Molecular views of recombination proteins and their control (original) (raw)

• Cox, M. M. Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu. Rev. Genet. 35, 53–82 (2001).
  CAS PubMed Google Scholar
• Ogawa, T., Yu, X., Shinohara, A. & Egelman, E. H. Similarity of the yeast Rad51 filament to the bacterial RecA filament. Science 259, 1896–1899 (1993). The similarity between E. coli RecA and yeast Rad51 was seen by electron microscopy and indicated that the nucleoprotein filament structure that is important for recombination in bacteria has been conserved throughout evolution.
  CAS PubMed Google Scholar
• Benson, F. E., Stasiak, A. & West, S. C. Purification and characterisation of the human RAD51 protein, an analogue of E. coli RecA. EMBO J. 13, 5764–5771 (1994).
  CAS PubMed Central PubMed Google Scholar
• Yu, X., Jacobs, S. A., West, S. C., Ogawa, T. & Egelman, E. H. Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc. Natl Acad. Sci. USA 98, 8419–8424 (2001).
  CAS PubMed Central PubMed Google Scholar
• Pellegrini, L. et al. Insights into DNA recombination from the structure of a RAD51–BRCA2 complex. Nature 420, 287–293 (2002). Describes the crystal structure of a RAD51–BRC fusion protein, and illustrates how the interaction with a BRC repeat might 'cap' RAD51 in the monomeric form and inhibit nucleoprotein-filament formation.
  CAS PubMed Google Scholar
• Mazin, A. V., Zaitseva, E., Sung, P. & Kowalczykowski, S. C. Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing. EMBO J. 19, 1148–1156 (2000).
  CAS PubMed Central PubMed Google Scholar
• McIlwraith, M. J. et al. Reconstitution of the strand invasion step of double-strand break repair using human RAD51, RAD52 and RPA proteins. J. Mol. Biol. 304, 151–164 (2000).
  CAS PubMed Google Scholar
• Benson, F. E., Baumann, P. & West, S. C. Synergistic actions of RAD51 and RAD52 in genetic recombination and DNA repair. Nature 391, 401–404 (1998).
  CAS PubMed Google Scholar
• Sung, P. Function of yeast Rad52 protein as a mediator between replication protein-A and the Rad51 recombinase. J. Biol. Chem. 272, 28194–28197 (1997).
  CAS PubMed Google Scholar
• New, J. H., Sugiyama, T., Zaitseva, E. & Kowalczykowski, S. C. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein-A. Nature 391, 407–410 (1998).
  CAS PubMed Google Scholar
• Shinohara, A. & Ogawa, T. Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature 391, 404–407 (1998).
  CAS PubMed Google Scholar
• Game, J. C. DNA double-strand breaks and the RAD50–RAD57 genes in Saccharomyces. Semin. Cancer Biol. 4, 73–83 (1993).
  CAS PubMed Google Scholar
• Milne, G. T. & Weaver, D. T. Dominant-negative alleles of RAD52 reveal a DNA repair recombination complex including Rad51 and Rad52. Genes Dev. 7, 1755–1765 (1993).
  CAS PubMed Google Scholar
• Shen, Z. Y., Cloud, K. G., Chen, D. J. & Park, M. S. Specific interactions between the human RAD51 and RAD52 proteins. J. Biol. Chem. 271, 148–152 (1996).
  CAS PubMed Google Scholar
• Mortensen, U. H., Bendixen, C., Sunjevaric, I. & Rothstein, R. DNA strand annealing is promoted by the yeast Rad52 protein. Proc. Natl Acad. Sci. USA 93, 10729–10734 (1996). The first evidence that Rad52 protein promotes single-strand-annealing reactions in vitro.
  CAS PubMed PubMed Central Google Scholar
• Sung, P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast Rad51 protein. Science 265, 1241–1243 (1994). Shows that Rad51 promotes strand-exchange reactions that are similar to those catalysed by E. coli RecA.
  CAS PubMed Google Scholar
• Baumann, P., Benson, F. E. & West, S. C. Human RAD51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87, 757–766 (1996).
  CAS PubMed Google Scholar
• Sung, P. & Stratton, S. A. Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis. J. Biol. Chem. 271, 27983–27986 (1996).
  CAS PubMed Google Scholar
• Morrison, C. et al. The essential functions of human RAD51 are independent of ATP hydrolysis. Mol. Cell. Biol. 19, 6891–6897 (1999).
  CAS PubMed Central PubMed Google Scholar
• Stark, J. M. et al. ATP hydrolysis by mammalian RAD51 has a key role during homology-directed DNA repair. J. Biol. Chem. 277, 20185–20194 (2002).
  CAS PubMed Google Scholar
• Petukhova, G., Stratton, S. & Sung, P. Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature 393, 91–94 (1998).
  CAS PubMed Google Scholar
• Van Komen, S., Petukhova, G., Sigurdsson, S., Stratton, S. & Sung, P. Superhelicity-driven homologous DNA pairing by yeast recombination factors Rad51 and Rad54. Mol. Cell 6, 563–572 (2000).
  CAS PubMed Google Scholar
• Mazin, A. V., Bornarth, C. J., Solinger, J. A., Heyer, W. -D. & Kowalczykowski, S. C. Rad54 protein is targeted to pairing loci by the Rad51 nucleoprotein filament. Mol. Cell 6, 583–592 (2000).
  CAS PubMed Google Scholar
• Solinger, J. A., Lutz, G., Sugiyama, T., Kowalczykowski, S. C. & Heyer, W. D. Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament. J. Mol. Biol. 307, 1207–1221 (2001).
  CAS PubMed Google Scholar
• Van Komen, S., Petukhova, G., Sigurdsson, S. & Sung, P. Functional cross-talk among Rad51, Rad54, and replication protein A in heteroduplex DNA joint formation. J. Biol. Chem. 277, 43578–43587 (2002).
  CAS PubMed Google Scholar
• Petukhova, G., Van Komen, S., Vergano, S., Klein, H. & Sung, P. Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation. J. Biol. Chem. 274, 29453–29462 (1999).
  CAS PubMed Google Scholar
• Tan, T. L. R. et al. Mouse RAD54 affects DNA conformation and DNA-damage-induced RAD51 foci formation. Curr. Biol. 9, 325–328 (1999).
  CAS PubMed Google Scholar
• Sigurdsson, S., Van Komen, S., Petukhovan, G. & Sung, P. Homologous DNA pairing by human recombination factors RAD51 and RAD54. J. Biol. Chem. 277, 42790–42794 (2002).
  CAS PubMed Google Scholar
• Solinger, J. A., Kiianitsa, K. & Heyer, W. D. Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments. Mol. Cell 10, 1175–1188 (2002).
  CAS PubMed Google Scholar
• Paques, F. & Haber, J. E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63, 349–404 (1999). A comprehensive review of recombination pathways and mechanisms in yeast.
  CAS PubMed Central PubMed Google Scholar
• Szostak, J. W., Orr-Weaver, T. L., Rothstein, R. J. & Stahl, F. W. The double-strand break repair model for recombination. Cell 33, 25–35 (1983). Describes the prototypic model for repair that is initiated by a double-strand break.
  CAS PubMed Google Scholar
• West, S. C. Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet. 31, 213–244 (1997).
  CAS PubMed Google Scholar
• Kleff, S., Kemper, B. & Sternglanz, R. Identification and characterization of yeast mutants and the gene for a cruciform cutting endonuclease. EMBO J. 11, 699–704 (1992).
  CAS PubMed Central PubMed Google Scholar
• White, M. F. & Lilley, D. M. J. The structure-selectivity and sequence-preference of the junction-resolving enzyme Cce1 of Saccharomyces cerevisiae. J. Mol. Biol. 257, 330–341 (1996).
  CAS PubMed Google Scholar
• Whitby, M. C. & Dixon, J. A new Holliday junction resolving enzyme from Schizosaccharomyces pombe that is homologous to Cce1 from Saccharomyces cerevisiae. J. Mol. Biol. 272, 509–522 (1997).
  CAS PubMed Google Scholar
• Oram, M., Keeley, A. & Tsaneva, I. Holliday junction resolvase in Schizosaccharomyces pombe has identical endonuclease activity to the Cce1 homolog Ydc2. Nucleic Acids Res. 26, 594–601 (1998).
  CAS PubMed Central PubMed Google Scholar
• Constantinou, A., Davies, A. A. & West, S. C. Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells. Cell 104, 259–268 (2001). Shows that mammalian cells have activities that promote coupled branch migration and Holliday junction resolution in reactions that are similar to those catalysed by E. coli RuvABC.
  Article CAS PubMed Google Scholar
• Constantinou, A., Chen, X. -B., McGowan, C. H. & West, S. C. Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities. EMBO J. 21, 5577–5585 (2002).
  CAS PubMed Central PubMed Google Scholar
• Boddy, M. N. et al. Mus81–Eme1 are essential components of a Holliday junction resolvase. Cell 107, 537–548 (2001).
  CAS PubMed Google Scholar
• Chen, X. B. et al. Human MUS81-associated endonuclease cleaves Holliday junctions in vitro. Mol. Cell 8, 1117–1127 (2001).
  CAS PubMed Google Scholar
• Kaliraman, V., Mullen, J. R., Fricke, W. M., Bastin-Shanower, S. A. & Brill, S. J. Functional overlap between Sgs1–Top3 and the Mms4–Mus81 endonuclease. Genes Dev. 15, 2730–2740 (2001).
  CAS PubMed Central PubMed Google Scholar
• Doe, C. L., Ahn, J. S., Dixon, J. & Whitby, M. C. Mus81–Eme1 and Rqh1 involvement in processing stalled and collapsed replication forks. J. Biol. Chem. 277, 32753–32759 (2002).
  CAS PubMed Google Scholar
• Van Dyck, E., Hajibagheri, N. M. A., Stasiak, A. & West, S. C. Visualisation of human RAD52 protein and its complexes with RAD51 and DNA. J. Mol. Biol. 284, 1027–1038 (1998).
