Abstract
The cap structure, m7GpppN, which is present at the 5′ end of most eukaryotic mRNAs, facilitates the initiation of protein synthesis1. Rabbit reticulocytes and mouse L and ascites cells have been shown to contain a protein (molecular weight (MW) 24,000) that specifically recognizes the cap of reovirus mRNA and several other capped mRNAs2. That protein partially co-purifies with eIF-3 and eIF-4B (refs 2, 3), two eukaryotic initiation factors involved in mRNA binding to ribosomes4. We have isolated essentially homogeneous 24,000-MW polypeptide which stimulated translation of capped mRNAs in vitro5. Consistent with those findings, we now report that among the many protein synthesis factors tested, preparations of eIF-3 and eIF-4B that also contained the 24,000-MW cap binding protein (CBP) markedly increased translation in HeLa cell extracts of capped mRNAs but not of naturally uncapped viral messengers. Moreover, removal of the 24,000-MW protein diminished the ability of eIF-3 to stimulate translation of capped mRNA. Purified CBP, which had no effect on uncapped satellite tobacco necrosis virus (STNV) RNA, stimulated translation of this RNA after addition of a cap. The protein also relieved translational competition between capped and naturally uncapped mRNAs in favour of the capped species. These findings support the hypothesis that the CBP participates in the regulation of eukaryotic mRNA translation in normal and virus-infected cells6.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Shatkin, A. J. Cell 9, 645–653 (1976).
Sonenberg, N., Morgan, M. A., Merrick, W. C. & Shatkin, A. J. Proc. natn. Acad. Sci. U.S.A. 75, 4843–4847 (1978).
Bergmann, J. E., Trachsel, H., Sonenberg, N., Shatkin, A. J. & Lodish, H. F. J. biol. Chem. 254, 1440–1443 (1979).
Trachsel, H., Erni, B., Schreier, M. H. & Staehelin, T. J. molec. Biol. 116, 755–767 (1977).
Sonenberg, N., Rupprecht, K. M., Hecht, S. M. & Shatkin, A. J. Proc. natn. Acad. Sci. U.S.A. 76, 4345–4349 (1979).
Trachsel, H. et al. Proc. natn. Acad. Sci. U.S.A. 77, 770–774 (1980).
Dubin, D. T., Timko, K., Gillies, S. & Stollar, V. Virology 98, 131–141 (1979).
Frisby, D., Eaton, M. & Fellner, P. Nucleic Acids Res. 3, 2771–2787 (1976).
Simmons, D. T. & Strauss, J. H. J. molec. Biol. 86, 397–409 (1974).
Shatkin, A. J. & Both, G. W. Cell 7, 305–313 (1976).
Wimmer, E., Chang, A. Y., Clark, J. M. Jr & Reichman, M. E. J. molec. Biol. 38, 59–73 (1968).
Van Vloten-Doting, L. & Jaspars, E. M. J. Comprehensive Virol. 11, 1–53 (1977).
Herson, D., Schmidt, A., Seal, S., Marcus, A. & Van Vloten-Doting, L. J. biol. Chem. 254, 8245–8249 (1979).
Golini, F. et al. Proc. natn. Acad. Sci. U.S.A. 73, 3040–3044 (1976).
Kabat, D. & Chappell, J. R. J. biol. Chem. 252, 2684–2690 (1977).
Shafritz, D. A. et al. Nature 261, 291–294 (1976).
Rose, J. K., Trachsel, H., Leong, K. & Baltimore, D. Proc. natn. Acad. Sci. U.S.A. 75, 2732–2736 (1978).
Gette, W. R. & Heywood, S. M. J. biol. Chem. 254, 9879–9885 (1979).
Moss, B. Biochem. biophys. Res. Commun. 74, 374–383 (1977).
Sonenberg, N., Shatkin, A. J., Ricciardi, R. P., Rubin, M. & Goodman, R. M. Nucleic Acids Res. 5, 2501–2512 (1978).
Salvato, M. S. & Fraenkel-Conrat, H. Proc. natn. Acad. Sci. U.S.A. 74, 2288–2292 (1977).
Nudel, U., Lebleu, B. & Revel, M. Proc. natn. Acad. Sci. U.S.A. 70, 2139–2144 (1973).
Lebleu, B., Nudel, U., Falcoff, E., Prives, C. & Revel, M. FEBS Lett. 25, 97–103 (1972).
Skup, D. & Millward, S. Proc. natn. Acad. Sci. U.S.A. 77, 152–156 (1980).
Cancedda, R. & Shatkin, A. J. Eur. J. Biochem. 94, 41–50 (1979).
Eggen, K. L. & Shatkin, A. J. J. Virol. 9, 636–645 (1972).
Laemmli, U. K. & Favre, J. J. molec. Biol. 80, 575–599 (1973).
Sonenberg, N. & Shatkin, A. J. Proc. natn. Acad. Sci. U.S.A. 74, 4288–4292 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Sonenberg, N., Trachsel, H., Hecht, S. et al. Differential stimulation of capped mRNA translation in vitro by cap binding protein. Nature 285, 331–333 (1980). https://doi.org/10.1038/285331a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/285331a0
This article is cited by
-
Signal transduction mechanisms in the regulation of protein synthesis
Molecular Biology Reports (1994)
-
Translation of vaccinia virus and cellular mRNA in cell-free systems prepared from uninfected and vaccinia virus infected L929 cells
Archives of Virology (1984)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.