Abstract
Eukaryotic mRNAs are generally monocistronic (1, 2). Ribosomes attach at or near the 5′-end of the mRNA, and translation is limited to the 5′-proximal cistron (3, see preceding chapter of this volume). By contrast, on prokaryotes ribosomes initiate protein synthesis on some mRNAs at multiple internal sites, resulting in polycistronic translation (4). Two kinds of mRNA structural features may account at least in part for this functional difference between the messages of higher and lower organisms. One is the 5′-terminal cap structure, m7G (5′)ppp(5′)N, which is unique to eukaryotic cellular and most viral mRNAs (5). A variety of experimental findings indicate that the presence of a cap promotes translation by facilitating stable binding of ribosomes (6, 7). Implied from these results is a recognition of the cap by putative cap binding proteins during initiation of protein synthesis. Messengers in bacteria apparently are not methylated or otherwise modified and nascent transcripts are read directly by a process of coupled transcription/translation (8). The mRNAs of prokaryotes include a purine-rich sequence, located ~10 nucleotide upstream from initiator triplets, that helps to stabilize initiation complexes by base-pairing with the 3′-terminal end of 16S ribosomal RNA (4, 9).
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References
Oberg, B.F. and Shatkin, A.J. (1972), Proc. Nat. Acad. Sci. U.S.A. 69, 3589–3593.
Glanville, N., Ranki, Mi, Morser, J., Kääriäinen, L. and Smith, A.E. (1976), Proc. Nat. Acad. Sci. U.S.A. 73, 3059–3063.
Kozak, M. (1978), Cell 15, 1109–1123.
Steitz, J.A. (1979) In Biological Regulation and Development, (Goldberger, R.F., ed.)Plenum Press, New York and London, pp. 349–399.
Shatkin, A.J. (1976), Cell 9, 645–653.
Filipowicz, W. (1978), FEBS Lett. 96, 1–11.
Banerjee, A.K. (1980), Microbiol. Revs. 44, 175-205.
Oxender, D.L., Zurawski, G. and Yanofsky, C. (1979), Proc. Nat. Acad. Sci. U.S.A. 76, 5521–5528.
Shine, J. and Dalgarno, L. (1974), Proc. Nat. Acad. Sci. U.S.A. 71, 1342–1346.
Hägenbuchle, O., Santer, M., Steitz, J.A. and Mans, R.J. (1978), Cell 13, 551–563.
Baralle, F.E. and Brownlee, G.G. (1978), Nature, London, 274, 84–87.
Both, G.W. (1979), FEBS Lett. 101, 220–224.
De Wächter, R. (1979), Nucleic Acids Res. 7, 2045–2054.
Ziff, E.B. and Evans, R.M. (1978), Cell 15, 1463–1475.
Schroeder, Jr., H.W., Liarakos, C.D., Gupta, R.C., Randerath, K. and Malley, B.W. (1979), Biochemistry 18, 5798–5808.
Rottman, F.M. (1978), In Biochemistry of Nucleic Acids II, (Clark, B.F.C., ed.) University Park Press, Baltimore Vol. 17, pp. 47–73.
Darnell, Jr., J.E. (1979), Prog. Nuc. Acid. Res. Mol. Biol. 22, 327–353.
Furuichi, Y., Muthukrishnan, S., Tomasz, J. and Shatkin, A.J. (1976), J. Biol. Chem. 251, 5043–5053.
Martin, S.A. and Moss, B. (1976), J. Biol. Chem., 251, 7313–7321.
Venkatesan, S. and Moss, B. (1980), J. Biol. Chem. 255, 2835–2842.
Venkatesan, S., Gershowitz, A. and Moss, B. (1980), J. Biol. Chem. 255, 903–908.
Both, G.W., Banerjee, A.K. and Shatkin, A.J. (1975), Proc. Nat. Acad. Sci. U.S.A. 72, 1189–1193.
Muthukrishnan, S., Both, G.W., Furuichi, Y. and Shatkin, A.J. (1975), Nature, London, 255, 33–37
Rose, J.K. and Lodish, H.F. (1976), Nature, London 262, 32–37.
Shimotohno, K., Kodama, Y., Hashimoto, J. and Miura, K.I. (1977), Proc. Nat. Acad. Sci. U.S.A. 74, 2734–2738.
Zan-Kcrwalczewska, M., Bretner, M., Sierakowaka, H., Szczesna, E. Filipowicz, Y. and Shatkin, A.J. (1977), Nucleic Acids Res. 4, 3065–3081.
Muthukrishnan, S., Morgan, M., Banerjee, A.K. and Shatkin, A.J. (1976), Biochemistry, 15, 5761–5768.
Weber, L.A., Hickey, E.D., Nuss, D.L. and Baglioni, C. (1977) Proc. Nat. Acad. Sci. U.S.A., 74, 3254–3258.
Held, W.A., West, K. and Gallagher, J.F. (1977) J-Biol. Chem. 252, 8489–8497.
Furuichi, Y., Lafiandra, A. and Shatkin, A.J. (1977) Nature, London, 266, 235–239.
Kaehler, M., Coward, J. and Hottman, F. (1977) Biochemistry 16, 5770–5775.
Dimock, K. and Stoltzfus, C.M. (1978), Biochemistry 17, 3627–3632.
Caboche, M. and La Bonnardiere, C. (1979) Virology, 93, 547–557.
Jacquemont, B. and Huppert, J. (1977) J. Virol. 22, 160–167.
