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(NAS Colloquium) Links Between Recombination and Replication: Vital Roles of Recombination (2002)
Proceedings of the National Academy of Sciences (PNAS)

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223
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Colloquium on Links Between Recombination and Replication: Vital Roles of Recombination

24. Thacker, J. (1999) Trends Genet. 15, 166–168.

25. Thompson, L.H. & Schild, D. (1999) Biochimie 81, 87–105.

26. Jeggo, P.A. (1998) Radiat. Res. 150, 80–91.

27. Kanaar, R., Hoeijmakers, J.H. & van Gent, D.C. (1998) Trends Cell. Biol. 8, 483–489.

28. Bressan, D.A., Baxter, B.K. & Petrini, J.H. (1999) Mol. Cell. Biol. 19, 7681–7687.

29. Gu, Y., Jin, S., Gao, Y., Weaver, D.T. & Alt, F.W. (1997) Proc. Natl. Acad. Sci. USA 94, 8076–8081.

30. Ouyang, H., Nussenzweig, A., Kurimasa, A., da Costa Soares, V., Li, X., Cordon-Cardo, C., Li, W.-H., Cheong, N., Nussenzweig, M., Iliakis, G., et al. (1997) J. Exp. Med. 186, 921–929.

31. Essers, J., Hendriks, R.W., Swagemakers, S.M.A., Troelstra, C., de Wit, J., Bootsma, D., Hoeijmakers, J.H.J. & Kanaar, R. (1997) Cell 89, 195–204.

32. Essers, J., van Steeg, H., de Wit, J., Swagemakers, S.M., Vermeij, M., Hoeijmakers, J.H. & Kanaar, R. (2000) EMBO J. 19, 1703–1710.

33. Gao, Y., Chaudhuri, J., Zhu, C., Davidson, L., Weaver, D.T. & Alt, F.W. (1998) Immunity 9, 367–376.

34. Kadyk, L.C. & Hartwell, L.H. (1992) Genetics 132, 387–402.

35. Cheong, N., Wang, X., Wang, Y. & Iliakis, G. (1994) Mutat. Res. 314, 77–85.

36. Liu, N., Lamerdin, J.E., Tebbs, R.S., Schild, D., Tucker, J.D., Shen, M.R., Brookman, K.W., Siciliano, M.J., Walter, C.A., Fan, W., et al. (1998) Mol. Cell 1, 783–793.

37. Haber, J.E. (2000) Trends Genet. 16, 259–264.

38. Moore, J.K. & Haber, J.E. (1996) Mol. Cell. Biol. 16, 2164–2173.

39. Benjamin, M.B., Potter, H., Yandell, D.W. & Little, J.B. (1991) Proc. Natl. Acad. Sci. USA 88, 6652–6656.

40. Godwin, A.R., Bollag, R.J., Christie, D.M. & Liskay, R.M. (1994) Proc. Natl. Acad. Sci. USA 91, 12554–12558.

41. Moynahan, M.E. & Jasin, M. (1997) Proc. Natl. Acad. Sci. USA 94, 8988–8993.

42. Richardson, C., Moynahan, M.E. & Jasin, M. (1998) Genes Dev. 12, 3831–3842.

43. Richardson, C., Jasin, M., Dronkert, M.L., Beverloo, H.B., Johnson, R.D., Hoeijmakers, J.H., Kanaar, R., Moynahan, M.E., Chiu, J.W. & Koller, B.H. (2000) Nature (London) 405, 697–700.

44. Tan, T.L.R., Essers, J., Citterio, E., Swagemakers, S.M.A., De Wit, J., Benson, F.E., Hoeijmakers, J.H.J. & Kanaar, R. (1999) Curr. Biol. 9, 325–328.

45. Calderon, I.L., Contopoulou, C.R. & Mortimer, R.K. (1983) Curr. Genet. 7, 93–100.

46. Shinohara, A., Ogawa, H. & Ogawa, T. (1992) Cell 69, 457–470.

47. Haaf, T., Raderschall, E., Reddy, G., Ward, D.C., Radding, C.M. & Golub, E.I. (1999) J. Cell Biol. 144, 11–20.

48. Raderschall, E., Golub, E.I. & Haaf, T. (1999) Proc. Natl. Acad. Sci. USA 96, 1921–1926.

49. Tashiro, S., Walter, J., Shinohara, A., Kamada, N. & Cremer, T. (2000) J. Cell Biol. 150, 283–291.

50. Liu, Y. & Maizels, N. (2000) EMBO Rep. 1, 85–90.

51. Bishop, D.K., Ear, U., Bhattacharyya, A., Calderone, C., Beckett, M., Weichselbaum, R.R. & Shinohara, A. (1998) J. Biol. Chem. 273, 21482–21488.

