Role of plasma membranes in stimulation of RNA-directed DNA synthesis


THERE has been considerable speculation about the small size of DNA transcripts (less than 10S) obtained by reverse transcription in vitro of 60–70S RNA from oncorna-viruses1–4. On the basis of evidence suggesting that at least part of the virus-specific DNA synthesis could be taking place at the plasma membrane5,6 we have examined the role of membrane-bound factors on RNA-directed DNA synthesis (RDDS). We report here the existence of a protein factor, associated with plasma membrane preparations from chick embryonic cells, that stimulates RDDS in avian my-eloblastosis virus (AMV). The stimulated synthesis is sensitive to RNase, and the product DNA is 33–35S in alkaline sucrose gradients.

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  1. 1

    Temin, H. M., and Baltimore, D., Adv. Virus Res., 17, 129–186 (1972).

  2. 2

    Mizutani, S., and Temin, H. M., Cold Spring Harb. Symp. quant. Biol., 35, 847–849 (1970).

  3. 3

    Gillespie, D., Saxinger, W. C., and Gallo, R. C., Prog. Nucleic Acids Res. Molec. Biol., 15, 1–108 (1975).

  4. 4

    Junghuns, R. P., Duesberg, P. H., and Knight, C. A., Proc. natn. Acad. Sci. U.S.A., 72, 4895–4899 (1975).

  5. 5

    Hatanaka, M., Kakefuda, T., Gilden, R. V., and Callan, E. A. O., Proc. natn. Acad. Sci. U.S.A., 68, 1844–1847 (1971).

  6. 6

    Takano, T., and Hatanaka, M., Proc. natn. Acad. Sci. U.S.A., 72, 343–347 (1975).

  7. 7

    Hung, P. P., and Lee, S. G., Nature, 259. 499–502 (1976).

  8. 8

    Emmelot, P., Bos, C. J., van Hoeven, R. P., and van Blitterswijk, W. J., in Methods in Enzymology, 31 (edit. by Fleischer, S., and Packer, L.), 75–90 (Academic, New York, 1974).

  9. 9

    Warren, L., and Glick, M. C., in Fundamental Techniques in Virology (edit. by Habel, K., and Salzman, N. P.), 66–71 (Academic, New York, 1969).

  10. 10

    Perdue, J. F., and Sneider, J., Biochim. biophys. Acta, 196, 125–140 (1970).

  11. 11

    Post, R. L., and Sen, A. K., in Methods in Enzymology, 10 (edit. by Estabrook, R. W., and Pullman, M. E.), 762–768 (Academic, New York, 1967).

  12. 12

    Morre, D. J., in Methods in Enzymology, 22 (edit. by Jakoby, W. B.), 137–138 (Academic, New York, 1967).

  13. 13

    Malamy, M., and Horecker, B. L., in Methods in Enzymology, 9 (edit. by Wood, W. A.), 639–642 (Academic, New York, 1966).

  14. 14

    King, T. E., in Methods in Enzymology, 10 (edit. by Estabrook, R. W., and Pullman, M. E.), 322–331 (Academic, New York, 1967).

  15. 15

    Pennington, R. J., Biochem. J., 80, 649–654 (1961).

  16. 16

    Das, M. R., Sadasivan, E., Koshy, R., Vaidya, A. B., and Sirsat, S. M., Nature new Biol., 239, 92–95 (1972).

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