Ligand interactions with eukaryotic translation initiation factor 2: Role of the γ-subunit

EMBO Journal

Volumn 15, Issue 22, 1996, Pages 6311-6320

  Erickson, F Les ^a   Hannig, Ernest M ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

Author keywords

Eukaryotic initiation factor 2; Protein synthesis; subunit

Indexed keywords

GUANINE NUCLEOTIDE; HISTIDINE; INITIATION FACTOR 2; METHIONINE TRANSFER RNA; PROTEIN SUBUNIT; TRANSFER RNA;

ARTICLE; DISSOCIATION CONSTANT; ESCHERICHIA COLI; EUKARYOTE; GENE MUTATION; LIGAND BINDING; PRIORITY JOURNAL; TRANSLATION INITIATION; YEAST;

BACTERIA (MICROORGANISMS); ESCHERICHIA; ESCHERICHIA COLI; EUKARYOTA;

EID: 0029858531     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb01021.x     Document Type: Article

References (67)

1. Ahmad, M.F., Nasrin, N., Bagchi, M.K., Chakravarty, I. and Gupta, N.K. (1985a) 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.
2. Ahmad, M.F., Nasrin, N., Banerjee, A.C. and Gupta, N.K. (1985b) Purification and properties of eukaryotic initiation factor 2 and its ancillary protein factor (Co-eIF-2A) from yeast Saccharomyces cerevisiae. J. Biol. Chem., 60, 6955-6959.
3. Val. Eur. J. Biochem., 141, 483-487.
4. Arai, K., Kawakita, M. and Kaziro, Y. (1974) Studies on the polypeptide elongation factors from E. coli. V. Properties of various complexes containing EF-Tu and EF-Ts. J. Biochem., 76, 293-306.
5. Ausubel, F.M. Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (1995) Current Protocols in Molecular Biology. John Wiley and Sons, Chichester, UK.
6. Baan, R.A., Keller, P.B. and Dahlberg, A.E. (1981) Isolation of eukaryotic initiation factor 2 from yeast Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 256, 1063-1066.
7. Barrieux, A. and Rosenfeld, M.G. (1977) Characterization of GTP-dependent Met-tRNA, binding protein. J. Biol. Chem., 252, 3843-3847.
8. Berchtold, H., Reshetnikova, L., Reiser, C.O.A., Schirmer, N.K., Sprinzl, M. and Hilgenfeld, R. (1993) Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature, 365, 126-132.
9. Bommer, U.-A., Kraft, R., Kurzchalia, T.V., Price, N.T. and Proud, C.G. (1991) Amino acid sequence analysis of the β- and γ-subunits of eukaryotic initiation factor eIF-2. Identification of regions interacting with GTP. Biochim. Biophys. Acta, 1079, 308-315.
10. Bourne, H.R., Sanders, D.A. and McCormick, F. (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature, 349, 117-127.
11. Bushman, J.L., Asuru, A.I., Matts, R.L. and Hinnebusch, A.G. (1993) Evidence that GCD6 and GCD7, translational regulators of GCN4, are subunits of the guanine nucleotide exchange factor for eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 1920-1932.
12. Bystrom, A.S. and Fink, G.R. (1989) A functional analysis of the repeated methionine initiator tRNA genes (IMT) in yeast. Mol. Gen. Genet., 216, 276-286.
13. Cigan, A.M., Pabich, E.K., Feng, L. and Donahue, T.F. (1989) Yeast translation initiation suppressor sui2 encodes the α-subunit of eukaryotic initiation factor 2 and snares identity with the human α-subunit. Proc. Natl Acad Sci. USA, 86, 2784-2788.
14. Cigan, A.M., Bushman, J.L., Boal, T.R. and Hinnebusch, A.G. (1993) A protein complex of translational regulators of GCN4 mRNA is the guanine nucleotide-exchange factor for translation initiation factor 2 in yeast. Proc. Natl Acad. Sci. USA, 90, 5350-5354.
15. Clanton, D.J., Hattori, S. and Shih, T.Y. (1986) Mutations of the ras gene product p21 that abolish guanine nucleotide binding. Proc. Natl Acad. Sci. USA, 83, 5076-5080.
16. Cooper, H.L. and Braverman, R. (1981) Close correlation between initiator methionyl-tRNA level and rate of protein synthesis during human lymphocyte growth cycle. J. Biol. Chem., 256, 7461-7467.
17. H mutants deficient in GTP binding. Mol. Cell. Biol., 6, 3291-3294.
