Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2

EMBO Journal

Volumn 18, Issue 6, 1999, Pages 1673-1688

  Asano, Katsura ^a   Krishnamoorthy, Thanuja ^a   Phan, Lon ^a   Pavitt, Graham D ^b   Hinnebusch, Alan G ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

eIF2; Evolution of eIFs; GAP; GEF; Translation initiation complex

Indexed keywords

ACID PROTEIN; AROMATIC AMINO ACID; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; INITIATION FACTOR; INITIATION FACTOR 2; INITIATION FACTOR 3; INITIATION FACTOR 5; LYSINE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARCHAEBACTERIUM; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SEQUENCE HOMOLOGY; TRANSLATION INITIATION; YEAST;

AMINO ACID SEQUENCE; ANIMALS; CLONING, MOLECULAR; CONSERVED SEQUENCE; DROSOPHILA; EUKARYOTIC INITIATION FACTOR-2; EUKARYOTIC INITIATION FACTOR-2B; EUKARYOTIC INITIATION FACTOR-5; GTP-BINDING PROTEINS; GTPASE-ACTIVATING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; HUMANS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PEPTIDE CHAIN INITIATION, TRANSLATIONAL; PEPTIDE INITIATION FACTORS; PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; EUKARYOTA; LEPIDOPTERA;

EID: 0033559265     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (54)

