The Role of RecA Protein in Homologous Genetic Recombination

  • Michael M. Cox

Abstract

Homologous genetic recombination is the process by which genetic information is rearranged between chromosomes that possess similar sequences. This type of recombination is responsible, in prokaryotes, for DNA rearrangements that occur during transformation or conjugation, postreplication repair of DNA, and a number of other processes [1]. Additional roles have been identified in eukaryotic cells [1,2]. About 30 homologous recombination events occur somewhere in the human genome during each meiosis, scattered more or less randomly about the chromosomes [3]. In bacteria, the probability of recombination occurring in a given length of DNA is increased about 500-fold relative to human meiotic chromosomes. A recombination event takes at least 35 minutes in bacteria [4] and perhaps 8 to 10 times longer in fungi [5].

Keywords

Hydrolysis Migration Recombination Expense Pyrimidine 

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References

  1. 1.
    Radding, C.M. (1973) Annu. Rev. Genet. 7, 87–111.PubMedCrossRefGoogle Scholar
  2. 2.
    Radding, C.M. (1978) Annu. Rev. Biochem. 47, 847–880.PubMedCrossRefGoogle Scholar
  3. 3.
    Low, K.B. (1988) In The Recombination of Genetic Material, 1–21, Low, K.B., ed. Academic Press, San Diego.Google Scholar
  4. 4.
    Porter, R.D., McLaughlin, T., and Low, B. (1979) Cold Spring Harbor Symp. Quant. Biol. 43, 1043–1047.PubMedGoogle Scholar
  5. 5.
    Holliday, R. (1971) Nature 232, 233–236.Google Scholar
  6. 6.
    Szostak, J.M., Orr-Weaver, T.L., Rothstein, R.J., and Stahl, F.W. (1983) Cell 33, 25–35.PubMedCrossRefGoogle Scholar
  7. 7.
    Cox, M.M., and Lehman, I.R. (1987) Annu. Rev. Biochem. 56, 229–262.PubMedCrossRefGoogle Scholar
  8. 8.
    Das Gupta, C., Wu, A.M., Kahn, R., Cunningham, R.P., and Radding, C.M. (1981) Cell 25, 507–516.CrossRefGoogle Scholar
  9. 9.
    West, S.C., Cassuto, E., and Howard-Flanders, P. (1981) Proc. Natl. Acad. Sci. USA 78, 2100–2104.PubMedCrossRefGoogle Scholar
  10. 10.
    West, S.C., and Howard-Flanders, P. (1984) Cell 37, 683–691.PubMedCrossRefGoogle Scholar
  11. 11.
    Cox, M.M., and Lehman, I.R. (1982) J. Biol. Chem. 257, 8523–8532.PubMedGoogle Scholar
  12. 12.
    Flory, J., Tsang, S.S., and Muniyappa, K. (1984) Proc. Natl. Acad. Sci. USA 81, 7026–7030.PubMedCrossRefGoogle Scholar
  13. 13.
    Flory, J., and Radding, C.M. (1982) Cell 28, 747–756.PubMedCrossRefGoogle Scholar
  14. 14.
    Dunn, K., Chrysogelos, S., and Griffith, J. (1982) Cell 28, 757–765.PubMedCrossRefGoogle Scholar
  15. 15.
    Di Capua, E., Engel, A., Stasiak, A., and Koller, T. (1982) J. Mol. Biol. 157, 87–103.PubMedCrossRefGoogle Scholar
  16. 16.
    Williams, R.C., and Spengler, S.J. (1986) J. Mol. Biol. 187, 109–118.PubMedCrossRefGoogle Scholar
  17. 17.
    Stasiak, A., and Egelman, E.H. (1987) UCLA Symp. Mol. Cell. Biol., New Ser. 47, 619–628.Google Scholar
  18. 18.
    Griffith, J.D., and Harris, L.D. (1988) CRC Crit. Rev. Biochem. (Suppl.) 23, 543–586.Google Scholar
  19. 19.
    Kowalczykowski, S.C. (1987) Trends Biochem. Sci. 12, 141–145.CrossRefGoogle Scholar
  20. 20.
    Bianchi, M., Das Gupta, C., and Radding, C.M. (1983) Cell 34, 931–939.PubMedCrossRefGoogle Scholar
  21. 21.
    Chow, S.A., and Radding, C.M. (1985) Proc. Natl. Acad. Sci. USA 82, 5646–5650.PubMedCrossRefGoogle Scholar
  22. 22.
