Abstract
Physical and enzymatic studies on RecA protein from Escherichia coli provide the basis for a molecular model of general genetic recombination, a novel feature of which is the role attributed to spiral filaments of RecA protein.
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References
Holliday, R. Genet. Res. 5, 282–304 (1964).
West, S. C., Cassuto, E. & Howard-Flanders, P. Nature 294, 659–662 (1981).
Radding, C. M. A. Rev. Genet. 16, 405–437 (1983).
Meselson, M. & Radding, C. M. Proc. natn. Acad. Sci. U.S.A. 72, 358–361 (1975).
Stahl, F. W. Genetics Suppl. 61, 1–13 (1969).
Stahl, F. W. Genetic Recombination: Thinking about it in Phage and Fungi (Freeman, San Francisco, 1979).
Szostak, J. W., Orr-Weaver, T.L., Rothstein, R.J. & Stahl, F.W. Cell 33, 25–35 (1983).
Rupp, W. D., Wilde, C. E., Reno, D. L. & Howard-Flanders, P. J. molec. Biol. 61, 25–44 (1971).
Cassuto, E., West, S. C., Mursalim, J., Conlon, S. & Howard-Flanders, P. Proc. natn. Acad. Sci. U.S.A. 77, 3962–3966 (1980).
Cunningham, R. P., DasGupta, C., Shibata, T. & Radding, C.M. Cell 20, 223–235 (1980).
West, S. C., Cassuto, E. & Howard-Flanders, P. Molec. gen. Genet. 187, 209–217 (1982).
Fogel, S., Mortimer, R., Lusnak, K. & Travers, F. Cold Spring Harb. Symp. quant. Biol. 43, 1325–1341 (1979).
Hamza, H., Haedens, V., Mekki-Berrada, A. & Rossignol, J.L. Proc. natn. Acad. Sci. U.S.A. 78, 7648–7651 (1981).
Orr-Weaver, T. L., Szostak, J. W. & Rothstein, R. J. Proc. natn. Acad. Sci. U.S.A. 78, 6354–6358 (1981).
Strathern, J. N. et al. Cell 31, 183–192 (1982).
Lin, P. F., Bardwell, E. & Howard-Flanders, P. Proc. natn. Acad. Sci. U.S.A. 74, 291–295 (1977).
Clark, A. J. & Margulies, A. D. Proc. natn. Acad. Sci. U.S.A. 53, 451–459 (1965).
Gudas, L. J. & Pardee, A. J. molec. Biol. 101, 459–477 (1976).
McEntee, K., Hesse, J. E. & Epstein, W. Proc. natn. Acad. Sci. U.S.A. 73, 3979–3983 (1976).
Gudas, L. J. & Mount, D. W. Proc. natn. Acad. Sci. U.S.A. 74, 5280–5284 (1977).
Emmerson, P. T. & West, S. C. Molec. gen. Genet. 155, 77–85 (1977).
Little, J. W. & Kleid, D. G. J. biol. Chem. 252, 6251–6252 (1977).
Roberts, J. W., Roberts, C. W. & Craig, N. L. Proc. natn. Acad. Sci. U.S.A. 75, 4714–4718 (1978).
Horii, T., Ogawa, T. & Ogawa, H. Proc. natn. Acad. Sci. U.S.A. 77, 313–317 (1980).
Sancar, A., Stachelek, C., Konigsberg, W. & Rupp, W. D. Proc. natn. Acad. Sci. U.S.A. 77, 2611–2615 (1980).
McEntee, K., Weinstock, G. M. & Lehman, I. R. J. biol. Chem. 256, 8835–8844 (1981).
West, S. C., Cassuto, E., Mursalim, J. & Howard-Flanders, P. Proc. natn. Acad. Sci. U.S.A. 77, 2569–2573 (1980).
Stasiak, A., DiCapua, E. & Koller, T. Cold Spring Harb. Symp. quant. Biol. 47, 811–820 (1983).
DiCapua, E., Engel, A. E., Stasiak, A. & Koller, T. J. molec. Biol. 157, 87–103 (1982).
Stasiak, A. & DiCapua, E. Nature 299, 185–186 (1982).
Dombrowski, D. F., Scraba, D. G., Bradley, R. B. & Morgan, A. R. Nucleic Acids Res. 11, 7487–7504 (1983).
Chrysogelos, S., Register, J. C. & Griffith, J. J. biol. Chem. 258, 12624–12631 (1983).
Flory, J. & Radding, C. M. Cell 28, 747–756 (1982).