52. Van Dyck, E., Stasiak, A.Z., Stasiak, A. & West, S.C. (1999) Nature (London) 398, 728–731.

53. Kunkel, T.A. (1999) Trends Genet. 15, 93–94.

54. Lindahl, T. (1993) Nature (London) 362, 709–715.

55. Flores Rozas, H. & Kolodner, R.D. (2000) Trends Biochem. Sci. 25, 196–200.

56. Haber, J.E. (1999) Trends Biochem. Sci. 24, 271–275.

57. Wyatt, M.D., Allan, J.M., Lau, A.Y., Ellenberger, T.E. & Samson, L.D. (1999) BioEssays 21, 668–676.

58. Kogoma, T. (1997) Microbiol. Mol. Biol. Rev. 61, 212–238.

59. Tsuzuki, T., Fujii, Y., Sakumi, K., Tominaga, Y., Nakao, K., Sekiguchi, M., Matsushiro, A., Yoshimura, Y. & Morita, T. (1996) Proc. Natl. Acad. Sci. USA 93, 6236–6240.

60. Xiao, Y. & Weaver, D.T. (1997) Nucleic Acids Res. 25, 2985–2991.

61. Griffin, C.S., Simpson, P.J., Wilson, C.R. & Thacker, J. (2000) Nat. Cell Biol. 2, 757–761.

62. Bollag, R.J., Waldman, A.S. & Liskay, R.M. (1989) Annu. Rev. Genet. 23, 199–225.

63. Painter, R.B. (1980) Mutat. Res. 70, 337–341.

64. Zwanenburg, T.S. & Natarajan, A.T. (1984) Cytogenet. Cell Genet. 38, 278–281.

65. Pinkel, D., Thompson, L.H., Gray, J.W. & Vanderlaan, M. (1985) Cancer Res. 45, 5795–5798.

66. Paques, F., Leung, W.Y. & Haber, J.E. (1998) Mol. Cell. Biol. 18, 2045–2054.

67. Dronkert, M.L., Beverloo, H.B., Johnson, R.D., Hoeijmakers, J.H., Jasin, M. & Kanaar, R. (2000) Mol. Cell. Biol. 20, 3147–3156.

68. Deng, C. & Capecchi, M.R. (1992) Mol. Cell. Biol. 12, 3365–3371.

69. Leung, W., Malkova, A. & Haber, J.E. (1997) Proc. Natl. Acad. Sci. USA 94, 6851–6856.

70. Liang, F., Romanienko, P.J., Weaver, D.T., Jeggo, P.A. & Jasin, M. (1996) Proc. Natl. Acad. Sci. USA 93, 8929–8933.

71. Darroudi, F. & Natarajan, A.T. (1987) Mutat. Res. 177, 149–160.

72. Kemp, L.M. & Jeggo, P.A. (1986) Mutat. Res. 166, 255–263.

73. Grawunder, U., Zimmer, D., Fugmann, S., Schwarz, K. & Lieber, M.R. (1998) Mol. Cell 2, 477–484.

74. Difilippantonio, M.J., Zhu, J., Chen, H.T., Meffre, E., Nussenzweig, M.C., Max, E.E., Ried, T. & Nussenzweig, A. (2000) Nature (London) 404, 510–514.

75. Gao, Y., Ferguson, D.O., Xie, W., Manis, J.P., Sekiguchi, J., Frank, K.M., Chaudhuri, J., Horner, J., DePinho, R.A. & Alt, F.W. (2000) Nature (London) 404, 897–900.

76. Sung, P. (1997) J. Biol. Chem. 272, 28194–28197.

77. Benson, F.E., Baumann, P. & West, S.C. (1998) Nature (London) 391, 401–404.

78. New, J.H., Sugiyama, T., Zaitseva, E. & Kowalczykowski, S.C. (1998) Nature (London) 391, 407–410.

79. Shinohara, A. & Ogawa, T. (1998) Nature (London) 391, 404–407.

80. Ivanov, E.L., Sugawara, N., Fishman-Lobell, J. & Haber, J.E. (1996) Genetics 142, 693–704.

81. Bartsch, S., Kang, L.E. & Symington, L.S. (2000) Mol Cell Biol. 20, 1194–1205.

82. Rijkers, T., van den Ouweland, J., Morolli, B., Rolink, A.G., Baarends, W.M., Van Sloun, P.P.H, Lohman, P.H.M. & Pastink, A. (1998) Mol. Cell. Biol. 18, 6423–6429.

