GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae

Genes and Development

Volumn 11, Issue 18, 1997, Pages 2396-2413

  Huang, Han Kuei ^a   Yoon, Heejeong ^a   Hannig, Ernest M ^b   Donahue, Thomas F ^a  

^a INDIANA UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS AT DALLAS   (United States)

Author keywords

AUG selection; eIF 2; eIF 5; GTP hydrolysis; Ribosomal scanning; Translation initiation

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATE; INITIATION FACTOR 2; PROTEIN SUBUNIT; TRANSFER RNA;

ARTICLE; DIPLOIDY; GENE ISOLATION; HAPLOIDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; RIBOSOME; SACCHAROMYCES CEREVISIAE; SITE DIRECTED MUTAGENESIS; START CODON; SUPPRESSOR GENE; TRANSLATION INITIATION;

SACCHAROMYCES CEREVISIAE;

EID: 0030886675     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.11.18.2396     Document Type: Article

References (56)

1. Balch, W.E. 1990. Small GTP-binding proteins in vesicular transport. Trends Biochem. Sci. 15: 473-477.
2. Bourne, H.R., D.A. Sanders, and F. McCormick. 1991. The GT-Pase superfamily: Conserved structure and molecular mechanism. Nature 349: 117-127.
3. Bushman, J.L., A.I. Asuru, R.L. Matts, and A.G. Hinnebusch. 1993a. Evidence that GCD6 and GCD7, translational regulator of GCN4, are subunits of guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 1920-1932.
4. Bushman, J.L., M. Foiani, A.M. Cigan, C.J. Paddon, and A.G. Hinnebusch. 1993b. Guanine nucleotide exchange factor for eukaryotic translation initiation factor 2 in Saccharomyces cerevisiae: Interactions between the essential subunits GCD2, GCD6 and GCD7 and the regulatory subunit GCN3. Mol. Cell. Biol. 13: 4618-4631.
5. Castilho-Valavacius, B., H. Yoon, and T.F. Donahue. 1990. Genetic characterization of the Saccharomyces cerevisiae translation initiation suppressors sui1, sui2, and SUI3 and their effects on HIS4 expression. Genetics 24: 483-495.
6. 2-Cys motif in the β subunit of eukaryotic translation initiation factor 2. Gene Exp. 2: 297-309.
7. Chakrabarti, A. and U. Maitra. 1991. Function of eukaryotic initiation factor 5 in the formation of 80S ribosome polypeptide chain initiation complex. J. Biol. Chem. 266: 14039-14045.
8. Chakravarti, D. and U. Maitra. 1993. Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae. J. Biol. Chem. 268: 10524-10533.
9. Chakravarti, D., T. Maiti, and U. Maitra. 1993. Isolation and immunochemical characterization of eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae. J. Biol. Chem. 268: 5754-5762.
10. r=48,000 and 38,000. J. Biol. Chem. 256: 3988-3994.
11. j functions in directing the scanning ribosome to the start site of translation. Science 242: 93-97.
12. Cigan, A.M., E.K. Pabich, and T.F. Donahue. 1988b. Mutational analysis of the HIS4 translational initiator region in Saccharomyces cerevisiae. Mol. Cell. Biol. 8: 2964-2975.
13. 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 identity with the human α subunit. Proc. Natl. Acad. Sci. 86: 2784-2788.
14. Cigan, A.M., J.L. Bushman, T.R. Boal, and A.G. Hinnebusch. 1993. A protein complex composed of translational regulators of GCN4 mRNA is the guanine nucleotide exchange factor for translation initiation factor 2 in yeast. Proc. Natl. Acad. Sci. 90: 5350-5354.
15. Das, K., J. Chevesich, and U. Maitra. 1993. Molecular cloning and expression of cDNA for mammalian translation initiation factor 5. Proc. Natl. Acad. Sci. 90: 3058-3062.
16. i ternary complexes. Mol. Cell. Biol. 15: 6351-6363.
17. 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.
18. Donahue, T.F., P.J. Farabaugh, and G.R. Fink. 1982. The nucleotide sequence of the HIS4 region of yeast. Gene 18: 47-59.
19. Donahue, T.F., A.M. Cigan, E.K. Pabich, and B. Castilho-Valavicius. 1988. Mutations at a Zn(II) finger motif in the yeast eIF-2β gene alter ribosomal start-site selection during the scanning process. Cell 54: 621-632.
20. Dubnoff, J.S. and U. Maitra. 1972. Characterization of the ribosome-dependent guanosine triphosphatase activity of polypeptide chain initiation factor IF 2. J. Biol. Chem. 247: 2876-2883.
21. Erickson, F.L. and E.M. Hannig. 1996. Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-subunit. EMBO J. 15: 6311-6320.
22. Gaspar, N.J., T.G. Kinzy, B.J. Scherer, M. Hümbelin, J.W.B. Hershey, and W.C. Merrick. 1994. Translation initiation factor eIF-2: Cloning and expression of the human cDNA encoding the γ-subunit. J. Biol. Chem. 269: 3415-3422.
23. Gualerzi, C.O. and C.L. Pon. 1990. Initiation of mRNA translation in prokaryotes. Biochemistry 29: 5881-5889.
24. Guthrie, C. and G.R. Fink. 1991. Guide to yeast genetics and molecular biology. Methods Enzymol. 194: .....
