Abstract
Site-specific recombination of the bacteriophage λ genome into and out of the host bacterial genome is postulated to involve the formation of Holliday structure intermediates by reciprocal single-strand exchanges. Synthetic analogues of the predicted recombination intermediates are resolved in vitro by the protein product of the λ int gene. Some of the structural features and reaction conditions for this genetic recombination can now be defined.
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References
Nash, H. A. A. Rev. Genet. 15, 143–167 (1981).
Weisberg, R. & Landy, A. in Lambda II (eds Hendrix, R. W., Roberts, J. W., Stahl, F. W. & Weisberg, R. W.) 211–250 (Cold Spring Harbor Laboratory, New York, 1983).
Kikuchi, A. & Nash, H. A. Proc. natn. Acad. Sci. U.S.A. 76, 3760–3764 (1979).
Nash, H. A. & Robertson, C. A. J. biol. Chem. 256, 9246–9253 (1981).
Abremski, K. & Gottesman, S. J. biol. Chem. 257, 9658–9710 (1982).
Better, M., Wickner, S., Auerback, J., Williams, R. & Echols, H. Cell 32, 161–168 (1983).
Hsu, P-L., Ross, W. & Landy, A. Nature 285, 85–91 (1980).
Landy, A. & Ross, W. Science 197, 1147–1160 (1977).
Ross, W. & Landy, A. Proc. natn. Acad. Sci. U.S.A. 79, 7724–7728 (1982).
Ross, W. & Landy, A. Cell 33, 261–272 (1983).
Mizuuchi, M. & Mizuuchi, K. Proc. natn. Acad. Sci. U.S.A. 77, 3220–3224 (1980).
Mizuuchi, K. et al. Cold Spring Harb. Symp. quant. Biol. 45, 429–437 (1981).
Weisberg, R., Enquist, L., Foeller, C. & Landy, A. J. molec. Biol. 170, 319–342 (1983).
Enquist, L. W., Nash, H. A. & Weisberg, R. A. Proc. natn. Acad. Sci. U.S.A. 76, 1363–1367 (1979).
Echols, H. & Green, L. Genetics 93, 297–307 (1979).
Holliday, R. Genet. Res. 5, 282–304 (1964).
Sigal, N. & Alberts, B. J. molec. Biol. 71, 789–793 (1972).
Holliday, R. Genetics 78, 273–287 (1974).
Dressler, E. & Potter, H. A. Rev. Biochem. 51, 727–761 (1982).
Stahl, F. Genetic Recombination. Thinking about it in Phage and Fungi (Freeman, San Francisco, 1979).
Thompson, B. et al. J. molec. Biol. 91, 409–419 (1975).
Benbow, R., Zuccavelli, A. & Sinsheimer, R. Proc. natn. Acad. Sci. U.S.A. 72, 235–239 (1975).
Valenzuela, M. & Inman, R. Proc. natn. Acad. Sci. U.S.A. 72, 3024–3028 (1975).
Thompson, B. J., Camien, M. N. & Warner, R. C. Proc. natn. Acad. Sci. U.S.A. 73, 2299–2303 (1976).
Potter, H. & Dressler, D. Proc. natn. Acad. Sci. U.S.A. 73, 3000–3004 (1976).
Bell, L. & Byers, B. Proc. natn. Acad. Sci. U.S.A. 76, 3445–3449 (1979).
Wolgemuth, D. J. & Hsu, M. T. Nature 287, 168–171 (1980).
Cozzarelli, N. R. Science 207, 953–960 (1980).
Gellert, M. A. Rev. Biochem. 50, 879–910 (1981).
Liu, L. F. & Miller, K. G. Proc. natn. Acad. Sci. U.S.A. 78, 3487–3491 (1981).
Liu, L. F., Liu, C.-C. & Alberts, B. M. Nature 281, 456–461 (1979).
Miller, K. G., Liu, L. F. & Englund, P. T. J. biol. Chem. 256, 9334–9339 (1981).
Miller, H. I. & Friedman, D. I. Cell 20, 711–719 (1980).
Nash, H. A., Mizuuchi, K., Enquist, L. W. & Weisberg, R. A. Cold Spring Harb. Symp. quant. Biol. 45, 417–428 (1981).
Craig, N. & Nash, H. Cell 35, 795–803 (1983).
Mizuuchi, K., Kemper, B., Hays, J. & Weisberg, R. Cell 29, 357–365 (1982).
Hamilton, P., Yuan, R. & Kikuchi, Y. J. molec. Biol. 152, 163–170 (1981).
Better, M., Chi, L., Williams, R. C. & Echols, H. Proc. natn. Acad. Sci. U.S.A. 79, 5837–5841 (1982).
Davies, R. W., Schreier, P. H., Kotewicz, M. L. & Echols, H. Nucleic Acids Res. 7, 2255–2273 (1979).
Nash, H. & Pollock, T. J. molec. Biol. 170, 19–38 (1983).
Pollock, T. & Nash, H. J. molec. Biol. 170, 1–18 (1983).
Rossi, J. J., Ross, W., Egan, J., Lipman, D. J. & Landy, A. J. molec. Biol. 128, 21–47 (1979).
Nash, H. A. Meth. Enzym. 100, 210–216 (1983).
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Hsu, P., Landy, A. Resolution of synthetic att-site Holliday structures by the integrase protein of bacteriophage λ. Nature 311, 721–726 (1984). https://doi.org/10.1038/311721a0
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DOI: https://doi.org/10.1038/311721a0
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