The Cell Free Translation of Purified Simian Virus 40 Messenger RNA

  • Carol Prives
Part of the NATO Advanced Study Institutes Series book series (NSSA, volume 5)


In order to understand the expression of the Simian Virus 40 (SV40) genome, it is important to be able to ascertain which new proteins appearing after infection are virus specified. This is especially true considering the potent transforming properties of the virus where the number of changes induced in the transformation process are far too numerous to be accounted for directly by the SV40 genome. The cell free synthesis of viral polypeptides directed by purified viral genetic material is one clear method of establishing which proteins are virus specific. Since SV40 does not inhibit host RNA or protein synthesis after infection and viral proteins do not comprise more than 10% of the total proteins synthesized even late in infection (Walter, Roblin, and Dulbecco, 1972; Anderson and Gesteland, 1972), the translation of total messenger RNA from SV40 infected cells will not establish which products are virus specific. In order to obtain purified SV40 mRNA, we have hybridized poly(A)-containing RNA from SV40 infected monkey cells (BS-C-1 line) to SV40 DNA according to a technique described by Weinberg, Warnaar, and Winocour (1972).


SV40 Virion Cellulose Chromatography SV40 Genome Wheat Germ System Cell Free Product 
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  1. Anderson, C. W., and R. F. Gesteland. 1972. J. Virol. 9:758.PubMedGoogle Scholar
  2. Aviv, H., and P. Leder. 1972. Proc. Nat. Acad. Sci. U.S.A. 69: 1408.CrossRefGoogle Scholar
  3. Crawford, L. V. 1973. Brit. Med. Bull. 29:253.PubMedGoogle Scholar
  4. Greenway, P. J., and D. LeVine. 1973. Bioehem. Biophys. Res. Comm. 52:1221.CrossRefGoogle Scholar
  5. Lavi, S., and E. Winocour. 1972. J. Virol. 9:309.PubMedGoogle Scholar
  6. Prives, C. L., H. Aviv, B. M. Paterson, B. E. Roberts, S. Rosenblatt, M. Revel, and E. Winocour. 1974. Proc. Nat. Acad. Sci. U.S.A. 71:302.CrossRefGoogle Scholar
  7. Roberts, B. E., and B. M. Paterson. 1973. Proc. Nat. Acad. Sci. U.S.A. 70:2330.CrossRefGoogle Scholar
  8. Rosenblatt, S., and E. Winocour. 1972. Virology 50Google Scholar
  9. Singer, R. H., and S. Penman. 1973. J. Mol. Biol. 78:321.PubMedCrossRefGoogle Scholar
  10. Walter, G., R. Roblin, and R. Dulbecco. 1972. Proc. Nat. Acad. Sci. U.S.A. 69:929.Google Scholar
  11. Weinberg, R. A., S. O. Warnaar, and E. Winocour. 1972. J. Virol. 10:193.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1975

Authors and Affiliations

  • Carol Prives
    • 1
  1. 1.Biochemistry DepartmentWeizman Institute of ScienceRehovotIsrael

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