. 262:1206–1212.
   PubMedGoogle Scholar
• Gupta, N. K., C. L. Woodley, Y. N. Chen, and K. K. Bose. 1973. Protein synthesis in rabbit reticulocytes: assays, purification, and properties of different ribosomal factors and their roles in polypeptide chain initiation. J. Biol. Chem. 248:4500–4511.
   PubMedGoogle Scholar
• Hartwell, L. H., and C. S. McLaughlin. 1969. A mutant of yeast apparently defective in the initiation of protein synthesis. Proc. Natl. Acad. Sci. USA 62:468–474.
   PubMedGoogle Scholar
• Hershey, J. W. B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60:717–754.
   PubMed Web of Science ®Google Scholar
• Hewick, R. M., M. W. Hunkapiller, L. E. Hood, and W. J. Dreyer. 1981. A gas-liquid solid phase peptide and protein sequenator. J. Biol. Chem. 256:7790–7997.
   Google Scholar
• Kozak, M. 1978. How do eucaryotic ribosomes select initiation regions in messenger RNA? Cell 15:1109–1123.
   PubMed Web of Science ®Google Scholar
• Kozak, M. 1980. Evaluation of the 'scanning model' of initiation of protein synthesis in eucaryotes. Cell 22:7–8.
   PubMed Web of Science ®Google Scholar
• Maxam, A. M., and W. Gilbert. 1980. Sequencing end-labelled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499–560.
   PubMedGoogle Scholar
• Orr-Weaver, T. L., J. K. Szostak, and R. J. Rothstein. 1983. Genetic applications of yeast transformation with linear and gapped plasmids. Methods Enzymol. 101:228–245.
   PubMed Web of Science ®Google Scholar
• Pathak, V. K., P. Nielsen, H. Trachsel, and J. W. B. Hershey. 1988. Structure of the β subunit of translation initiation factor elF-2. Cell 54:633–639.
   PubMedGoogle Scholar
• Petes, T. D., L. M. Hereford, and K. G. Skryabin. 1978. Characterization of two types of yeast ribosomal DNA genes. J. Bacteriol. 134:295–305.
   PubMedGoogle Scholar
• Rothstein, R. J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101:202–211.
   PubMed Web of Science ®Google Scholar
• Safer, B. 1989. Nomenclature of initiation, elongation and termination factors for translation in eukaryotes. Eur. J. Biochem. 186:1–3.
   PubMedGoogle 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
• Schnier, J., H. G. Schwelberger, Z. Smit-McBride, H. A. Kang, and J. W. B. Hershey. 1991. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 11:3105–3114.
   PubMedGoogle Scholar
• Schreier, M. H., B. Erni, and T. Staehelin. 1977. Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors. J. Mol. Biol. 116:727–753.
   PubMed Web of Science ®Google Scholar
• Sherman, F. 1990. Protein modifications and mitochondrial import of yeast cytochrome c: an overview, p. 637–646. In J. E. G. McCarthy and M. F. Tuite (ed.), Post-transcriptional control of gene expression. Springer-Verlag KG, Berlin.
   Google Scholar
• Sherman, F., G. R. Fink, and C. W. Lawrence. 1972. Methods in yeast genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Sherman, F., and J. W. Stewart. 1982. Mutations altering initiation of translation of yeast iso-l-cytochrome c: contrasts between the eukaryotic and prokaryotic initiation process, p. 301–333. In J. N. Strathern, E. W. Jones, and J. R. Broach (ed.), The molecular biology of the yeast Saccharomyces: metabolism and gene expression. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Thomas, A., H. Goumans, H. O. Voorma, and R. Benne. 1980. The mechanism of action of eukaryotic initiation factor 4C in protein synthesis. Eur. J. Biochem. 107:39–45.
   PubMedGoogle Scholar
• Woolford, J. L., Jr., and J. R. Warner. 1982. The ribosome and its synthesis. In J. R. Broach, E. W. Jones, and J. Pringle (ed.), The molecular and cellular biology of the yeast Saccharomyces: genome dynamics, protein synthesis, and energetics, in press. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar