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Part of the book series: NATO Advanced Study Institutes Series ((NSSA,volume 41))

Abstract

Initiation of protein synthesis is the process whereby the ribosome binds mRNA and the first aminoacyl-tRNA to form an initiation complex which is capable of entering the elongation phase of protein synthesis. The pathway is complex and involves numerous steps: First, the 80S ribosome dissociates into 40S and 60S ribosomal subunits; the 40S subunit forms a preinitiation complex with methionyl-tRNA and mRNA; this is joined by the 60S subunit to complete formation of the 80S initiation complex. During these steps, two critical events occur: the ribosome selects for translation a specific mRNA from among numerous species of mRNAs; and the methionyl-tRNA interacts with a specific initiator site on the mRNA to assure proper translation in the correct phase. The reactions are promoted or catalyzed by a complex array of initiation factors and involve the hydrolysis of ATP and GTP.

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References

  1. Schreier, M.H., Erni, B., and Staehelin, T. (1977), J. Mol. Biol, 116, 727–753.

    Article  PubMed  CAS  Google Scholar 

  2. Merrick, W.C. (1979), Methods Enzymol. 60, 101–148.

    Article  PubMed  CAS  Google Scholar 

  3. Benne, R., Brown-Luedi, M.L., and Hershey, J.W.B. (1979), Methods Enzymol. 60, 15–35.

    Article  PubMed  CAS  Google Scholar 

  4. Voorma, H.O., Thomas, A., Goumans, H., Amesz, H., and van der Mast, C. (1979), Methods Enzymol. 60, 124–135.

    Article  PubMed  CAS  Google Scholar 

  5. Merrick, W.C. (1979), Methods Enzymol. 60, 108–123.

    Article  PubMed  CAS  Google Scholar 

  6. Dasgupta, A., Das, A., Roy, R., Ralston, R., Majumdar, A., and Gupta, N.K. (1978), J. Biol. Chem. 253, 6054–6059.

    PubMed  CAS  Google Scholar 

  7. Das, A., and Gupta, N.K. (1977), Biochem. Biophys. Res. Commun. 71, 1307–1316.

    Article  Google Scholar 

  8. deHaro, C., Datta, A., and Ochoa, S. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 243–247.

    Article  CAS  Google Scholar 

  9. Sonenberg, N., Morgan, M.A., Merrick, W.C., and Shatkin, A.J. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 4843–4847.

    Article  CAS  Google Scholar 

  10. Merrick, W.C., and Anderson, W.F. (1975), J. Biol. Chem. 250, 1197–1206.

    PubMed  CAS  Google Scholar 

  11. Erni, B. (1976), Thesis, Swiss Federal Institute of Technology, Zurich.

    Google Scholar 

  12. Benne, R., and Hershey, J.W.B. (1978), J. Biol. Chem. 253, 3078–3087.

    PubMed  CAS  Google Scholar 

  13. Staehelin, T., Trachsel, H., Erni, B., Boschetti, A., and Schreier, M.H. (1975), Proc. FEBS Meeting, 10th, 39, 309–323.

