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Functional and Structural Characteristics of Eukaryotic mRNA Cap Binding Protein Complex

  • Odd Nygård
  • Peter Westermann
Chapter
  • 63 Downloads

Abstract

We describe a purified mRNA cap binding protein complex comprising three major polypeptides of ∿ 24, 50 and 220 kilodaltons (kDa). The 24 kDa polypeptide corresponds to the 24 kDa cap binding protein previously described (Sonenberg et al., 1978; Tahara et al., 1981), while the 50 kDa polypeptide is eIF-4A. We show some functional characteristics of the CBP complex and present direct evidence that the 220 kDa polypeptide can be proteolyzed in vitro by a component present in extracts from poliovirus-infected cells.

Keywords

Vesicular Stomatitis Virus mRNA Secondary Structure Major Polypeptide Poliovirus Infection Binding Protein Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bablanian, R. (1975) In “Progress in Medical Virology”. Mel nick, J.L. ed. Karger, Basel, Vol. 29, pp. 101–176.Google Scholar
  2. Banerjee, A.K. (1980) Bacterid. Rev. 44, 175–205.Google Scholar
  3. Benne, R. and Hershey, J.W.B. (1978) J. Biol. Chem. 253, 3078–3087.PubMedGoogle Scholar
  4. Bergmann, J.E., Trachsel, H., Sonenberg, N., Shatkin, A.J. and Lodish, H.F. (1979) J. Biol. Chem. 254, 1440–1443.PubMedGoogle Scholar
  5. Bonatti, S., Sonenberg, N., Shatkin, A.J. and Cancedda, R. (1980) J. Biol. Chem. 255, 11473–11477.PubMedGoogle Scholar
  6. Chu, L.-Y. and Rhodes, R.E. (1978) Biochem. 17, 2450–2454.CrossRefGoogle Scholar
  7. Dorner, A.J., Dorner, L.F., Larsen, G.R., Wimmer, E. and Anderson, C.W. (1982) J. Virol. 42, 1017–1028.PubMedGoogle Scholar
  8. Duncan, R., Etchison, D. and Hershey, J.W.B. (1983) J. Biol. Chem., in press.Google Scholar
  9. Edery, I., Humbelin, M., Darveau, A., Lee, K.A.W., Milburn, S., Hershey, J.W.B., Trachsel, H. and Sonenberg, N. (1983) Submitted.Google Scholar
  10. Ehrenfeld, E. (1982) Cell 28, 435–436.Google Scholar
  11. Etchison, D., Milburn, S.C., Edery, I., Sonenberg, N. and Hershey, J.W.B. (1982) J. Biol. Chem. 257, 14806–14810.PubMedGoogle Scholar
  12. Gehrke, L., Auron, P.E., Quigley, G.J., Rich, A. and Sonenberg, N. (1983) Submitted.Google Scholar
  13. Gehrke, L., Auron, P.E., Quigley, G.J., Rich, A. and Sonenberg, N. (1983) Submitted.Google Scholar
  14. Grifo, O.A., Tahara, S., Leis, J., Morgan, M.A., Shatkin, A.J. and Merrick, W.C. (1982) J. Biol. Chem. 257, 5246–5252.PubMedGoogle Scholar
  15. Hansen, J.L. and Ehrenfeld, E. (1981) J. Virol. 38, 438–445.PubMedGoogle Scholar
  16. Held, W.A., West, K. and Gallagher, J.F. (1977) J. Biol. Chem. 252, 8489–8497.PubMedGoogle Scholar
  17. Helentjaris, T., Ehrenfeld, E., Brown-Leudi, M.L. and Hershey, J.W.B. (1979) J. Biol. Chem. 254, 10973–10978.PubMedGoogle Scholar
  18. Hickey, E.D. and Weber, L.A. (1982) Biochem. 21, 1513–1521.CrossRefGoogle Scholar
  19. Holder, J.W. and Lingrel, J.B. (1975) Biochem. 14, 4209–4215.CrossRefGoogle Scholar
  20. Jackson, R.J. (1982) In “Protein Synthesis in Eukaryotes” Perez-Bercoff, R. ed. Plenum Press, New York, pp. 363–418.Google Scholar
  21. Jagus, R., Anderson, W.F. and Safer, B. (1981) Nucl. Acid Res. and Mol. Biol. 25, 127–185.CrossRefGoogle Scholar
  22. Kaempfer, R., Rosen, H. and Israeli, R. (1978) Proc. Natl. Acad. Sci. USA 75, 650–654.PubMedCrossRefGoogle Scholar
  23. Kaufman, Y., Goldstein, E. and Penman, S. (1976) Proc. Natl. Acad. Sci. USA 73, 1834–1838.CrossRefGoogle Scholar
  24. Korant, B.D. (1979) In “The Molecular Biology of Picorna- viruses” Perez-Bercoff, ed. Plenum Publishing Corp., New York, pp. 113–125.Google Scholar
  25. Kozak, M. (1980) Cell 22, 459–467.PubMedCrossRefGoogle Scholar
  26. Larsen, G.R., Semler, B.L. and Wimmer, E. (1981) J. Virol. 37, 328–335.PubMedGoogle Scholar
  27. Lee, K.A.W., Guertin, D. and Sonenberg, N. (1983) J. Biol. Chem. 258, 707–710.PubMedGoogle Scholar
  28. Lee, K.A.W. and Sonenberg, N. (1982) Proc. Natl. Acad. Sci. USA 79, 3447–3451.PubMedCrossRefGoogle Scholar
