Abstract
Eukaryotic initiation factor 2 (eIF-2) has a dual function in initiation of protein synthesis: it binds Met-tRNAf to the small ribosomal subunit, and it binds directly to mRNA. The binding of eIF-2 to mRNA is highly specific and occurs in satellite tobacco necrosis virus RNA and Mengovirus RNA at the nucleotide sequences that constitute the ribosome binding sites. These findings support the concept that, during translation, eIF-2 may guide the ribosome to this site. Cl− or OAc− ions inhibit the direct binding of globin mRNA to eIP-2 in a manner that closely resembles their inhibitory effect on the translation of globin mRNA, an inhibition that is relieved by excess eIF-2. Hence,these anions may act to inhibit the interaction between mRNA and eIF-2 during protein synthesis. In mRNA-dependent reticulocyte lysates, a molecule of Mengovirus RNA competes in translation 35-fold more strongly than (on average) a molecule of globin mRNA. This competition is relieved by excess eIF-2. Mengovirus RNA binds directly to eIF-2 with 30-fold higher affinity than does globin mRNA. These results reveal a direct correlation between the affinity of a given mRNA species for eIF-2 and its ability to compete in translation. Indeed, the translational competition between α- and β-globin mRNA is also relieved by excess eIF-2, and in direct binding analysis, β-globin mRNA exhibits greater affinity for eIF-2 than does α-globin mRNA.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Barrieux, A. & Rosenfeld, M.G. (1977). J. Biol. Chem. 252, 3843–3847.
Barrieux, A. & Rosenfeld, M.G. (1978). J. Biol. Chem. 253, 6311–6315.
Browning, K.S., Leung, D.W. & Clark, J.M., Jr. (1980). Biochemistry 19, 2276–2282.
Clemens, M.J., Safer, B., Merrick, W.C., Anderson, W.F. & London, I.M. (1975). Proc. Natl. Acad. Sci. USA 72, 1286–1290.
Darnbrough, C.H., Legon, S., Hunt, T. & Jackson, R.J. (1973). J. Mol. Biol. 76, 379–403.
Di Segni, G., Rosen, H. & Kaempfer, R. (1979). Biochemistry 18, 2847–2854.
Grifo, J.A., Tahara, S.M., Leis, J.P., Morgan, M.A. Shatkin, A.J. & Merrick, W.C. (1982). J. Biol. Chem. 257, 5246–5252.
Hackett, P.B., Egberts, E. & Traub, P. (1978a). Eur. J. Biochem. 83, 341–352.
Hackett, P.B., Egberts, E. & Traub, P. (1978b).Eur. J. Biochem. 83, 353–361.
Kaempfer, R. (1974). Biochem. Biophys. Res. Commun. 61, 591–597.
Kaempfer, R., Hoilender, R., Abrams, W.R. & Israeli R. (1978a). Proc. Natl. Acad. Sci. USA 75, 209–213.
Kaempfer, R., Rollender, R., Soreq, H. & Nudel, U. (1979a). Eur. J. Biochem. 94., 591–600.
Kaempfer, R., Israeli, R., Rosen, H., Knoller, S., Zilber-Stein, A., Schmidt, A. & Revel, M. (1979b).Virology 99, 170–173.
Kaempfer, R. & Konijn, A.M. (1983).Eur. J. Biochem.131, 545–550.
Kaempfer, R., Rosen, H., Di Segni, G. & Knoller, S. (1983). InMechanisms of Viral Pathogenesis (Kohn, A., ed.) Martinus Nijhoff, The Hague, in press
Kaempfer, R., Rosen, H. & Israeli, R. (1978b).Proc. Natl. Acad. Sci. USA.75 650–654.
Kaempfer, R., van Emroelo, J. & Fiers, W. (1981). Proc. Natl. Acad. Sci. USA 78, 1542–1546.
Lawrence, C. & Thach, R. (1974). J. Virol. 14, 598–610.
Lee, K.A.W., Guertin, D. S Sonenberg, N. (1983). J. Biol. Chem. 258, 707–710.
Leung, D.W., Browning, K.S., Heckmann, J.E., RajBhandary, U. L. & Clark, J.M. Jr. (1979). Biochemistry 18, 1361–1366.
Levin, D.H., Kyner, D. & Acs, G. (1973). Proc. Natl. Acad. Sci. USA 70, 41–45.
Lodish, H.F. (1971). J. Biol. Chem. 246, 7131–7138.
Lodish, H.F. (1974). Nature (London) 251, 385–388.
Pelham, H.R.B. & Jackson, R.J. (1976). Eur. J. Blochem. 67, 247–256.
Perez-Bercoff, R. & Kaempfer, R. (1982). J. Virol. 41, 30–41.
Ray, B.K., Brendler, T.G., Adya, S., Daniels-McQueen, S., Miller, J.K., Hershey, J.W.B., Grifo, J.A., Merrick, W.C. & Thach, R.E. (1983). Proc. Natl. Acad. Sci. USA 80, 663–667.
Rosen, H., Di Segni, G. & Kaempfer, R. (1982). J. Biol. Chem. 257, 946–952.
Rosen, 11. & Kaempfer, R. (1979). Biochem. Biophys Res. Commun. 91, 449–455.
Rosen, H., Knoller, S. & Kaempfer, R. (1981). Biochemistry 20, 3011–3020.
Schreier, M.H. & Staehelin, T. (1973). Nature ( London ), New Biol. 242, 35–38.
Sonenberg, N. (1981). Nuclelc Acids Res. 9 1643–1656.
Trachsel, H., Erni, B., Schreier, M.H. & Staehelin, T. (1977). J. Mol. Biol. 116, 755–767.
Weber, L.A., Hickey, E.D., Maroney, P.A. & Baglioni, C. (1977). J. Biol. Chem. 252, 4007–4010.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1983 The Human Press Inc.
About this chapter
Cite this chapter
Nygård, O., Westermann, P. (1983). Differential Gene Expression by Messenger RNA Competition. In: Abraham, A.K., Eikhom, T.S., Pryme, I.F. (eds) Protein Synthesis. Humana Press. https://doi.org/10.1007/978-1-4612-5310-5_4
Download citation
DOI: https://doi.org/10.1007/978-1-4612-5310-5_4
Publisher Name: Humana Press
Print ISBN: 978-1-4612-9780-2
Online ISBN: 978-1-4612-5310-5
eBook Packages: Springer Book Archive