1. Anderson, J., Phan, L., Cuesta, R., Carlson, B.A., Pak, M., Asano, K., Björk, G.R., Tamame, M. and Hinnebusch, A.G. (1998) The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev., 12, 3650-3662.
2. Asano, K., Vornlocher, H.-P., Richter-Cook, N.J., Merrick, W.C., Hinnelousch, A.G. and Hershey, J.W.B. (1997) Structure of cDNAs encoding human eIF3 subunits. J. Biol. Chem., 272, 27042-27052.
3. Asano, K., Phan, L., Anderson, J. and Hinnebusch, A.G. (1998) Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J. Biol. Chem., 273, 18573-18585.
4. Bartel, P.L., Chien, C.T., Stemglanz, R. and Fields, S. (1993) Using the two-hybrid system to detect protein-protein interactions. In Hartley, D.A. (ed.), Cellular Interactions in Development: A Practical Approach. Oxford University Press, Oxford, UK, pp. 153-179.
5. Boeke, J.D., Trueheart, J., Natsoulis, G. and Fink, G.R. (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genes. Methods Enzymol., 154, 164-175.
6. Bult, C.J. et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science, 273, 1058-1073.
7. Bushman, J.L., Asuru, A.I., Matts, R.L. and Hinnebusch, A.G. (1993a) 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.
8. Bushman, J.L., Foiani, M., Cigan, A.M., Paddon, C.J. and Hinnebusch, A.G. (1993b) Guanine nucleotide exchange factor for eIF-2 in yeast: genetic and biochemical analysis of interactions between essential subunits GCD2, GCD6 and GCD7 and regulatory subunit GCN3. Mol. Cell. Biol., 13, 4618-4631.
9. Chaudhuri, J., Das, K. and Maitra, U. (1994) Purification and characterization of bacterially expressed mammalian translation initiation factor 5 (eIF-5): demonstration that eIF-5 forms a specific complex with eIF-2. Biochemistry, 33, 4794-4799.
10. Met binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast. Science, 280, 1757-1760.
11. Christianson, T.W., Sikorski, R.S., Dante, M., Shero, J.H. and Hieter, P. (1992) Multifunctional yeast high-copy-number shuttle vectors. Gene, 110, 119-122.
12. Cigan, A.M., Foiani, M., Hannig, E.M. and Hinnebusch, A.G. (1991) Complex formation by positive and negative translational regulators of GCN4. Mol. Cell. Biol., 11, 3217-3228.
13. Clemens, M.J. (1996) Protein kinases that phosphorylate eIF2 and eIF2B, and their role in eukaryotic cell translational control. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds). Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. NY. pp. 139-172.
14. Danaie, P., Wittmer, B., Altmann, M. and Trachsel, H. (1995) Isolation of a protein complex containing translation initiation factor Prt1 from Saccharomyes cerevisiae. J. Biol. Chem., 270, 4288-4292.
15. Das, S., Maiti, T., Das , K. and Maitra, U. (1997) Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the β-subunit of eIF2. J. Biol. Chem., 272, 31712-31718.
16. Met ternary complexes. Mol. Cell. Biol., 15, 6351-6363.
17. Donahue, T.F., Cigan, A.M., Pabich, E.K. and Castilho-Valavicius, B. (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.
18. Feinberg, B., McLaughlin, C.S. and Moldave, K. (1982) Analysis of temperature-sensitive mutant ts187 of Saccharomyces cerevisiae altered in a component required for the initiation of protein synthesis. J. Biol. Chem., 257, 10846-10851.
19. Gietz, R.D. and Sugino, A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
20. Greenberg, J.R., Phan, L., Gu, Z., deSilva, A., Apolito, C., Sherman, F., Hinnebusch, A.G. and Goldfarb, D.S. (1998) Nip1 p associates with 40S ribosomes and the Prtlp subunit of eIF3 and is required for efficient translation initiation. J. Biol. Chem., 273, 23485-23494.
21. Hannig, E.M., Cigan, A.M., Freeman, B.A. and Kinzy, T.G. (1992) GCD11, a negative regulator of GCN4 expression, encodes the gamma subunit of eIF-2 in Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 506-520.
22. Hinnebusch, A.G. (1996) Translational control of GCN4: gene-specific regulation by phosphorylation of eIF2. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds). Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 199-244.
23. Hinnebusch, A.G. (1997) Translational regulation of yeast GCN4: a window on factors that control initiator-tRNA binding to the ribosome. J. Biol. Chem., 272, 21661-21664.
24. Huang, H., Yoon, H., Hannig, E M. and Donahue, T.F. (1997) GTP hydrolysis controls stringent selection of the AUG start codon during translation initiation in Saccharomyces cerevisiae. Genes Dev., 11, 2396-2413.
25. Imataka, H. and Sonenberg, N. (1997) Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell Biol. 17, 6940-6947.
26. Jones, E.W. (1991) Tackling the protease problem in Saccharomyces cerevisiae. Methods Enzymol., 194, 428-453.
27. Kasperaitis, M.A., Voorma, H.O. and Thomas, A.A. (1995) The amino acid sequence of eukaryotic translation initiation factor 1 and its similarity to yeast initiation factor SUI1. FEBS Lett., 365, 47-50.
28. Kawagishi-Kobayashi, M., Silverman, J.B., Ung, T.K. and Dever, T.E. (1997) Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2α. Mol. Cell. Biol., 17, 4146-4158.
29. Kimball, S.R., Heinzinger, N.K., Horetsky, R.L. and Jefferson, L.S. (1998) Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B. J. Biol. Chem., 273, 3039-3044.
30. Klenk, H.-P. et al. (1997) The complete genome sequence of the hyperthermophilic sulphate-reducing archaeon Archaeoglobus fulgidus. Nature, 390, 364-370.
31. Koonin, E.V. (1995) Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs. Protein Sci., 4, 1608-1617.
32. Kyrpides, N.C. and Woese, C.R. (1998) Universally conserved translation initiation factors. Proc: Natl Acad. Sci. USA, 95, 224-228.
33. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
34. Lamphear, B.J., Kirchweger, R., Skern, T. and Rhoads, R.E. (1995) Mapping of functional domains in eukaryotic protein synthesis initiation factor 4G (eIF4G) with picornaviral proteases. J. Biol. Chem., 270, 21975-21983.
35. Maiti, T. and Maitra, U. (1997) Characterization of translation initiation factor 5 (eIF5) from Saccharomyces cerevisiae. J. Biol. Chem. 272, 1833-18340.
36. Merrick, W.C. and Hershey, J.W.B. (1996) The pathway and mechanism of eukaryotic protein synthesis. In Hershey, J.W.B., Mathews, M.B. and Sonenherg, N. (eds). Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 31-69.
37. Naranda, T., MacMillan, S.E. and Hershey, J.W.B. (1994) Purified yeast translational initiation factor eIF-3 is an RNA-hinding protein complex that contains the PRT1 protein. J. Biol. Chem., 269, 32286-32292.
38. Naranda, T., MacMillan, S.E., Donahue, T.F. and Hershey, J.W.B. (1996) SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomcyes cerevisiae. Mol. Cell. Biol., 16, 2307-2313.
39. Pathak, V.K., Nielsen, P.J., Trachsel, H. and Hershey, J.W.B. (1988) Structure of β subunit of translational initiation factor eIF-2. Cell. 54, 633-639.
40. Pavitt, G.D., Yang, W. and Hinnebusch, A.G. (1997) Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2. Mol. Cell. Biol., 17, 1298-1313.
41. Pavitt, G.D., Ramaiah, K.V.A., Kimball, S.R. and Hinnebusch, A.G. (1998) eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange. Genes Dev., 12, 514-526.
42. Pestova, T.V., Borukhov, S.I. and Hellen, C.U.T. (1998) Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature, 394, 854-859.
43. Phan, L., Zhang, X., Asano, K., Anderson, J., Vornlocher, H.P., Greenberg, J.R., Qin, J. and Hinnebusch, A.G. (1998) Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol. Cell. Biol., 18, 4935-4946.
44. Qiu, H., Garcia-Barrio, M.T. and Hinnebusch, A.G. (1998) Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain. Mol. Cell. Biol., 18, 2697-2711.
45. Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
46. Smith, D.B. and Johnson, K.S. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene, 67, 31-40.
47. Smith, D.R. et al. (1997) Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics. J. Bacteriol., 179, 7135-7155.
48. Sonenberg, N. (1996) mRNA 5′ cap-binding protein eIF4E and control of cell growth. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds). Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 245-269.
49. Tabor, S. and Richardson, C.C. (1987) DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl Acad. Sci. USA, 84, 4767-4771.
50. Trachsel, H. (1996) Binding of initiator methionyl-tRNA to ribosomes. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds), Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. pp. 113-138.
51. Verlhac, M.-H., Chen, R.-H., Hanachi, P., Hershey, J.W.B. and Derynck, R. (1997) Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. EMBO J., 16, 6812-6822.
52. Voorma, H.O. (1996) Control of translation initiation in prokaryotes. In Hershey, J.W.B., Mathews, M.B. and Sonenberg, N. (eds). Translational Control. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 759-777.
53. Yang, W. and Hinnebusch, A.G. (1996) Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. Mol. Cell. Biol., 16, 6603-6616.
54. Met recognition of the start codon. Mol. Cell. Biol., 12, 248-260.