  29. Leung, D.W., Browning, K.S., Heckman, J.E., RajBhandary, U.L. and Clark, J.M. Jr. (1979) Biochem. 18, 1361–1366.CrossRefGoogle Scholar
  30. Lodish, H.F. (1976) Ann. Rev. Biochem. 45, 39–72.PubMedCrossRefGoogle Scholar
  31. Marcus, A. (1970) J. Biol. Chem. 245, 955–961.PubMedGoogle Scholar
  32. Morgan, M.A. and Shatkin, A.J. (1980) Biochem. 19, 5960–5966.CrossRefGoogle Scholar
  33. Perez-Bercoff, R. (1982) In “Protein Biosynthesis in Euka-ryotes” Perez-Bercoff, R. ed. Plenum Press, New York pp. 245–252.Google Scholar
  34. Raff, R. (1980) In “Cell Biology” Prescott, D.M. and Goldstein, L. eds. Academic Press, New York, Vol. 4, pp. 107–129.Google Scholar
  35. Ray, B.K., Brendler, T.G., Adya, S., Daniels-McQueen, S., Miller, J.K., Hershey, J.W.B., Grifo, J.A., Merrick, W.C. and Thach, R.E. (1983) Proc. Natl. Acad. Sci. USA 80 663–667.PubMedCrossRefGoogle Scholar
  36. Rose, J.K., Trachsel, H., Leong, K. and Baltimore, D. (1978) Proc. Natl. Acad. Sci. USA 75, 2732–2736.PubMedCrossRefGoogle Scholar
  37. Safer, B., Kemper, W. and Jagus, R. (1978) J. Biol. Chem. 253, 3384–3386.PubMedGoogle Scholar
  38. Shatkin, A.J. (1976) Cell 9, 645–653.PubMedCrossRefGoogle Scholar
  39. Sonenberg, N., Guertin, D. and Lee, K.A.W. (1982) Mol. Cell Biol. 2, 1633–1638.PubMedGoogle Scholar
  40. Sonenberg, N., Guertin, D., Cleveland, D. and Trachsel, H. (1981) Cell 27, 563–572.PubMedCrossRefGoogle Scholar
  41. Sonenberg, N. (1981) Nucleic Acids Res. 9, 1643–1656.PubMedCrossRefGoogle Scholar
  42. Sonenberg, N., Trachsel, H., Hecht, S.M. and Shatkin, A.J. (1980) Nature 285, 331–333.PubMedCrossRefGoogle Scholar
  43. Sonenberg, N., Rupprecht, K.M., Hecht, S.M. and Shatkin, A.J. (1979) Proc. Natl. Acad. Sci. USA 76, 4345–4358.PubMedCrossRefGoogle Scholar
  44. Sonenberg, N., Morgan, M.A., Merrick, W.C. and Shatkin, A.J. (1978) Proc. Natl. Acad. Sci. USA 75, 4843–4847.PubMedCrossRefGoogle Scholar
  45. Sonenberg, N. and Shatkin, A.J. (1978) J. Biol. Chem. 253, 6630–6632.PubMedGoogle Scholar
  46. Sonenberg, N. and Shatkin, A.J. (1977) Proc. Natl. Acad. Sci. USA 74, 4288–4292.PubMedCrossRefGoogle Scholar
  47. Shafritz, D.A., Weinstein, J.A., Safer, B., Merrick, W.C., Weber, L.A., Hickey, E.D. and Baglioni, C. (1976) Nature 261, 291–294.PubMedCrossRefGoogle Scholar
  48. Storti, R.V., Scott, M.O., Rich, A. and Pardue, M.L. (1980) Cell 22, 825–834.PubMedCrossRefGoogle Scholar
  49. Tahara, S.M., Morgan, M.A. and Shatkin, A.J. (1981) J. Biol. Chem. 256, 7691–7694.PubMedGoogle Scholar
  50. Tahara, S.M., Morgan, M.A., Grifo, J.A., Merrick, W.C. and Shatkin, A.J. (1982) in “Interaction of Translational and Transcriptional Controls in the Regulation of Gene Expression,” (Grunberg-Manago, M. and Safer, B. eds.) Elsevier, New York, pp. 359–372.Google Scholar
  51. Trachsel, H., Sonenberg, N., Shatkin, A.J., Rose, J.K., Leong, K., Bergmann, J.E., Gordon, J. and Baltimore, D. (1980) Proc. Natl. Acad. Sci. USA 77, 770–774.PubMedCrossRefGoogle Scholar
  52. Trachsel, H., Erni, B., Schreier, M.H. and Staehelin, T. (1977) J. Mol. Biol. 116, 755–767.PubMedCrossRefGoogle Scholar
  53. Towbin, H., Staehelin, T. and Gordon, J. (1979) Proc. Natl. Acad. Sci. USA 76, 4350–4354.PubMedCrossRefGoogle Scholar
  54. Waiden, W.E. and Thach, R.E. (1982). In: “Interaction cf Translational & Transcriptional Controls in the Regulation of Gene Expression.” Eds. M. Grunberg-Manago and B. Safer, Elsevier, New York, Vol. 24, pp. 399–413.Google Scholar
  55. Weber, L.A., Hickey, E.D., Nuss, D.L. and Baglioni, C. (1977) Proc. Natl. Acad. Sci. USA 74, 3254–3258.PubMedCrossRefGoogle Scholar

Copyright information

© The Human Press Inc. 1983

Authors and Affiliations

  • Odd Nygård
    • 1
  • Peter Westermann
    • 2
  1. 1.The Wenner-Gren InstituteUniversity of StockholmStockholmSweden
  2. 2.Central Institute of Molecular BiologyAcademy of Sciences of GDRBerlin-BuchGermany

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