McKay, D. B., Steitz, T. A., Weber, I. T., West, S. C. & Howard-Flanders, P. J. biol. Chem. 225, 6662 (1980).
Cox, M. M. & Lehman, I. R. Proc. natn. Acad. Sci. U.S.A. 78, 6018–6022 (1981).
Kahn, R., Cunningham, R. P., DasGupta, C. & Radding, C. M. Proc. natn. Acad. Sci. U.S.A. 78, 4786–4790 (1981).
West, S. C., Cassuto, E. & Howard-Flanders, P. Proc. natn. Acad. Sci U.S.A. 78, 6159–6153 (1981).
Roberts, J. W., Roberts, C. W., Craig, N. L. & Phizicky, E. M. Cold Spring Harb. Symp. quant. Biol. 43, 917–923 (1979).
Ogawa, T. et al. Cold Spring Harb. Symp. quant. Biol. 43, 909–915 (1979).
Shibata, T. et al. Proc. natn. Acad. Sci. U.S.A. 76, 1638–1642 (1979).
McEntee, K., Weinstock, G. M. & Lehman, I. R. Proc. natn. Acad. Sci. U.S.A. 76, 2615–2619 (1979).
Shibata, T. et al. J. biol. Chem. 256, 7565–7572 (1981).
Shibata, T., Ohtani, T., Chang, P. K. & Ando, T. J. biol. Chem. 257, 370–376 (1982).
Cox, M. M. & Lehman, I. R. Proc. natn. Acad. Sci. U.S.A. 78, 3433–3437 (1981).
DasGupta, C., Shibata, T., Cunningham, R. P. & Radding, C. M. Cell 22, 437–446 (1980).
Cox, M. M. & Lehman, I. R. J. biol. Chem. 257, 8523–8532 (1982).
Soltis, D. A. & Lehman, I. R. J. biol. Chem. 258, 6073–6108 (1983).
West, S. C., Cassuto, E. & Howard-Flanders, P. Proc. natn. Acad. Sci. U.S.A. 78, 2100–2104 (1981).
DasGupta, C., Wu, A., Kahn, R., Cunningham, R. P. & Radding, C. M. Cell 25, 507–516 (1981).
West, S. C., Countryman, J. K. & Howard-Flanders, P. Cell 32, 817–829 (1983).
Gonda, D. K. & Radding, C. M. Cell 34, 647–654 (1983).
Holloman, W. K. & Radding, C. M. Proc. natn. Acad. Sci. U.S.A. 73, 3910–3914 (1976).
West, S. C., Cassuto, E. & Howard-Flanders, P. Nature 290, 29–33 (1981).
Wu, A. M., Bianchi, M., DasGupta, C. & Radding, C. M. Proc. natn. Acad. Sci. U.S.A. 80, 1256–1260 (1983).
Iwabuchi, M., Shibata, T., Ohtani, T., Natori, M. & Seno, T. J. biol. Chem. 258, 12394–12404 (1983).
McGavin, S. J. molec. Biol. 55, 293–298 (1971).
McGavin, S. Heredity 39, 15–25 (1977).
Wilson, J. H. Proc. natn. Acad. Sci. U.S.A. 76, 3641–3645 (1979).
Arnott, S., Bond, P. J., Seising, E. & Smith, P. C. J. Nucleic Acids Res. 3, 2459–2470 (1976).
DasGupta, C. & Radding, C. M. Proc. natn. Acad. Sci. U.S.A. 79, 762–766 (1982).
Bianchi, M. & Radding, C. M. Cell 35, 511–520 (1983).
Livneh, Z. & Lehman, I. R. Proc. natn. Acad. Sci. U.S.A. 79, 3171–3175 (1982).
Ohtani, T., Shibata, T., Iwabuchi, M., Nakagawa, K. & Ando, T. J. Biochem. (Tokyo) 91, 1767–1775 (1982).
Shibata, T., Ohtani, T., Iwabuchi, M. & Ando, T. J. biol. Chem. 257, 13981–13986 (1982).
Ohtani, T. et al. Nature 299, 86–94 (1982).
Wu, A. M., Kahn, R., DasGupta, C. & Radding, C. M. Cell 30, 37–44 (1982).
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Howard-Flanders, P., West, S. & Stasiak, A. Role of RecA protein spiral filaments in genetic recombination. Nature 309, 215–220 (1984). https://doi.org/10.1038/309215a0
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DOI: https://doi.org/10.1038/309215a0
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