83. Bezzubova, O., Shinohara, A., Mueller, R.G., Ogawa, H. & Buerstedde, J.M. (1993) Nucleic Acids Res. 21, 1577–1580.

84. Bezzubova, O.Y., Schmidt, H., Ostermann, K., Heyer, W.D. & Buerstedde, J.M. (1993) Nucleic Acids Res. 21, 5945–5949.

85. Usui, T., Ohta, T., Oshiumi, H., Tomizawa, J., Ogawa, H. & Ogawa, T. (1998) Cell 95, 705–716.

86. Wilson, S., Warr, N., Taylor, D.L. & Watts, F.Z. (1999) Nucleic Acids Res. 27, 2655–2661.

87. Stasiak, A.Z., Larquet, E., Stasiak, A., Muller, S., Engel, A., Van Dyck, E., West, S.C. & Egelman, E.H. (2000) Curr. Biol. 10, 337–340.

88. Bai, Y. & Symington, S. (1996) Genes Dev. 10, 2025–2037.

89. Ostermann, K., Lorentz, A. & Schmidt, H. (1993) Nucleic Acids Res. 21, 5940–5944.

90. Suto, K., Nagata, A., Murakami, H. & Okayama, H. (1999) Mol. Biol. Cell. 10, 3331–3343.

91. Hays, S.L., Firmenich, A.A. & Berg, P. (1995) Proc. Natl. Acad. Sci. USA 92, 6925–6929.

92. Johnson, R.D. & Symington, L.S. (1995) Mol. Cell. Biol. 15, 4843–4850.

93. Sung, P. (1997) Genes Dev. 11, 1111–1121.

94. Schild, D., Lio, Y.-C., Collins, D.W., Tsomondo, T. & Chen, D.J. (2000) J. Biol. Chem. 275, 16443–16449.

95. Braybrooke, J.P., Spink, K.G., Thacker, J. & Hickson, I.D. (2000) J. Biol. Chem. 257, 29100–29106.

96. Dosanjh, M.K., Collins, D.W., Fan, W., Lennon, G.G., Albala, J.S., Shen, Z. & Schild, D. (1998) Nucleic Acids Res. 26, 1179–1184.

97. Pittman, D.L., Cobb, J., Schimenti, K.J., Wilson, L.A., Cooper, D.M., Brignull, E., Handel, M.A. & Schimenti, J.C. (1998) Mol. Cell 1, 697–705.

98. Rice, M.C., Smith, S.T., Bullrich, F., Havre, P. & Kmiec, E.B. (1997) Proc. Natl. Acad. Sci. USA 94, 7417–7422.

99. Shinohara, A., Ogawa, H., Matsuda, Y., Ushio, N., Ikeo, K. & Ogawa, T. (1993) Nat. Genet. 4, 239–243.

100. Mortensen, U.H., Bendixen, C., Sunjevaric, I. & Rothstein, R. (1996) Proc. Natl. Acad. Sci. USA 93, 10729–10734.

101. Sugawara, N., Ira, G. & Haber, J.E. (2000) Mol. Cell. Biol. 20, 5300–5309.

102. Chen, J., Silver, D.P., Walpita, D., Cantor, S.B., Gazdar, A.F., Tomlinson, G., Couch, F.J., Weber, B. L, Ashley, T., Livingston, D.M. & Scully, R. (1998) Mol. Cell 2, 317–328.

103. Chen, P.L., Chen, C.F., Chen, Y., Xiao, J., Sharp, Z.D. & Lee, W.H. (1998) Proc. Natl. Acad. Sci. USA 95, 5287–5292.

104. Katagiri, T., Saito, H., Shinohara, A., Ogawa, H., Kamada, N., Nakamura, Y. & Miki, Y. (1998) Genes Chromosomes Cancer 21, 217–222.

105. Sharan, S.K. & Bradley, A. (1997) Genomics 40, 234–241.

106. Rubin, G.M., Yandell, M.D., Wortman, J.R., Gabor Miklos, G.L., Nelson, C.R., Hariharan, I.K., Fortini, M.E., Li, P.W., Apweiler, R., Fleischmann, W., et al. (2000) Science 287, 2204–2215.

107. Monteiro, A.N. (2000) Trends Biochem. Sci. 25, 469–474.

108. Bhattacharyya, A., Ear, U.S., Koller, B.H., Weichselbaum, R.R. & Bishop, D.K. (2000) J. Biol. Chem. 275, 23899–23903.

109. Moynahan, M.E., Chiu, J.W., Koller, B.H. & Jasin, M. (1999) Mol. Cell 4, 511–518.

110. Wang, Y., Cortez, D., Yazdi, P., Neff, N., Elledge, S.J. & Qin, J. (2000) Genes Dev. 14, 927–939.

111. Yu, V.P., Koehler, M., Steinlein, C., Schmid, M., Hanakahi, L.A., van Gool, A.J., West, S.C. & Venkitaraman, A.R. (2000) Genes Dev. 14, 1400–1406.

