The Mof2/Sui1 Protein Is a General Monitor of Translational Accuracy

REFERENCES

• Alani, E., L. Cao, and N. Kleckner 1987. A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains. Genetics 116: 541–545.
   PubMed Web of Science ®Google Scholar
• Anderson, R. P., and J. R. Menninger 1987. Tests of the ribosome editor hypothesis. III. A mutant Escherichia coli with a defective ribosome editor. Mol. Gen. Genet. 209: 313–318.
   PubMedGoogle Scholar
• Asano, K., T. G. Kinzy, W. C. Merrick, and J. W. B. Hershey 1997. Conservation and diversity of eukaryotic translation initiation factor eIF3. J. Biol. Sci. 272: 1101–1109.
   Google 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
• Balasundaram, D., J. D. Dinman, R. B. Wickner, C. W. Tabor, and H. Tabor 1994. Spermidine deficiency increases +1 ribosomal frameshifting efficiency and inhibits Ty1 retrotransposition in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 91: 172–176.
   PubMedGoogle Scholar
• Belcourt, M. F., and P. J. Farabaugh 1990. Ribosomal frameshifting in the yeast retrotransposon Ty: tRNAs induce slippage on a 7 nucleotide minimal site. Cell 62: 339–352.
   PubMed Web of Science ®Google Scholar
• Brierley, I. A., P. Dingard, and S. C. Inglis 1989. Characterization of an efficient coronavirus ribosomal frameshifting signal: requirement for an RNA pseudoknot. Cell 57: 537–547.
   PubMed Web of Science ®Google Scholar
• Burgess, S. M., and C. Guthrie 1993. Beat the clock: paradigms for NTPases in the maintenance of biological fidelity. Trends Biochem. Sci. 18: 381–384.
   PubMedGoogle Scholar
• Castilho-Valavicius, B., H. Yoon, and T. F. Donahue 1990. Genetic characterization of the Saccharomyces cerevisiae translational initiation suppressors sui1, sui2 and SUI3 and their effects on HIS4 expression. Genetics 124: 483–495.
   PubMedGoogle Scholar
• Chandler, M., and O. Fayet 1993. Translational frameshifting in the control of transposition in bacteria. Mol. Microbiol. 7: 497–503.
   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
• Cui, Y., J. D. Dinman, and S. W. Peltz 1996. mof4-1 is an allele of the UPF1/IFS2 gene which affects both mRNA turnover and −1 ribosomal frameshifting efficiency. EMBO J. 15: 5726–5736.
   PubMedGoogle Scholar
• Cui, Y., K. W. Hagan, S. Zhang, and S. W. Peltz 1995. Identification and characterization of genes that are required for the accelerated degradation of mRNAs containing a premature translational termination codon. Genes Dev. 9: 423–436.
   PubMed Web of Science ®Google Scholar
• Dinman, J. D. 1995. Ribosomal frameshifting in yeast viruses. Yeast 11: 1115–1127.
   PubMedGoogle Scholar
• Dinman, J. D., T. Icho, and R. B. Wickner 1991. A −1 ribosomal frameshifting in a double-stranded RNA virus of yeast forms a Gag-pol fusion protein. Proc. Natl. Acad. Sci. USA 88: 174–178.
   PubMed Web of Science ®Google Scholar
• Dinman, J. D., and T. G. Kinzy 1997. Translational misreading: mutations in translation elongation factor 1α differentially affect programmed ribosomal frameshifting and drug sensitivity. RNA 3: 870–881.
   PubMedGoogle Scholar
• Dinman, J. D., M. J. Ruiz-Echevarria, K. Czaplinski, and S. W. Peltz 1997. Peptidyl-transferase inhibitors have antiviral properties by altering programmed −1 ribosomal frameshifting efficiencies: development of model systems. Proc. Natl. Acad. Sci. USA 94: 6606–6611.
   PubMedGoogle Scholar
• Dinman, J. D., T. Icho, and R. B. Wickner 1991. A −1 ribosomal frameshifting in a double-stranded RNA virus of yeast forms a Gag-pol fusion protein. Proc. Natl. Acad. Sci. USA 88: 174–178.
   PubMed Web of Science ®Google Scholar
• Dinman, J. D., and R. B. Wickner 1992. Ribosomal frameshifting efficiency and gag/gag-pol ratio are critical for yeast M1 double-stranded RNA virus propagation. J. Virol. 66: 3669–3676.
   PubMed Web of Science ®Google Scholar
• Dinman, J. D., and R. B. Wickner 1994. Translational maintenance of frame: mutants of Saccharomyces cerevisiae with altered −1 ribosomal frameshifting efficiencies. Genetics 136: 75–86.
   PubMed Web of Science ®Google Scholar
• Dinman, J. D., and R. B. Wickner 1995. 5S rRNA is involved in fidelity of translational reading frame. Genetics 141: 95–105.
   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 eIF2β gene alter ribosomal start-site selection during the scanning process. Cell 54: 621–632.
   PubMed Web of Science ®Google Scholar
• Farabaugh, P. J. 1995. Post-transcriptional regulation by Ty retrotransposon of Saccharomyces cerevisiae. J. Biol. Chem. 270: 10361–10364.