25. Hann, S.R., M.W. King, D.L. Bentley, C.W. Anderson, and C.W. Eisenman. 1988. A non-AUG translational initiation in c-myc exon 1 generates an N-terminally distinct protein whose synthesis is disrupted in Burkitt's lymphomas. Cell 52: 185-195.
26. Hannig, E.M., A.M. Cigan, B.A. Freeman, and T.G. Kinzy. 1993. GCD11, a negative regulator of GCN4 expression, encodes the γ subunit of eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 13: 506-520.
27. Hershey, J.W.B. 1991. Translational control in mammalian cells. Annu. Rev. Biochem. 60: 717-755.
28. Huang, H.-k. and T.F. Donahue. 1997. The fundamentals of translation initiation. In mRNA metabolism and post-transcriptional gene regulation (ed. J.B. Harford and D.R. Morris), Vol. 17. pp. 147-164. John Wiley & Sons, Inc., New York, NY.
29. Kasperaitis, M.A.M., H.O. Voorma, and A.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.
30. Koepp, D.M. and P.A. Silver. 1996. A GTPase controlling nuclear trafficking: Running the right way or walking randomly? Cell 87: 1-4.
31. Kozak, M. 1978. How do eukaryotic ribosomes select initiation regions in messenger RNA? Cell 15: 1109-1123.
32. _. 1989a. The scanning model for translation: An update. J. Cell Biol. 108: 229-241.
33. _. 1989b. Context effects and inefficient initiation at non-AUG codons in eukaryotic cell-free translation system. Mol. Cell. Biol. 9: 5073-5080.
34. Merrick, W.C. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56: 291-315.
35. Naranda, T., S.E. MacMillan, T.F. Donahue, and J.W.B. Hershey. 1996. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol. Cell. Biol. 16: 2307-2313.
36. Phe, EF-Tu, and a GTP analog. Science 270: 1464-1472.
37. Orr-Weaver, T.L., J.W. Szostak, and R.J. Rothstem. 1983. Genetic applications of yeast transformation with linear and gapped plasmids. Methods Enzymol. 101: 228-245.
38. 2+ and guanine nucleotide exchange factor on the binding of guanine nucleotides to eukaryotic initiation factor 2. J. Biol. Chem. 263: 5519-5525.
39. Parent, S.A., C.M. Fenimore, and K.A. Bostain. 1985. Vector systems for the expression, analysis and cloning of DNA sequences in S. cerevisiae. Yeast 1: 83-138.
40. Pathak, V.K., P.J. Nielsen, H. Trachsel, and J.W.B. Hersey. 1988. Structure of the β subunit of translation initiation factor eIF-2. Cell 54: 633-639.
41. Peterson, D.T., B. Safer, and W.C. Merrick. 1979. Role of eukaryotic initiation factor 5 in the formation of 80S initiation complex. J. Biol. Chem. 254: 7730-7735.
42. Rothstein, R.J. 1983. One-step gene disruption in yeast. Methods Enzymol. 101: 202-210.
43. Roeder, G.S. and G.R. Fink. 1980. DNA rearrangements associated with a transposable element in yeast. Cell 21: 239-249.
44. Rybin, V., O. Ullrich, M. Rubino, K. Alexandrov, I. Silmon, M.C. Seabra, R. Goody, and M. Zerial. 1996. GTPase activity of Rab5 acts as a timer for endocytic membrane fusion. Nature 383: 266-269.
45. Sambrook, J., E.F. Fristch, and T. Maniatis. 1989. Molecular cloning: A laboratory manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
46. Sanger, F., S. Nicklen, and A.R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. 74: 5463-5467.
47. Sikorski, R.S. and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
48. Thompson, R.C. 1988. EFTu provides an internal kinetic standard for translation accuracy. Trends Biochem. Sci. 13: 91-93.
49. Thompson, R.C., D.B. Dix, and A.M. Karim. 1986. The reaction of ribosomes with elongation factor Tu · GTP complexes: Aminoacyl-tRNA-independent reactions in the elongation cycle determine the accuracy of protein synthesis. J. Biol. Chem. 261: 4868-4874.
50. Toraño, A., A. Sandoval, and C.F. Heredia. 1974. Soluble protein factors and ribosomal subunits from yeast. Interactions with ammoacyl-tRNA. Methods Enzymol. 30: 254-261.
51. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose: Procedure and some applications. Proc. Natl. Acad. Sci. 76: 4350-4354.
52. von Mollard, G.F., B. Stahl, C. Li, T.C. Südhof, and R. Jahn. 1994. Rab proteins in regulated exocytosis. Trends Biochem. Sci. 19: 164-168.
53. Warner, J.R. and C. Gorenstein. 1978. The ribosomal proteins of Saccharomyces cerevisiae. Methods Cell Biol. 20: 45-60.
54. Williams, N.P., A.G. Hinnebusch, and T.F. Donahue. 1989. Mutations in the structural genes for eukaryotic translation initiation factors 2α and 2β of Saccharomyces cerevisiae disrupt translational control of GCN4 mRNA. Proc. Natl. Acad. Sci. 86: 7515-7519.
55. Wu, S., K. Zeng, I.A. Wilson, and W.E. Balch. 1996. Structural insights into the function of the Rab GDI superfamily. Trends Biochem. Sci. 21: 472-476.
56. i recognition of the start codon. Mol. Cell. Biol. 12: 248-260.