112. Patel, K.J., Vu, V.P., Lee, H., Corcoran, A., Thistlethwaite, F.C., Evans, M.J., Colledge, W.H., Friedman, L.S., Ponder, B.A. & Venkitaraman, A.R. (1998) Mol. Cell 1, 347–357.

113. Yuan, S.S., Lee, S.Y., Chen, G., Song, M., Tomlinson, G.E. & Lee, E.Y. (1999) Cancer Res. 59, 3547–3551.

114. Bashkirov, V.I., King, J.S., Bashkirova, E.V., Schmuckli Maurer, J. & Heyer, W.D. (2000) Mol. Cell. Biol. 20, 4393–4404.

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Front Matter (R1-R3)
Links between recombination and replication: Vital roles of recombination (8172-8172)
Historical overview: Searching for replication help in all of the rec places (8173-8180)
Rescue of arrested replication forks by homologous recombination (8181-8188)
Circles: The replication-recombination-chromosome segregation connection (8189-8195)
Participation of recombination proteins in rescue of arrested replication forks in UV-irradiated Escherichia coli need not involve recombination (8196-8202)
Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant (8203-8210)
RecA protein promotes the regression of stalled replication forks in vitro (8211-8218)
Topological challenges to DNA replication: Conformations at the fork (8219-8226)
Rescue of stalled replication forks by RecG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation (8227-8234)
Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled (8235-8240)
Single-strand interruptions in replicating chromosomes cause double-strand breaks (8241-8246)
Handoff from recombinase to replisome: Insights from transportation (8247-8254)
Break-induced replication: A review and an example in budding yeast (8255-8262)
Links between replication and recombination in Saccharomyces cerevisiae: A hypersensitive requirement for homologous recombination in the absence of Rad27 activity (8263-8269)
Evidence that replication fork components catalyze establishment of cohesion between sister chromatids (8270-8275)
Rad52 forms DNA repair and recombination centers during S phase (8276-8282)
A yeast gene, MGS1, encoding a DNA-dependent AAA+ ATPase is required to maintain genome stability (8283-8289)
The tight linkage between DNA replication and double-strand break repair in bacteriophage T4 (8290-8297)
Mediator proteins orchestrate enzyme-ssDNA assembly during T4 recombination-dependent DNA replication and repair (8298-8305)
Two recombination-dependent DNA replication pathways of bacteriophage T4, and their roles in mutagenesis and horizontal gene transfer (8306-8311)
Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: A versatile couple with roles in replication and recombination (8312-8318)
Instability of repetitive DNA sequences: The role of replication in multiple mechanisms (8319-8325)
Repeat expansion by homologous recombination in the mouse germ line at palindromic sequences (8326-8333)
Stationary-phase mutation in the bacterial chromosome: Recombination protein and DNA polymerase IV dependence (8334-8341)
Managing DNA polymerases: Coordinating DNA replication, DNA repair, and DNA recombination (8342-8349)
Roles of DNA polymerases V and II in SOS-induced error-prone and error-free repair in Escherichia coli (8350-8354)
Accuracy of lesion bypass by yeast and human DNA polymerase n (8355-8360)
ATP bound to the orgin recognition complex is important for preRC formation (8361-8367)
Creating a dynamic picture of the sliding clamp during T4 DNA polymerases holoenzyme assembly by using fluorescence resonance energy transfer (8368-8375)
Interaction of the ß sliding clamp with MutS, ligase, and DNA polymerase I (8376-8380)
Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase (8381-8387)
Homologous DNA recombination in vertebrate cells (8388-8394)
Meiotic recombination and chromosome segregation in Schizosaccharomyces pombe (8395-8402)
Manipulating the mammalian genome by homologous recombination (8403-8410)
Assembly of RecA-like recombinases: Distinct roles for mediator proteins in mitosis and meiosis (8411-8418)
Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA (8419-8424)
Homologous genetic recombination as an intrinsic dynamic property of a DNA structure induced by RecA/Rad51-family proteins: A possible advantage of DNA over RNA as genomic material (8425-8432)
The synaptic activity of HsDmc1, a human reccombination protein specific to meiosis (8433-8439)
Complex formation by the human RAD51C and XRCC3 recombination repair proteins (8440-8446)
Rad54 protein stimulates the postsynaptic phase of Rad51 protein-mediated DNA strand exchange (8447-8453)
The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA (8454-8460)
DNA replication meets genetic exchange: Chromosomal damage and its repair by homologous recombination (8461-8468)
Colloquium Program (8469-8471)