    Flory, S.S., Tsang, J., Muniyappa, K., Bianchi, M., Gordon, D., Kahn, R., Azhderian, E., Egner, C., Shaner, S., and Radding, C.M. (1984) Cold Spring Harbor Symp. Quant. Biol. 49, 513–523.PubMedGoogle Scholar
  23. 23.
    Riddles, P.W., and Lehman, I.R. (1985) J. Biol. Chem. 260, 165–169.PubMedGoogle Scholar
  24. 24.
    Schutte, B.C., and Cox, M.M. (1987) Biochemistry 26, 5616–5625.PubMedCrossRefGoogle Scholar
  25. 25.
    Schutte, B.C., and Cox, M.M. (1988) Biochemistry 27, 7886–7894.PubMedCrossRefGoogle Scholar
  26. 26.
    Register, J.C., Christiansen, G., and Griffith, J. (1987) J. Biol. Chem. 262, 12812–12820.PubMedGoogle Scholar
  27. 27.
    Das Gupta, C., Shibata, T., Cunningham, R.P., and Radding, C.M. (1980) Cell 22, 437–446.CrossRefGoogle Scholar
  28. 28.
    Cox, M.M., and Lehman, I.R. (1981) Proc. Natl. Acad. Sci. USA 78, 3433–3437.PubMedCrossRefGoogle Scholar
  29. 29.
    Honigberg, S.M., Gonda, D.K., Flory, J., and Radding, C.M. (1985) J. Biol. Chem. 260, 11845–11851.PubMedGoogle Scholar
  30. 30.
    West, S.C., Cassuto, E., and Howard-Flanders, P. (1981) Proc. Natl. Acad. Sci. USA 78, 6149–6153.PubMedCrossRefGoogle Scholar
  31. 31.
    Kahn, R., Cunningham, R.P., Das Gupta, C., and Radding, C.M. (1981) Proc. Natl. Acad. Sci. USA 78, 4786–4790.PubMedCrossRefGoogle Scholar
  32. 32.
    Cox, M.M., and Lehman, I.R. (1981) Proc. Natl. Acad. Sci. USA 78, 6018–6022.PubMedCrossRefGoogle Scholar
  33. 33.
    Wu, A.W., Kahn, R., Das Gupta, C., and Radding, C.M. (1982) Cell 30, 31–44.CrossRefGoogle Scholar
  34. 34.
    Leahy, M.C., and Radding, C.M. (1986) J. Biol. Chem. 261, 6954–6960.PubMedGoogle Scholar
  35. 35.
    Di Capua, E.D., and Müller, B. (1987) EMBO J. 6, 2493–2498.PubMedGoogle Scholar
  36. 36.
    Egelman, E.H., and Stasiak, A. (1986) J. Mol. Biol. 191, 677–697.PubMedCrossRefGoogle Scholar
  37. 37.
    Register, J.C., and Griffith, J. (1985) J. Biol. Chem. 260, 12308–12312.PubMedGoogle Scholar
  38. 38.
    Stasiak, A., Egelman, E.H., and Howard-Flanders, P. (1988) J. Mol. Biol. 202, 659–662.PubMedCrossRefGoogle Scholar
  39. 39.
    Brenner, S.L., Mitchell, R.S., Morrical, S.W., Neuendorf, S.K., Schutte, B.C., and Cox, M.M. (1987) J. Biol. Chem. 262, 4011–4016.PubMedGoogle Scholar
  40. 40.
    Leirmo, S., Harrison, C., Cayley, D.S., Burgess, R.R., and Record, M.T. Jr. (1987) Biochemistry 26, 2095–2101.PubMedCrossRefGoogle Scholar
  41. 41.
    Pugh, B.F., and Cox, M.M. (1988) J. Biol. Chem. 263, 76–83.PubMedGoogle Scholar
  42. 42.
    Cox, M.M., Soltis, D.A., Livneh, Z., and Lehman, I.R. (1983) J. Biol. Chem. 258, 2577–2585.PubMedGoogle Scholar
  43. 43.
    Kowalczykowski, S.C., Clow, J., and Krupp, R.A. (1987) Proc. Natl. Acad. Sci. USA 84, 3127–3131.PubMedCrossRefGoogle Scholar
  44. 44.
    Pugh, B.F., and Cox, M.M. (1987) J. Biol. Chem. 262, 1326–1336.PubMedGoogle Scholar
  45. 45.
    Pugh, B.F., and Cox, M.M. (1988) J. Mol. Biol. 203, 479–493.PubMedCrossRefGoogle Scholar
  46. 46.
    Lindsley, J.E., and Cox, M.M. (1989) J. Mol. Biol. 205, 695–711.PubMedCrossRefGoogle Scholar
  47. 47.
    Shaner, S.C., and Radding, C.M. (1987) J. Biol. Chem. 262, 9211–9219.PubMedGoogle Scholar
  48. 48.
    Pugh, B.F., and Cox, M.M. (1989) J. Mol. Biol. 205, 487–492.PubMedCrossRefGoogle Scholar
  49. 49.
    Stasiak, A., and Di Capua, E. (1982) Nature 299, 185–186.PubMedCrossRefGoogle Scholar
  50. 50.