    CAS  Google Scholar 

  14. Henderson, A.B., Miller, A.H., and Hardest)(y, B. (1979), Proc. Natl. Acad. Sci. U.S.A. 76, 2605–2609.

    Article  CAS  Google Scholar 

  15. Petersen, N., and McLaughlin, C.S. (1974), Molec. gen. Genet. 129, 189–200.

    Article  PubMed  CAS  Google Scholar 

  16. Gasior, E., Herrera, F., Sadnik, I., McLaughlin, C.S., and Moldave, K. (1979), J. Biol. Chem. 254, 3965–3969.

    PubMed  CAS  Google Scholar 

  17. Ghosh-Dost ider, P., Yaghmai, B., Das, A., Das, H.K., and Gupta, N.K. (1980), J. Biol. Chem. 255, 365–368.

    Google Scholar 

  18. Safer, B., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9067–9075.

    PubMed  CAS  Google Scholar 

  19. Lloyd, M.A., Osborne, J.C., Safer, B., Powell, G., and Merrick, W.C. (1980), J. Biol. Chem. 255., 1189–1191.

    Google Scholar 

  20. Kemper, W.M., Berry, K.W., and Merrick, W.C. (1976), J. Biol. Chem. 251, 5551–5557.

    PubMed  CAS  Google Scholar 

  21. Merrick, W.C., Kemper, W.M., and Anderson, W.F. (1975), J. Biol. Chem. 250, 5556–5562.

    PubMed  CAS  Google Scholar 

  22. Waldman, A.A., Marx, G., and Goldstein, J. (1975), Proc. Natl. Acad. Sci. U.S.A. 72, 2352–2356.

    Article  CAS  Google Scholar 

  23. Van der Mast, C., Thomas, A., Goumans, H., Amesz, H., and Voorma H.O., (1977), Eur. J. Biochem. 75, 455–464.

    Article  PubMed  Google Scholar 

  24. Kaempfer, R. (1971), Methods Enzymol. 60, 247–255.

    Article  Google Scholar 

  25. Moretti, S., Staehelin, T., Trachsel, H., and Gordon, J. (1979), Eur. J. Biochem. 97 609–614.

    Article  PubMed  CAS  Google Scholar 

  26. Cleveland, D.W., Fischer, S.G., Kirschner, M.W., and Laemmli U.K (1976), J. Biol. Chem. 252, 1102–1106.

    Google Scholar 

  27. Weber, K., and Osborn, M. (1969), J. Biol. Chem. 244, 4406–4412.

    PubMed  CAS  Google Scholar 

  28. Benne, R., Edman, J., Traut, R.R., and Hershey, J.W.B. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 108–112.

    Article  CAS  Google Scholar 

  29. Tahara, S.M., Traugh, J.A., Sharp, S.B., Lundak, T.S., Safer, B. and Merrick, W.C. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 789–793.

    Article  CAS  Google Scholar 

  30. Laemmli, U.K. (1970), Nature, London, 227, 680–685.

    Article  CAS  Google Scholar 

  31. Harbitz, I., and Hauge, J.G. (1979), Methods Enzymol. 60, 240–246

    Article  PubMed  CAS  Google Scholar 

  32. Stringer, E.A., Chaudhuri, A., Valenzuela, D., and Maitra, U. (1980), Proc. Natl. Acad. Sci. U.S.A. 77; 3356–3359.

    Article  CAS  Google Scholar 

  33. Barrieux, A., and Rosenfeld, M.G. (1977), J. Biol. Chem. 252, 3813–3847.

    Google Scholar 

  34. Benne, R., and Hershey, J.W.B. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 3005–3009.

    Article  CAS  Google Scholar 

  35. Safer, B., Adams, S.L., Kemper, W.M., Berry, K.W., Lloyd, M., and Merrick, W.C. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 2584–2588.

    Article  CAS  Google Scholar 

  36. Meyer, L.J. (1980), Thesis, University of California, Davis.

    Google Scholar 

  37. Trachsel, H., Erni, B., Schreier, M.H., Braun, L., and Staehelin, T. (1979), Biochim. Biophys. Acta 561, 484–490.

    Article  CAS  Google Scholar 

  38. Traugh, J.A., Tahara,-S.M., Sharp, S.B., Safer, B., and Merrick, W.C. (1976), Nature, London, 263, 163–165.

    Article  CAS  Google Scholar 

  39. Issinger, O.-G., Benne, R., Hershey, J.W.B., and Traut, R.R. (1976), J. Biol. Chem. 251, 61471–61473.

    Google Scholar 

  40. Mumby, M., and Traugh, J.A. (1979), Methods Enzymol. 60, 522–534.

    Article  PubMed  CAS  Google Scholar 

  41. Traugh, J.A., and Sharp, S.B. (1979), Methods Enzymol. 40, 534–541.

    Article  Google Scholar 

  42. Safer, B., Kemper, W., and Jagus, R. (1979), J. Biol. Chem. 254, 8091–8091.

    PubMed  CAS  Google Scholar 

  43. Meyer, L., and Hershey, J.W.B., manuscript in preparation.

    Google Scholar 

  44. Howe, J.G., Yanov, J., Meyer, L., Johnston, K., and Hershey, J.W.B. (1978), Arch. Biochem. Biophys. 191, 813–820.

    Article  PubMed  CAS  Google Scholar 

  45. Trachsel, H., Erni, B., Schreier, M.H., and Staehelin, T. (1977), J. Mol. Biol. 116, 755–767.

    Article  PubMed  CAS  Google Scholar 

  46. Safer, B., and Anderson, W.F. (1978), Crit. Rev. Biochem. 5., 261–290.

    Google Scholar 

  47. Kaempfer, R. (1970), In Ribosomes (Nomura, M., Tissieres, A., and Lengyel, P., ed.) pp. 679–704, Cold Spring Harbor Laboratory, New York.

