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The Initiation Factors

  • John W. B. Hershey
Part of the NATO Advanced Study Institutes Series book 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.

Keywords

Ternary Complex Initiation Factor Ribosomal Subunit Sucrose Density Gradient Centrifugation mRNA Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Schreier, M.H., Erni, B., and Staehelin, T. (1977), J. Mol. Biol, 116, 727–753.PubMedCrossRefGoogle Scholar
  2. 2.
    Merrick, W.C. (1979), Methods Enzymol. 60, 101–148.PubMedCrossRefGoogle Scholar
  3. 3.
    Benne, R., Brown-Luedi, M.L., and Hershey, J.W.B. (1979), Methods Enzymol. 60, 15–35.PubMedCrossRefGoogle Scholar
  4. 4.
    Voorma, H.O., Thomas, A., Goumans, H., Amesz, H., and van der Mast, C. (1979), Methods Enzymol. 60, 124–135.PubMedCrossRefGoogle Scholar
  5. 5.
    Merrick, W.C. (1979), Methods Enzymol. 60, 108–123.PubMedCrossRefGoogle Scholar
  6. 6.
    Dasgupta, A., Das, A., Roy, R., Ralston, R., Majumdar, A., and Gupta, N.K. (1978), J. Biol. Chem. 253, 6054–6059.PubMedGoogle Scholar
  7. 7.
    Das, A., and Gupta, N.K. (1977), Biochem. Biophys. Res. Commun. 71, 1307–1316.CrossRefGoogle Scholar
  8. 8.
    deHaro, C., Datta, A., and Ochoa, S. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 243–247.CrossRefGoogle Scholar
  9. 9.
    Sonenberg, N., Morgan, M.A., Merrick, W.C., and Shatkin, A.J. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 4843–4847.CrossRefGoogle Scholar
  10. 10.
    Merrick, W.C., and Anderson, W.F. (1975), J. Biol. Chem. 250, 1197–1206.PubMedGoogle Scholar
  11. 11.
    Erni, B. (1976), Thesis, Swiss Federal Institute of Technology, Zurich.Google Scholar
  12. 12.
    Benne, R., and Hershey, J.W.B. (1978), J. Biol. Chem. 253, 3078–3087.PubMedGoogle Scholar
  13. 13.
    Staehelin, T., Trachsel, H., Erni, B., Boschetti, A., and Schreier, M.H. (1975), Proc. FEBS Meeting, 10th, 39, 309–323.Google Scholar
  14. 14.
    Henderson, A.B., Miller, A.H., and Hardest)(y, B. (1979), Proc. Natl. Acad. Sci. U.S.A. 76, 2605–2609.CrossRefGoogle Scholar
  15. 15.
    Petersen, N., and McLaughlin, C.S. (1974), Molec. gen. Genet. 129, 189–200.PubMedCrossRefGoogle Scholar
  16. 16.
    Gasior, E., Herrera, F., Sadnik, I., McLaughlin, C.S., and Moldave, K. (1979), J. Biol. Chem. 254, 3965–3969.PubMedGoogle Scholar
  17. 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. 18.
    Safer, B., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9067–9075.PubMedGoogle Scholar
  19. 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. 20.
    Kemper, W.M., Berry, K.W., and Merrick, W.C. (1976), J. Biol. Chem. 251, 5551–5557.PubMedGoogle Scholar
  21. 21.
    Merrick, W.C., Kemper, W.M., and Anderson, W.F. (1975), J. Biol. Chem. 250, 5556–5562.PubMedGoogle Scholar
  22. 22.
    Waldman, A.A., Marx, G., and Goldstein, J. (1975), Proc. Natl. Acad. Sci. U.S.A. 72, 2352–2356.CrossRefGoogle Scholar
  23. 23.
    Van der Mast, C., Thomas, A., Goumans, H., Amesz, H., and Voorma H.O., (1977), Eur. J. Biochem. 75, 455–464.PubMedCrossRefGoogle Scholar
  24. 24.
    Kaempfer, R. (1971), Methods Enzymol. 60, 247–255.CrossRefGoogle Scholar
  25. 25.