18. Dever, T.E., Glynias, M.T. and Merrick, W.C. (1987) The GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl Acad. Sci USA, 84, 1814-1818.
19. Dever, T.E., Feng, L., Wek, R.C., Cigan, A.M., Donahue, T.F. and Hinnebusch, A.G. (1992) Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell, 68, 585-596.
20. i ternary complexes. Mol. Cell. Biol., 15, 6351-6353.
21. Donahue, T.F., Cigan, A.M., Pabich, E.K. and Valavicius, B.C. (1988) Mutations at a Zn(H) finger motif in the yeast eIF-2β gene alter ribosomal start-site selection during the scanning process. Cell, 54, 621-632.
22. Dorris, D.R., Erickson, F.L. and Hannig, E.M. (1995) Mutations in GCD11, the structural gene for eIF-2γ in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis. EMBO J., 14, 2239-2249.
23. Dubnoff, J.S. and Maitra, U. (1971) Isolation and properties of protein factors involved in polypeptide chain initiation in Escherichia coli. Methods Enzymol., 20, 248-261.
24. Ernst, H., Duncan, R.F. and Hershey, J.W.B. (1987) Cloning and sequencing of complementary DNAs encoding the α-subunit of translational initiation factor eIF-2. J. Biol. Chem., 262, 1206-1212.
25. Flynn A, Oldfield, S. and Proud, C.G. (1993) The role of the β-subunit of initiation factor eIF-2 in initiation complex formation. Biochim. Biophys. Acta, 1174, 117-121.
26. Gaspar, N.J., Kinzy, T.G., Scherer, B.J., Humbelin, M., Hershey, J.W.B. and Merrick, W.C. (1994) Translation initiation factor eIF-2. Cloning and expression of the human cDNA encoding the γ-subunit. J. Biol. Chem., 269, 3415-3422.
27. Met. Biochem. Biophys. Res. Commun., 181, 1500-1507.
28. Haney, S.A. and Broach, J.R. (1994) Cdc25p, the guanine nucleotide exchange factor for the Ras proteins of Saccharomyces cerevisiae, promotes exchange by stabilizing Ras in a nucleotide-free state. J. Biol. Chem., 269, 16541-16548.
29. Hannig, E.M. and Hinnebusch, A.G. (1988) Molecular analysis of GCN3, a translational activator of GCN4: evidence for posttranslational control of GCN3 regulatory function. Mol. Cell. Biol., 8, 4808-4820.
30. Hannig, E.M., Cigan, A.M., Freeman, B.A. and Kinzy, T.G. (1993) GCD11, a negative regulator of GCN4 expression, encodes the γ subunit of eIF-2 in Sacchammyces cerevisiae. Mol. Cell Biol., 13, 506-520.
31. Hershey, J.W.B. (1989) Protein phosphorylation controls translation rates. J. Biol. Chem., 264, 20823-20826.
32. Hershey, J.W.B. (1991) Translational control in mammalian cells. Annu. Rev. Biochem., 60, 717-755.
33. Hinnebusch, A.G. (1993) Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol., 10, 215-223.
34. Hinnebusch, A.G. (1994) Translational control of GCN4: an in vivo barometer of initiation-factor activity. Trends Biochem. Sci., 19, 409-414.
35. Hinnebusch, A.G. and Liebman, S.W. (1991) Protein synthesis and translational control in Sacchammyces cerevisiae. In Broach, J.R., Pringle, J.R. and Jones, E.W. (eds), The Molecular and Cellular Biology of the Yeast Saccharomyces. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
36. Hwang, Y.-W., Sanchez, A. and Miller, D.L. (1989) Mutagenesis of bacterial elongation factor Tu at lysine 136. J. Biol. Chem., 264, 8304-8309.
37. Hwang, Y.-W., Carter, M. and Miller, D.L. (1992) The identification of a domain in Escherichia colt elongation factor Tu that interacts with elongation factor Ts. J. Biol. Chem., 267, 22198-22205.
38. Hwang, Y.-W., Zhong, J.-M., Poullet, P. and Parmeggiani, A. (1993) Inhibition of SDC25 C-domain-induced guanine nucleotide exchange by guanine ring binding domain mutants of v-H-ras. J. Biol. Chem., 268, 24692-24698.
39. Jonak, J., Petersen, T.E., Meloun, B. and Rychlik, I. (1984) Histidine residues in elongation factor Tu from Escherichia coli protected by aminoacyl-tRNA against photo-oxidation. Eur. J. Biochem., 144, 295-303.
40. Jurnak, F., Heffron, S., Schick, B. and Delaria, K. (1990) Three-dimensional models of the GDP and GTP forms of the guanine nucleotide domain of Escherichia coli elongation factor Tu. Biochim. Biophts. Acta, 1050, 209-214.
