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
Schreier, M.H., Erni, B., and Staehelin, T. (1977), J. Mol. Biol, 116, 727–753.
Merrick, W.C. (1979), Methods Enzymol. 60, 101–148.
Benne, R., Brown-Luedi, M.L., and Hershey, J.W.B. (1979), Methods Enzymol. 60, 15–35.
Voorma, H.O., Thomas, A., Goumans, H., Amesz, H., and van der Mast, C. (1979), Methods Enzymol. 60, 124–135.
Merrick, W.C. (1979), Methods Enzymol. 60, 108–123.
Dasgupta, A., Das, A., Roy, R., Ralston, R., Majumdar, A., and Gupta, N.K. (1978), J. Biol. Chem. 253, 6054–6059.
Das, A., and Gupta, N.K. (1977), Biochem. Biophys. Res. Commun. 71, 1307–1316.
deHaro, C., Datta, A., and Ochoa, S. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 243–247.
Sonenberg, N., Morgan, M.A., Merrick, W.C., and Shatkin, A.J. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 4843–4847.
Merrick, W.C., and Anderson, W.F. (1975), J. Biol. Chem. 250, 1197–1206.
Erni, B. (1976), Thesis, Swiss Federal Institute of Technology, Zurich.
Benne, R., and Hershey, J.W.B. (1978), J. Biol. Chem. 253, 3078–3087.
Staehelin, T., Trachsel, H., Erni, B., Boschetti, A., and Schreier, M.H. (1975), Proc. FEBS Meeting, 10th, 39, 309–323.
Henderson, A.B., Miller, A.H., and Hardest)(y, B. (1979), Proc. Natl. Acad. Sci. U.S.A. 76, 2605–2609.
Petersen, N., and McLaughlin, C.S. (1974), Molec. gen. Genet. 129, 189–200.
Gasior, E., Herrera, F., Sadnik, I., McLaughlin, C.S., and Moldave, K. (1979), J. Biol. Chem. 254, 3965–3969.
Ghosh-Dost ider, P., Yaghmai, B., Das, A., Das, H.K., and Gupta, N.K. (1980), J. Biol. Chem. 255, 365–368.
Safer, B., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9067–9075.
Lloyd, M.A., Osborne, J.C., Safer, B., Powell, G., and Merrick, W.C. (1980), J. Biol. Chem. 255., 1189–1191.
Kemper, W.M., Berry, K.W., and Merrick, W.C. (1976), J. Biol. Chem. 251, 5551–5557.
Merrick, W.C., Kemper, W.M., and Anderson, W.F. (1975), J. Biol. Chem. 250, 5556–5562.
Waldman, A.A., Marx, G., and Goldstein, J. (1975), Proc. Natl. Acad. Sci. U.S.A. 72, 2352–2356.
Van der Mast, C., Thomas, A., Goumans, H., Amesz, H., and Voorma H.O., (1977), Eur. J. Biochem. 75, 455–464.
Kaempfer, R. (1971), Methods Enzymol. 60, 247–255.
Moretti, S., Staehelin, T., Trachsel, H., and Gordon, J. (1979), Eur. J. Biochem. 97 609–614.
Cleveland, D.W., Fischer, S.G., Kirschner, M.W., and Laemmli U.K (1976), J. Biol. Chem. 252, 1102–1106.
Weber, K., and Osborn, M. (1969), J. Biol. Chem. 244, 4406–4412.
Benne, R., Edman, J., Traut, R.R., and Hershey, J.W.B. (1978), Proc. Natl. Acad. Sci. U.S.A. 75, 108–112.
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.
Laemmli, U.K. (1970), Nature, London, 227, 680–685.
Harbitz, I., and Hauge, J.G. (1979), Methods Enzymol. 60, 240–246
Stringer, E.A., Chaudhuri, A., Valenzuela, D., and Maitra, U. (1980), Proc. Natl. Acad. Sci. U.S.A. 77; 3356–3359.
Barrieux, A., and Rosenfeld, M.G. (1977), J. Biol. Chem. 252, 3813–3847.
Benne, R., and Hershey, J.W.B. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 3005–3009.
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.
Meyer, L.J. (1980), Thesis, University of California, Davis.
Trachsel, H., Erni, B., Schreier, M.H., Braun, L., and Staehelin, T. (1979), Biochim. Biophys. Acta 561, 484–490.
Traugh, J.A., Tahara,-S.M., Sharp, S.B., Safer, B., and Merrick, W.C. (1976), Nature, London, 263, 163–165.
Issinger, O.-G., Benne, R., Hershey, J.W.B., and Traut, R.R. (1976), J. Biol. Chem. 251, 61471–61473.