Rose, J.K. (1975) J. Biol. Chem. 250, 8098–8104.
Both, G.W., Furuichi, Y., Muthukrishnan, S. and Shatkin, A.J. (1975) Cell 6, 185–195.
Both, G.W., Furuichi, Y., Muthukrishnan, S. and Shatkin, A.J. (1976), J. Mol. Biol. 104, 637–658.
Kozak, M. and Shatkin, A.J. (1976), J. Biol. Chem. 251, 4259–4266.
Roman, R.J.D., Booker, S.N. and Marcus, A. (1976), Nature, London, 260, 359–360.
Hickey, E.D., Weber, L.A. and Baglioni, C. (1976), Proc. Nat. Acad. Sci. U.S.A. 73, 19–23.
Canaani, D., Revel, M. and Groner, Y. (1976), FEBS Lett. 64, 326–331.
Adams, B.L., Morgan, M., Muthukrishnan, S., Hecht, S.M. and Shatkin, A.J. (1978), J. Biol. Chem. 253, 2589–2595.
Furuichi, Y., Morgan, M. and Shatkin, A.J. (1979) J. Biol. Chem. 251, 6732–6738.
Wimmer, E., Chang, A.Y., Clark, Jr., J.M. and Reichmann, M.E. (1968), J. Mol. Biol. 38, 59–73.
Seal, S.N., Schmidt, A., Tomas zewski, M. and Marcus, A. (1978), Biochem. Biophys. Res. Commun. 82, 553–559.
Bergmann, J.E. and Lodish, H.F. (1979) J. Biol. Chem. 254, 459–468.
Bergmann, J.E., Trachsel, H., Sonenberg, N., Shatkin, A.J. and Lodish, H.F. (1979) J. Biol. Chem. 1440–1443.
Filipowicz, W., Furuichi, Y., Sierra, J.M., Muthukrishnan, S., Shatkin, A.J. and Ochoa, S. (1976), Proc. Nat. Acad. Sci. U.S.A. 73, 1559–1563.
Kaempfer, R., Rosen, H. and Israeli, R. (1978), Proc. Nat. Acad. Sci. U.S.A. 15, 650–651.
Shafritz, D.A., Weinstein, J.A., Safer, B., Merrick, W.C., Weber, L.A., Hiekey, E.D. and Baglioni, C. (1976), Nature, London, 261, 291–294.
Sonenberg, N. and Shatkin, A.J. (1977), Proc. Nat. Acad. Sci. U.S.A. 74 4288–4292.
Sonenberg, N., Morgan, M.A., Testa, D., Colonno, R.J. and Shatkin, A.J. (1979), Nucleic Acids Res. 7, 15–29.
Sonenberg, N., Morgan, M.A., Merrick, W.C. and Shatkin, A.J. (1978), Proc. Nat. Acad. Sci. U.S.A. 75, 4843–4847.
Sonenberg, N., Trachsel, H., Hecht, S. and Shatkin, A.J. (1980), Nature, London, 285, 331–333.
Sonenberg, N., Rupprecht, K.M., Hecht, S.M. and Shatkin, A.J. (1979), Proc. Nat. Acad. Sci. U.S.A. 76, 4345–4349.
Kozak, M. (1980), Cell 19, 79–90.
Morgan, M.A. and Shatkin, A.J., Biochemistry, in press.
Kozak, M., Cell, in press.
Sonenberg, N., submitted.
Willems, M. and Penman, S. (1966), Virology 30, 355–367.
Ehrenfeld, E. and Lund, H. (1977), Virology 80, 297–308.
Fernandez-Munoz, R. and Darnell, J.E. (1976), J, Virol. 126, 719–726.
Rose, J.K., Trachsel, H., Leong, K. and Baltimore, D. (1978), Proc. Nat. Acad. Sci. U.S.A. 75, 2732–2736.
Skup, D. and Milliard, S. (1980), Proc. Nat. Acad. Sci. U.S.A. 77, 152–156.
Trachsel, H., Sonenberg, N., Shatkin, A.J., Rose, J.K., Leong, K., Bergman, J.E., Gordon, J. and Baltimore, D. (198O), Proc. Nat. Acad. Sci. U.S.A. 71, 770–774.
Shatkin, A.J., Darzynkiewicz, E., Nakashima, K., Sonenberg, N. and Tahara, S. (1980), Proceedings of Juselius Symposium, Helsinki, Finland, Academic Press, in press.
Isaacs, S.T., Shen, C.J., Hearst, J.E. and Rapoport, H. (1977), Biochemistry, 16, 1458–1464.
Cantor, C.R. (1980), Annals N.Y. Acad. Sci. 346, 379–385.
Nakashima, K., Lafiandra, A.J. and Shatkin, A.J. (1979), J. Biol. Chem. 254, 8007–8014.
Nakashima, K., Darzynkiewicz, E. and Shatkin, A.J., Nature, London, in press.
Krug, R.M., Broni, B.A., Lafiandra, A.J., Morgan, M.A. and Shatkin, A.J., Proc. Nat. Acad. Sci. U.S.A. in press.
Rose, J.K; (1978), Cell 14, 345–353.
Kozak, M. (1977), Nature, London, 269, 390–391.
Kozak, M. and Shatkin, A.J. (1979), Methods Ensymol. 60, 360–375.
Rabin, D. and Crothers, D.M. (1979), Nucleic Acids Res. 7, 689–703.
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Shatkin, A.J. (1982). A Closer Look at the 5′-End of mRNA in Relation to Initiation. 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_8
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