Abstract
In this and the accompanying paper we demonstrate that certain prokaryotic mRNAs, when modified at their 5′-termini with a cap structure, are translated in a eukaryotic cell-free protein synthesising system as efficiently as, or more efficiently than, eukaryotic mRNAs. Apparently, the prokaryotic mRNA contains all the information necessary for efficient recognition and initiation by eukaryotic translational components, except for the cap structure.
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References
Ro-Choi, T. S., Reddy, R., Choi, Y. C., Raj, N. B. & Henning, D. Fedn Proc. 33, 1548 (1974).
Shatkin, A. J. Cell 9, 645–653 (1976).
Cory, S. & Adam, J. M. J. molec. Biol. 99, 519–547 (1975).
Shatkin, A. J. & Both, G. W. Cell 7, 305–313 (1976).
Revel, M. & Groner, Y. Rev. Biochem. 47, 1079–1126 (1978).
Shih, D. S., Dasgupta, R. & Kaesberg, P. J. Virol. 19, 637–642 (1976).
Rose, J. K. & Lodish, H. F. Nature 262, 32–37 (1976).
Lodish, H. F. & Rose, J. K. J. biol. Chem. 252, 1181–1188 (1977).
Muthukrishnan, S., Morgan, M., Banerjee, A. K. & Shatkin, A. J. Biochemistry 15, 5761–5768 (1976).
Furuichi, Y., LaFiandra, A. & Shatkin, A. J. Nature 266, 235–239 (1977).
Kemper, B. Nature 262, 321–323 (1976).
Both, G. W., Furuichi, Y., Muthukrishnan, S. & Shatkin, A. J. J. molec. Biol. 104, 637–658 (1976).
Toneguzzo, F. & Ghosh, H. P. J. Virol. 17, 477–491 (1976).
Hickey, E. D., Weber, L. A. & Baglioni, C. Proc. natn. Acad. Sci. U.S.A. 73, 19–23 (1976).
Roman, R., Brooker, J. D., Seal, S. N. & Marcus, A. Nature 260, 359–360 (1976).
Filipowicz, W. et al. Proc. natn. Acad. Sci. U.S.A. 73, 1559–1563 (1976).
Shafritz, D. A. et al. Nature 261, 291–294 (1976).
Canaani, D., Revel, M. & Groner, Y. FEBS Lett. 64, 326–331 (1976).
Weber, L. A., Hickey, E. D., Nuss, D. L. & Baglioni, C. Proc. natn. Acad. Sci. U.S.A. 74, 3254–3258 (1977).
Weber, L. A., Hickey, E. D. & Baglioni, C. J. biol. Chem. 253, 178–183 (1978).
Anderson, C. W., Atkins, J. F. & Dunn, J. J. Proc. natn. Acad. Sci. U.S.A. 73, 2752–2756 (1976).
Aviv, H., Boime, I., Loyd, B. & Leder, P. Science 178, 1293–1295 (1972).
Wang, S., Marcu, K. B. & Inouye, M. Biochem. biophys. Res. Commun. 68, 1194–1200 (1976).
Davies, J. W. & Kaesberg, P. J. Virol. 12, 1434–1441 (1973).
Schreier, M. H., Staehelin, T., Gesteland, R. F. & Spahr, P. F. J. molec. Biol. 75, 575–578 (1973).
Morrison, T. G. & Lodish, H. F. Proc. natn. Acad. Sci. U.S.A. 70, 315–319 (1973).
Beck, O. E. & Gassen, H. G. Biochem. biophys. Res. Commun. 74, 16–24 (1977).
Rosenberg, M. & Paterson, B. M. Nature 279, 696–701 (1979).
Roberts, J. W. Nature 224, 1168–1174 (1969).
Roberts, J. W. Cold Spring Harb. Symp. quant. Biol. 35, 121–126 (1970).
Rosenberg, M., de Crombrugghe, B. & Weissman, S. J. biol. Chem. 250, 4755–4764 (1975).
Rosenberg, M., Court, D., Shimatake, H., Brady, C. & Wulff, D. Nature 272, 414–423 (1978).
Eisen, H. A. et al. Virology 30, 224–241 (1966).
Folkmanis, A., Takeda, Y., Simuth, J., Gussin, G. & Echols, H. Proc. natn. Acad. Sci. U.S.A. 73, 2249–2253 (1976).
Roberts, T. M., Shimatake, H., Brady, C. & Rosenberg, M. Nature 270, 274–275 (1977).
Hsiang, M. W., Cole, R. D., Takeda, Y. & Echols, H. Nature 270, 275–277 (1977).
Simon, M. N., Davis, R. W. & Davidson, N. The Bacteriophage Lambda (ed. Hershey, A. D.) 313–328 (Cold Spring Harbor Laboratory, New York, 1971).
Both, G. W., Banerjee, A. C. & Shatkin, A. J. Proc. natn. Acad. Sci. U.S.A. 72, 1189–1193 (1975).
Wei, C. M. & Moss, B. Proc. natn. Acad. Sci. U.S.A. 72, 318–323 (1975).
Moss, B. Biochem. biophys. Res. Commun. 74, 374–383 (1977).
Suzuki, H. FEBS Lett. 79, 11–14 (1977).
Dahlberg, J. E. & Blattner, F. R. Nucleic Acids Res. 2, 1441–1458 (1975).
Lozeron, H. A., Dahlberg, J. E. & Szybalski, W. Virology 71, 262–277 (1976).
Allet, B. & Solem, R. J. molec. Biol. 85, 475–484 (1974).
Reichardt, L. F. J. molec. Biol. 93, 267–288 (1975).
Paterson, B. & Bishop, J. O. Cell 12, 751–765 (1977).
Brownlee, G. G. & Sanger, F. Eur. J. Biochem. 13, 395–399 (1969).
Barrell, B. G. in Procedures in Nucleic Acid Research Vol. 2 (eds Cantoni, G. & Davies, D.) 751–779 (Harper and Row, New York, 1971).
Blattner, F. & Dahlberg, J. Nature 237, 227–232 (1972).
Steege, D. A. J. molec. Biol. 114, 559–568 (1977).
Rosenberg, M., de Crombrugghe, B. & Musso, R. Proc. natn. Acad. Sci. U.S.A. 73, 717–721 (1976).
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Paterson, B., Rosenberg, M. Efficient translation of prokaryotic mRNAs in a eukaryotic cell-free system requires addition of a cap structure. Nature 279, 692–696 (1979). https://doi.org/10.1038/279692a0
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DOI: https://doi.org/10.1038/279692a0
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