   PubMedGoogle Scholar
• Fields, C., and M. D. Adams 1994. Expressed sequence tags identify a human isolog of the SUI1 translation initiation factor. Biochem. Biophys. Res. Commun. 198: 288–291.
   PubMedGoogle Scholar
• Hayashi, S.-I., and Y. Murakami 1995. Rapid and regulated degradation of ornithine decarboxylase. Biochem. J. 306: 1–10.
   PubMedGoogle Scholar
• Holtzman, D. A., S. Yang, and D. G. Drubin 1993. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J. Cell Biol. 122: 635–644.
   PubMed Web of Science ®Google Scholar
• Jacks, T., H. D. Madhani, F. R. Masiraz, and H. E. Varmus 1988. Signals for ribosomal frameshifting in the Rous sarcoma virus gag-pol region. Cell 55: 447–458.
   PubMed Web of Science ®Google Scholar
• Jacks, T., M. D. Power, F. R. Masiarz, P. Luciw, P. J. Barr, and H. E. Varmus 1988. Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 331: 280–283.
   PubMed Web of Science ®Google Scholar
• Jacks, T., and H. E. Varmus 1985. Expression of the Rous sarcoma virus pol gene by ribosomal frameshifting. Science 230: 1237–1242.
   PubMed Web of Science ®Google Scholar
• Kasperaitis, M. A. M., H. O. Voorma, and A. M. Thomas 1995. The amino acid sequence of eukaryotic translation initiation factor 1 and its similarity to yeast initiation factor SUI1. FEBS Lett. 365: 47–50.
   PubMedGoogle Scholar
• Kozak, M. 1992. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8: 197–225.
   PubMedGoogle Scholar
• Lee, S. I., J. G. Umen, and H. E. Varmus 1995. A genetic screen identifies cellular factors involved in retroviral −1 frameshifting. Proc. Natl. Acad. Sci. USA 92: 6587–6591.
   PubMedGoogle Scholar
• Menninger, J. R. 1975. Peptidyl transfer RNA dissociates during protein synthesis from ribosomes of Escherichia coli. J. Biol. Chem. 251: 3392–3398.
   Google Scholar
• Merrick, W. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56: 291–315.
   PubMedGoogle Scholar
• Naranda, T., S. E. Macmillan, T. F. Donahue, and J. W. Hershey 1996. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell. Biol. 16: 2307–2313.
   PubMed Web of Science ®Google Scholar
• Palmer, E., J. Wilhelm, and F. Sherman 1979. Phenotypic suppression of nonsense mutants in yeast by aminoglycoside antibiotics. Nature 277: 148.
   PubMedGoogle Scholar
• Peltz, S. W., J. L. Donahue, and A. Jacobson 1992. A mutation in the tRNA nucleotidyltransferase gene promotes stabilization of mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 12: 5778–5784.
   PubMedGoogle Scholar
• Rodnina, M. V., T. Pape, R. Fricke, L. Kuhn, and W. Wintermeyer 1996. Initial binding of the elongation factor Tu·GTP·aminoacyl-tRNA complex preceding codon recognition on the ribosome. J. Biol. Chem. 271: 646–652.
   PubMed Web of Science ®Google Scholar
• Rose, M. D., F. Winston, and P. Hieter 1990. Methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Singh, A., D. Ursic, and J. Davies 1979. Phenotypic suppression and misreading in Saccharomyces cerevisiae. Nature 277: 146.
   PubMed Web of Science ®Google Scholar
• Somogyi, P., A. J. Jenner, I. A. Brierley, and S. C. Inglis 1993. Ribosomal pausing during translation of an RNA pseudoknot. Mol. Cell. Biol. 13: 6931–6940.
   PubMed Web of Science ®Google Scholar
• Tarun, S. Z., and A. B. Sachs 1995. A common function for mRNA 3′ and 5′ ends in translation initiation in yeast. Genes Dev. 9: 2997–3007.
   PubMedGoogle Scholar
• TenDam, E., K. Pleij, and D. Draper 1992. Structural and functional aspects of RNA pseudoknots. Biochemistry 31: 11665–11676.
   PubMedGoogle Scholar
• Thomas, A., W. Spaan, H. Van Steeg, H. O. Voorma, and R. Benne 1980. Model of action of protein synthesis factor eIF-1 from rabbit reticulocytes. FEBS Lett. 116: 67–71.
   PubMedGoogle Scholar
• Thompson, R. C., and D. B. Dix 1982. Accuracy of protein biosynthesis. J. Biol. Chem. 257: 6677–6682.
   PubMedGoogle Scholar
• Tu, C., T.-H. Tzeng, and J. A. Bruenn 1992. Ribosomal movement impeded at a pseudoknot required for ribosomal frameshifting. Proc. Natl. Acad. Sci. USA 89: 8636–8640.
   PubMed Web of Science ®Google Scholar
• Yoon, H., and T. F. Donahue 1992. The sui1 suppressor locus in Saccharomyces cerevisiae encodes a translation factor that functions during tRNAiMet recognition of the start codon. Mol. Cell. Biol. 12: 248–260.
   PubMed Web of Science ®Google Scholar