    Moretti, S., Staehelin, T., Trachsel, H., and Gordon, J. (1979), Eur. J. Biochem. 97 609–614.PubMedCrossRefGoogle Scholar
  26. 26.
    Cleveland, D.W., Fischer, S.G., Kirschner, M.W., and Laemmli U.K (1976), J. Biol. Chem. 252, 1102–1106.Google Scholar
  27. 27.
    Weber, K., and Osborn, M. (1969), J. Biol. Chem. 244, 4406–4412.PubMedGoogle Scholar
  28. 28.
    Benne, R., Edman, J., Traut, R.R., and Hershey, J.W.B. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 108–112.CrossRefGoogle Scholar
  29. 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.CrossRefGoogle Scholar
  30. 30.
    Laemmli, U.K. (1970), Nature, London, 227, 680–685.CrossRefGoogle Scholar
  31. 31.
    Harbitz, I., and Hauge, J.G. (1979), Methods Enzymol. 60, 240–246PubMedCrossRefGoogle Scholar
  32. 32.
    Stringer, E.A., Chaudhuri, A., Valenzuela, D., and Maitra, U. (1980), Proc. Natl. Acad. Sci. U.S.A. 77; 3356–3359.CrossRefGoogle Scholar
  33. 33.
    Barrieux, A., and Rosenfeld, M.G. (1977), J. Biol. Chem. 252, 3813–3847.Google Scholar
  34. 34.
    Benne, R., and Hershey, J.W.B. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 3005–3009.CrossRefGoogle Scholar
  35. 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.CrossRefGoogle Scholar
  36. 36.
    Meyer, L.J. (1980), Thesis, University of California, Davis.Google Scholar
  37. 37.
    Trachsel, H., Erni, B., Schreier, M.H., Braun, L., and Staehelin, T. (1979), Biochim. Biophys. Acta 561, 484–490.CrossRefGoogle Scholar
  38. 38.
    Traugh, J.A., Tahara,-S.M., Sharp, S.B., Safer, B., and Merrick, W.C. (1976), Nature, London, 263, 163–165.CrossRefGoogle Scholar
  39. 39.
    Issinger, O.-G., Benne, R., Hershey, J.W.B., and Traut, R.R. (1976), J. Biol. Chem. 251, 61471–61473.Google Scholar
  40. 4O.
    Mumby, M., and Traugh, J.A. (1979), Methods Enzymol. 60, 522–534.PubMedCrossRefGoogle Scholar
  41. 41.
    Traugh, J.A., and Sharp, S.B. (1979), Methods Enzymol. 40, 534–541.CrossRefGoogle Scholar
  42. 42.
    Safer, B., Kemper, W., and Jagus, R. (1979), J. Biol. Chem. 254, 8091–8091.PubMedGoogle Scholar
  43. 43.
    Meyer, L., and Hershey, J.W.B., manuscript in preparation.Google Scholar
  44. 44.
    Howe, J.G., Yanov, J., Meyer, L., Johnston, K., and Hershey, J.W.B. (1978), Arch. Biochem. Biophys. 191, 813–820.PubMedCrossRefGoogle Scholar
  45. 45.
    Trachsel, H., Erni, B., Schreier, M.H., and Staehelin, T. (1977), J. Mol. Biol. 116, 755–767.PubMedCrossRefGoogle Scholar
  46. 46.
    Safer, B., and Anderson, W.F. (1978), Crit. Rev. Biochem. 5., 261–290.Google Scholar
  47. 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. 48.
    Thompson, H.A., Sadnik, I., Scheinbuks, J., and Moldave, K. (1977) Biochemistry 16, 2221–2230.PubMedCrossRefGoogle Scholar
  49. 49.
    Emanuilov, I., Sabatini, D.D., Lake, J.A., and Freienstein, C. (1978), Proc. Natl. Acad. Sei. U.S.A. 75, 1389–1393.CrossRefGoogle Scholar
  50. 50.
    Thomas, A., Goumans, H., Voorma, H.O., and Benne, R. (1980), Eur. J. Biochem. 107, 39–46.PubMedCrossRefGoogle Scholar
  51. 51.
    Russell, D.W., and Spremulli, L.L. (1980), Arch. Biochem. Biophys. 201, 518–526.PubMedCrossRefGoogle Scholar
  52. 52.
    Levin, D.H., and Kyner, D. (1971), Fed. Proc. 30, 1289.Google Scholar
  53. 53.