Mumby, M., and Traugh, J.A. (1979), Methods Enzymol. 60, 522–534.
Traugh, J.A., and Sharp, S.B. (1979), Methods Enzymol. 40, 534–541.
Safer, B., Kemper, W., and Jagus, R. (1979), J. Biol. Chem. 254, 8091–8091.
Meyer, L., and Hershey, J.W.B., manuscript in preparation.
Howe, J.G., Yanov, J., Meyer, L., Johnston, K., and Hershey, J.W.B. (1978), Arch. Biochem. Biophys. 191, 813–820.
Trachsel, H., Erni, B., Schreier, M.H., and Staehelin, T. (1977), J. Mol. Biol. 116, 755–767.
Safer, B., and Anderson, W.F. (1978), Crit. Rev. Biochem. 5., 261–290.
Kaempfer, R. (1970), In Ribosomes (Nomura, M., Tissieres, A., and Lengyel, P., ed.) pp. 679–704, Cold Spring Harbor Laboratory, New York.
Thompson, H.A., Sadnik, I., Scheinbuks, J., and Moldave, K. (1977) Biochemistry 16, 2221–2230.
Emanuilov, I., Sabatini, D.D., Lake, J.A., and Freienstein, C. (1978), Proc. Natl. Acad. Sei. U.S.A. 75, 1389–1393.
Thomas, A., Goumans, H., Voorma, H.O., and Benne, R. (1980), Eur. J. Biochem. 107, 39–46.
Russell, D.W., and Spremulli, L.L. (1980), Arch. Biochem. Biophys. 201, 518–526.
Levin, D.H., and Kyner, D. (1971), Fed. Proc. 30, 1289.
Chen, Y.C., Woodley, C.L., Bose, K.K., and Gupta, N.K. (1972), Biochem. Biophys. Res. Commun. 48, 1–9.
Dettman, G.L., and Stanley, W.M. (1972), Biochim. Biophys. Acta 287, 124–133.
Safer, B., Adams, S.L., Anderson, W.F., and Merrick, W.C. (1975), J. Biol. Chem. 250, 9076–9082.
Walton, G.M., Gill, G.N. (1976), Biochim. Biophys. Acta 418, 195–203.
Benne, R., Amesz, H., Hershey, J.W.B., and Voorma, H.O. (1979), J. Biol. Chem. 254, 3201–3205.
Benne, R., Wong, C., Luedi, M., and Hershey, J.W.B. (1976), J. Biol. Chem. 251, 7675–7681.
Peterson, D., Merrick, W.C., and Safer, B. (1979), J. Biol. Chem. 254, 2509–2516.
Hirsch, C.A., Cox, M.A., van Venrooij, W.J.W., and Henshaw, E.C. (1973), J. Biol. Chem. 248, 4377–4385.
Kozak, M. (1978), Cell 15, 1109–1123.
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.
Brown-Luedi, M.L., Benne, R., Yau, P., and Hershey, J.W.B. (1978) Fed. Proc. 37, 1307.
Peterson, D.T., Safer, B., and Merrick, W.C. (1979), J. Biol. Chem. 25, 7730–7735.
Staehelin, T., Erni, B., and Schreier, M.H. (1979), Methods Enzymol. 60, 136–165.
Wigle, D.T., and Smith, A.E. (1973), Nature, London, New Biol. 229 136–140.
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.
Kabat, D., and Chappell, M.R. (1977), J. Biol. Chem. 252, 2681–2690.
Heywood, S.M., and Kennedy, D.S. (1979), Arch. Biochem. Biophys. 192, 270–281.
Gette, W.R., and Heywood, S.M. (1979), J. Biol. Chem. 254, 9879–9885.
Heywood, S.M., Kennedy, D.S., and Bester, A.J. (1979), Methods Enzymol. 60, 5141–5149.
Pluskal, M.G., and Mukherjie, A. (1980), Fed. Proc. 39, 1868.
Bergmann, J.E., and Lodish, H.F. (1979), J. Biol. Chem. 254, 11927–11937.
Lutsch, G., Bielka, H., Wahn, K., and Stahl, J. (1972), Acta Biol. Med. Ger. 29, 851–876.
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.
Westermann, P., Heumann, W., Bommer, U.A., Bielka, H., Nygard, O. and Hultin, T. (1979), FEBS Letts. 97, 101–104.
Tolan, D., Hershey, J.W.B., and Traut, R.R., manuscript in preparation.
Svoboda, A.J., and McConkey, E.H. (1979), Biochem. Biophys. Res. Commun. 81, 1145–1152.
Jagus, R., Anderson, W.F., and Safer, B. (1980), Prog. Nucl. Acids Res. Mol. Biol., in press.
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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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