    Google Scholar 

  48. Thompson, H.A., Sadnik, I., Scheinbuks, J., and Moldave, K. (1977) Biochemistry 16, 2221–2230.

    Article  PubMed  CAS  Google Scholar 

  49. Emanuilov, I., Sabatini, D.D., Lake, J.A., and Freienstein, C. (1978), Proc. Natl. Acad. Sei. U.S.A. 75, 1389–1393.

    Article  CAS  Google Scholar 

  50. Thomas, A., Goumans, H., Voorma, H.O., and Benne, R. (1980), Eur. J. Biochem. 107, 39–46.

    Article  PubMed  CAS  Google Scholar 

  51. Russell, D.W., and Spremulli, L.L. (1980), Arch. Biochem. Biophys. 201, 518–526.

    Article  PubMed  CAS  Google Scholar 

  52. Levin, D.H., and Kyner, D. (1971), Fed. Proc. 30, 1289.

    Google Scholar 

  53. Chen, Y.C., Woodley, C.L., Bose, K.K., and Gupta, N.K. (1972), Biochem. Biophys. Res. Commun. 48, 1–9.

    Article  CAS  Google Scholar 

  54. Dettman, G.L., and Stanley, W.M. (1972), Biochim. Biophys. Acta 287, 124–133.

    Article  CAS  Google Scholar 

  55. Safer, B., Adams, S.L., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9076–9082.

    PubMed  CAS  Google Scholar 

  56. Walton, G.M., Gill, G.N. (1976), Biochim. Biophys. Acta 418, 195–203.

    Article  CAS  Google Scholar 

  57. Benne, R., Amesz, H., Hershey, J.W.B., and Voorma, H.O. (1979), J. Biol. Chem. 254, 3201–3205.

    PubMed  CAS  Google Scholar 

  58. Benne, R., Wong, C., Luedi, M., and Hershey, J.W.B. (1976), J. Biol. Chem. 251, 7675–7681.

    Google Scholar 

  59. Peterson, D., Merrick, W.C., and Safer, B. (1979), J. Biol. Chem. 254, 2509–2516.

    PubMed  CAS  Google Scholar 

  60. Hirsch, C.A., Cox, M.A., van Venrooij, W.J.W., and Henshaw, E.C. (1973), J. Biol. Chem. 248, 4377–4385.

    PubMed  CAS  Google Scholar 

  61. Kozak, M. (1978), Cell 15, 1109–1123.

    Article  PubMed  CAS  Google Scholar 

  62. Shafritz, D.A., Weinetein, J.A., Safer, B., Merrick, W.C., Weber, L.A., Hickey, E.D., and Baglioni, C. (1976), Nature, London, 261, 291–294.

    Article  CAS  Google Scholar 

  63. Brown-Luedi, M.L., Benne, R., Yau, P., and Hershey, J.W.B. (1978) Fed. Proc. 37, 1307.

    Google Scholar 

  64. Peterson, D.T., Safer, B., and Merrick, W.C. (1979), J. Biol. Chem. 25, 7730–7735.

    Google Scholar 

  65. Staehelin, T., Erni, B., and Schreier, M.H. (1979), Methods Enzymol. 60, 136–165.

    Article  PubMed  CAS  Google Scholar 

  66. Wigle, D.T., and Smith, A.E. (1973), Nature, London, New Biol. 229 136–140.

    Google Scholar 

  67. Golini, F., Thach, S.S., Birge, C.H., Safer, B., Merrick, W.O., and Thach, R.E. (1976), Proc. Natl. Acad. Sei. U.S.A. 73, 3040–3044.

    Article  CAS  Google Scholar 

  68. Kabat, D., and Chappell, M.R. (1977), J. Biol. Chem. 252, 2681–2690.

    Google Scholar 

  69. Heywood, S.M., and Kennedy, D.S. (1979), Arch. Biochem. Biophys. 192, 270–281.

    Article  PubMed  CAS  Google Scholar 

  70. Gette, W.R., and Heywood, S.M. (1979), J. Biol. Chem. 254, 9879–9885.

    PubMed  CAS  Google Scholar 

  71. Heywood, S.M., Kennedy, D.S., and Bester, A.J. (1979), Methods Enzymol. 60, 5141–5149.

    Google Scholar 

  72. Pluskal, M.G., and Mukherjie, A. (1980), Fed. Proc. 39, 1868.

    Google Scholar 

  73. Bergmann, J.E., and Lodish, H.F. (1979), J. Biol. Chem. 254, 11927–11937.

    PubMed  CAS  Google Scholar 

  74. Lutsch, G., Bielka, H., Wahn, K., and Stahl, J. (1972), Acta Biol. Med. Ger. 29, 851–876.

    PubMed  CAS  Google Scholar 

  75. Lake, J.A., Sabatini, D.D., and Nomura, Y. (1970), In Ribosomes (Nomura, M., Tissieres, A., and Lengyel, P., ed.), pp. 543–557, Cold Spring Harbor Laboratory, New York.

    Google Scholar 

  76. Westermann, P., Heumann, W., Bommer, U.A., Bielka, H., Nygard, O. and Hultin, T. (1979), FEBS Letts. 97, 101–104.

    Article  CAS  Google Scholar 

  77. Tolan, D., Hershey, J.W.B., and Traut, R.R., manuscript in preparation.

    Google Scholar 

  78. Svoboda, A.J., and McConkey, E.H. (1979), Biochem. Biophys. Res. Commun. 81, 1145–1152.

    Article  Google Scholar 

  79. Jagus, R., Anderson, W.F., and Safer, B. (1980), Prog. Nucl. Acids Res. Mol. Biol., in press.

    Google Scholar 

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Hershey, J.W.B. (1982). The Initiation Factors. In: Pérez-Bercoff, R. (eds) Protein Biosynthesis in Eukaryotes. NATO Advanced Study Institutes Series, vol 41. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4124-6_3

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  • DOI: https://doi.org/10.1007/978-1-4684-4124-6_3

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