    Chen, Y.C., Woodley, C.L., Bose, K.K., and Gupta, N.K. (1972), Biochem. Biophys. Res. Commun. 48, 1–9.CrossRefGoogle Scholar
  54. 54.
    Dettman, G.L., and Stanley, W.M. (1972), Biochim. Biophys. Acta 287, 124–133.CrossRefGoogle Scholar
  55. 55.
    Safer, B., Adams, S.L., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9076–9082.PubMedGoogle Scholar
  56. 56.
    Walton, G.M., Gill, G.N. (1976), Biochim. Biophys. Acta 418, 195–203.CrossRefGoogle Scholar
  57. 57.
    Benne, R., Amesz, H., Hershey, J.W.B., and Voorma, H.O. (1979), J. Biol. Chem. 254, 3201–3205.PubMedGoogle Scholar
  58. 58.
    Benne, R., Wong, C., Luedi, M., and Hershey, J.W.B. (1976), J. Biol. Chem. 251, 7675–7681.Google Scholar
  59. 59.
    Peterson, D., Merrick, W.C., and Safer, B. (1979), J. Biol. Chem. 254, 2509–2516.PubMedGoogle Scholar
  60. 60.
    Hirsch, C.A., Cox, M.A., van Venrooij, W.J.W., and Henshaw, E.C. (1973), J. Biol. Chem. 248, 4377–4385.PubMedGoogle Scholar
  61. 61.
    Kozak, M. (1978), Cell 15, 1109–1123.PubMedCrossRefGoogle Scholar
  62. 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.CrossRefGoogle Scholar
  63. 63.
    Brown-Luedi, M.L., Benne, R., Yau, P., and Hershey, J.W.B. (1978) Fed. Proc. 37, 1307.Google Scholar
  64. 64.
    Peterson, D.T., Safer, B., and Merrick, W.C. (1979), J. Biol. Chem. 25, 7730–7735.Google Scholar
  65. 65.
    Staehelin, T., Erni, B., and Schreier, M.H. (1979), Methods Enzymol. 60, 136–165.PubMedCrossRefGoogle Scholar
  66. 66.
    Wigle, D.T., and Smith, A.E. (1973), Nature, London, New Biol. 229 136–140.Google Scholar
  67. 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.CrossRefGoogle Scholar
  68. 68.
    Kabat, D., and Chappell, M.R. (1977), J. Biol. Chem. 252, 2681–2690.Google Scholar
  69. 69.
    Heywood, S.M., and Kennedy, D.S. (1979), Arch. Biochem. Biophys. 192, 270–281.PubMedCrossRefGoogle Scholar
  70. 70.
    Gette, W.R., and Heywood, S.M. (1979), J. Biol. Chem. 254, 9879–9885.PubMedGoogle Scholar
  71. 71.
    Heywood, S.M., Kennedy, D.S., and Bester, A.J. (1979), Methods Enzymol. 60, 5141–5149.Google Scholar
  72. 72.
    Pluskal, M.G., and Mukherjie, A. (1980), Fed. Proc. 39, 1868.Google Scholar
  73. 73.
    Bergmann, J.E., and Lodish, H.F. (1979), J. Biol. Chem. 254, 11927–11937.PubMedGoogle Scholar
  74. 74.
    Lutsch, G., Bielka, H., Wahn, K., and Stahl, J. (1972), Acta Biol. Med. Ger. 29, 851–876.PubMedGoogle Scholar
  75. 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. 76.
    Westermann, P., Heumann, W., Bommer, U.A., Bielka, H., Nygard, O. and Hultin, T. (1979), FEBS Letts. 97, 101–104.CrossRefGoogle Scholar
  77. 77.
    Tolan, D., Hershey, J.W.B., and Traut, R.R., manuscript in preparation.Google Scholar
  78. 78.
    Svoboda, A.J., and McConkey, E.H. (1979), Biochem. Biophys. Res. Commun. 81, 1145–1152.CrossRefGoogle Scholar
  79. 79.
    Jagus, R., Anderson, W.F., and Safer, B. (1980), Prog. Nucl. Acids Res. Mol. Biol., in press.Google Scholar

Copyright information

© Plenum Press, New York 1982

Authors and Affiliations

  • John W. B. Hershey
    • 1
  1. 1.Department of Biological Chemistry, School of MedicineUniversity of CaliforniaDavisUSA

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