    Chow, S.A., Honigberg, S.M., Bainton, R.J., and Radding, C.W. (1986) J. Biol. Chem. 261, 6961–6971.PubMedGoogle Scholar
  51. 51.
    Chow, S.A., Honigberg, S.M., and Radding, C.M. (1988) J. Biol. Chem. 263, 3335–3347.PubMedGoogle Scholar
  52. 52.
    Cassuto, E., and Howard-Flanders, P. (1986) Nucleic Acids Res. 14, 1149–1157.PubMedCrossRefGoogle Scholar
  53. 53.
    Blaho, J.A., and Wells, R.D. (1987) J. Biol. Chem. 262, 6082–6088.PubMedGoogle Scholar
  54. 54.
    Warner, R.C., and Tessman, I.T. (1978) In The Single-Stranded DNA Phages, 417, Denhardt, D.T., et al. (eds.) Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.Google Scholar
  55. 55.
    Yancey, S.D., and Porter, R.D. (1984) Mol. Gen. Genet. 193, 53–57.PubMedCrossRefGoogle Scholar
  56. 56.
    Salles, B., and Paoletti, C. (1983) Proc. Natl. Acad. Sci. USA 80, 65–69.PubMedCrossRefGoogle Scholar
  57. 57.
    Ganesan, A.K. (1974) J. Mol. Biol. 87, 103–119.PubMedCrossRefGoogle Scholar
  58. 58.
    Rupp, W.D., Wilde, C.E. III, Reno, D.L., and Howard-Flanders, P. (1971) J. Mol. Biol. 61, 25–44.PubMedCrossRefGoogle Scholar
  59. 59.
    West, S.C., Cassuto, E., and Howard-Flanders, P. (1981) Nature 294, 659–662.PubMedCrossRefGoogle Scholar
  60. 60.
    Livneh, Z., and Lehman, I.R. (1982) Proc. Natl. Acad. Sci. USA 79, 3171–3175.PubMedCrossRefGoogle Scholar
  61. 61.
    Das Gupta, C., and Radding, C.M. (1982) Proc. Natl. Acad. Sci. USA 79, 762–766.CrossRefGoogle Scholar
  62. 62.
    Howard-Flanders, P., West, S.C., and Stasiak, A. (1984) Nature 309, 215–219.PubMedCrossRefGoogle Scholar
  63. 63.
    McGavin, S.J. (1971) J. Mol. Biol. 55, 293–298.PubMedCrossRefGoogle Scholar
  64. 64.
    Wilson, J.H. (1979) Proc. Natl. Acad. Sci. USA 76, 3641–3645.PubMedCrossRefGoogle Scholar
  65. 65.
    Cox, M.M., Pugh, B.F., Schutte, B.C., Lindsley, J.E., Lee, J., and Morrical, S.W. (1987) UCLA Symp. Mol. Cell. Biol., New Ser., 47, 597–607.Google Scholar
  66. 66.
    Pugh, B.F., and Cox, M.M. (1987) J. Biol. Chem. 262, 1337–1343.PubMedGoogle Scholar
  67. 67.
    Christiansen, G., and Griffith, J. (1986) Proc. Natl. Acad. Sci. USA 83, 2066–2070.PubMedCrossRefGoogle Scholar
  68. 68.
    Neuendorf, S.K., and Cox, M.M. (1986) J. Biol. Chem. 261, 8276–8282.PubMedGoogle Scholar
  69. 69.
    Menetski, J.P., and Kowalczykowski, S.C. (1987) J. Biol. Chem. 262, 2093–2100.PubMedGoogle Scholar
  70. 70.
    Bianchi, M.E., and Radding, C.M. (1983) Cell 35, 511–520.PubMedCrossRefGoogle Scholar
  71. 71.
    Howard-Flanders, P., West, S.C., Cassuto, E., Hahn, T.R., and Egelman, E. (1987) UCLA Symp. Mol. Cell. Biol., New Ser. 47, 609–617.Google Scholar
  72. 72.
    Cox, M.M., Morrical, S.W., and Neuendorf, S.K. (1984) Cold Spring Harbor Symp. Quant. Biol. 49, 525–533.PubMedGoogle Scholar
  73. 73.
    Roman, L.J., and Kowalczykowski, S.C. (1986) Biochemistry 25, 7375–7385.PubMedCrossRefGoogle Scholar
  74. 74.
    Kolodner, R., Evans, D.H., and Morrison, P.T. (1987) Proc. Natl. Acad. Sci. USA 84, 5560–5564.PubMedCrossRefGoogle Scholar
  75. 75.
    Hsieh, P., Meyn, M.S., and Camerini-Otero, R.D. (1986) Cell 44, 885–894.PubMedCrossRefGoogle Scholar
  76. 76.
    Jencks, W.P. (1980) Adv. Enzymol. 51, 75–106.PubMedGoogle Scholar
  77. 77.
    Honigberg, S.M., and Radding, C.M. (1988) Cell 54, 525–532.PubMedCrossRefGoogle Scholar

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  • Michael M. Cox

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