41. Kjeldgaard, M. and Nyborg, J. (1992) Refined structure of elongation factor EF-Tu from Escherichia coli. J. Mol. Biol., 223, 721-742.
42. Kjeldgaard, M., Nissen, P., Thirup, S. and Nyborg, J. (1993) The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure, 1, 35-50.
43. Konieczny, A. and Safer, B. (1983) Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange activity during protein synthesis. J. Biol. Chem., 258, 3402-3408.
44. Kunkel, T.A., Roberts, J.D. and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol., 154, 367-382.
45. London, I.M., Levin, D.H., Matts, R.L., Thomas, N.S.B., Petryshyn, R. and Chen, J.-J. (1987) Regulation of protein synthesis. Enzymes. 18, 359-380.
46. Lucchini, G., Hinnebusch, A.G., Chen, C. and Fink, G.R. (1984) Positive regulatory interactions of the HIS4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol., 4, 1326-1333.
47. Manchesler, K.L. (1987) Kinetic constants in the functioning of eIF-2 and eIF-2B. Biochem. Int., 15, 897-906.
48. i. Biochem. Int., 24, 475-484.
49. i complexes in protein synthesis. Biochem. Int., 20, 257-265.
50. Marton, M.J., Crouch, D. and Hinnebusch, A.G. (1993) GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2. Mol. Cell Biol., 13, 3541-3556.
51. Merrick, W.C. (1992) Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev., 56, 291-315.
52. Mueller, P.P., Harashima, S. and Hinnebusch, A.G. (1987) A segment of GCN4 mRNA containing the upstream AUG codons confers translational control upon a heterologous yeast transcript. Proc. Natl Acad Sci. USA, 84, 2863-2867.
53. Phe, EF-Tu, and a GTP analog. Science, 270, 1464-1472.
54. 2+ and guanine nucleotide exchange factor on the binding of guanine nucleotides to eukaryotic initiation factor 2. J. Biol. Chem., 263, 5519-5525.
55. Pathak, V.K., Nielsen, P.J., Trachsel, H. and Hershey, J.W.B. (1988) Structure of the β subunit of translational initiation factor eIF-2. Cell, 54, 633-639.
56. Price, N. and Proud, C. (1994) The guanine nucleotide-exchange factor, eIF-2B. Biochimie, 76, 748-760.
57. Rajbhandary, U.L. and Ghosh, H.P. (1969) Studies on polynucleotides. XCI. Yeast methionine transfer ribonucleic acid: purification, properties, and terminal nucleotide sequences. J. Biol. Chem., 244, 1104-1113.
58. Rhoads, R.E. (1993) Regulation of eukaryotic protein synthesis by initiation factors. J. Biol. Chem., 268, 3017-3020.
59. Romero, G., Chau, V. and Biltonen, R.L. (1985) Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides. and aminoacyl-tRNA. J. Biol. Chem., 260, 6167-6174.
60. Rose, M.D. and Broach, J.R. (1991) Cloning genes by complementation in yeast. Methods Enzymol., 191, 195-230.
61. Rowlands, A.G., Panniers, R. and Henshaw, E.C. (1988) The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem., 263, 5526-5533.
62. Salimans, M., Goumans, H., Amesz, H., Benne, R. and Voorma, H.O. (1984) Regulation of protein synthesis in eukaryotes. Mode of action of eRF, an eIF-2-recycling factor from rabbit reticulocytes involved in GDP/ GTP exchange. Eur. J. Biochem., 145, 91-98.
63. Sherman, E, Fink, G.R. and Lawrence, C.W. (1979) Methods in Yeast Genetics. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY.
64. Siekierka, J., Mauser, L. and Ochoa, S. (1982) Mechanism of polypeptide chain initiation in eukaryotes and its control by phosphorylation of the a subunit of initiation factor 2. Proc. Natl Acad. Sci. USA, 79, 2537-2540.
65. Sikorski, R.S. and Boeke, J.D. (1991) In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol., 191, 302-318.
66. Walton, G.M. and Gill, G.N. (1975) Nucleotide regulation of a eukaryotic protein synthesis initiation complex. Biochim. Biophys. Acta, 390, 231-245.
67. Yoon, H. and Donahue, T.F. (1992) Control of translation initiation in Saccharomyces cerevisiae. Mol. Microbiol., 6, 1413-1419.