  CAS PubMed Google Scholar
• Stasiak, A. Z. et al. The human RAD52 protein exists as a heptameric ring. Curr. Biol. 10, 337–340 (2000).
  CAS PubMed Google Scholar
• Shinohara, A., Shinohara, M., Ohta, T., Matsuda, S. & Ogawa, T. Rad52 forms ring structures and cooperates with RPA in single-strand DNA annealing. Genes Cells 3, 145–156 (1998).
  CAS PubMed Google Scholar
• Parsons, C. A., Baumann, P., Van Dyck, E. & West, S. C. Precise binding to single-stranded DNA termini by RAD52 protein. EMBO J. 19, 4175–4181 (2000).
  CAS PubMed Central PubMed Google Scholar
• Kagawa, W., Kurumizaka, H., Ikawa, S., Yokoyama, S. & Shibata, T. Homologous pairing promoted by the human RAD52 protein. J. Biol. Chem. 276, 35201–35208 (2001).
  CAS PubMed Google Scholar
• Park, M. S., Ludwig, D. L., Stigger, E. & Lee, S. H. Physical interaction between human RAD52 and RPA is required for homologous recombination in mammalian cells. J. Biol. Chem. 271, 18996–19000 (1996).
  CAS PubMed Google Scholar
• Kagawa, W. et al. Crystal structure of the homologous-pairing domain from the human RAD52 recombinase in the undecameric form. Mol. Cell 10, 359–371 (2002).
  CAS PubMed Google Scholar
• Singleton, M. R., Wentzell, L. M., Liu, Y., West, S. C. & Wigley, D. B. Structure of the single-strand annealing domain of human RAD52 protein. Proc. Natl Acad. Sci. USA 99, 13492–13497 (2002). References 49 and 50 present the X-ray crystal structure of the single-strand-annealing domain of human RAD52.
  CAS PubMed PubMed Central Google Scholar
• Singleton, M. R., Sawaya, M. R., Ellenberger, T. & Wigley, D. B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101, 589–600 (2000).
  CAS PubMed Google Scholar
• Haaf, T., Golub, E. I., Reddy, G., Radding, C. M. & Ward, D. C. Nuclear foci of mammalian RAD51 recombination protein in somatic cells after DNA damage and its localization in synaptonemal complexes. Proc. Natl Acad. Sci. USA 92, 2298–2302 (1995).
  CAS PubMed PubMed Central Google Scholar
• Scully, R. et al. Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. Cell 90, 425–435 (1997).
  CAS PubMed Google Scholar
• Liu, Y. & Maizels, N. Coordinated response of mammalian RAD51 and RAD52 to DNA damage. EMBO Rep. 1, 85–90 (2000).
  PubMed Central PubMed Google Scholar
• Lisby, M., Rothstein, R. & Mortensen, U. H. Rad52 forms DNA repair and recombination centers during S phase. Proc. Natl Acad. Sci. USA 98, 8276–8282 (2001).
  CAS PubMed PubMed Central Google Scholar
• Essers, J. et al. Nuclear dynamics of RAD52 group homologous recombination proteins in response to DNA damage. EMBO J. 21, 2030–2037 (2002).
  CAS PubMed Central PubMed Google Scholar
• Raderschall, E., Golub, E. I. & Haaf, T. Nuclear foci of mammalian recombination proteins are located at single-stranded DNA regions formed after DNA damage. Proc. Natl Acad. Sci. USA 96, 1921–1926 (1999).
  CAS PubMed PubMed Central Google Scholar
• Scully, R. et al. Association of BRCA1 with RAD51 in mitotic and meiotic cells. Cell 88, 265–275 (1997).
  CAS PubMed Google Scholar
• Chen, J. J. et al. Stable interaction between the products of the BRCA1 and BRCA2 tumor suppressor genes in mitotic and meiotic cells. Mol. Cell 2, 317–328 (1998). References 58 and 59 show the colocalization of RAD51 recombinase with the BRCA1 and BRCA2 tumour suppressors, leading to the concept that certain inheritable breast cancers might be due to defects in repair by homologous recombination.
  CAS PubMed Google Scholar
• Yuan, S. -S. F. et al. BRCA2 is required for ionizing radiation-induced assembly of RAD51 complex in vivo. Cancer Res. 59, 3547–3551 (1999).
  CAS PubMed Google Scholar
• Godthelp, B. C., Artwert, F., Joenje, H. & Zdzienicka, M. Z. Impaired DNA damage-induced nuclear RAD51 foci formation uniquely characterizes Fanconi anemia group D1. Oncogene 21, 5002–5005 (2002).
  CAS PubMed Google Scholar
• Tashiro, S. et al. S phase specific formation of the human RAD51 protein nuclear foci in lymphocytes. Oncogene 12, 2165–2170 (1996).
  CAS PubMed Google Scholar
• Tarsounas, M., Davies, D. & West, S. C. BRCA2-dependent and independent formation of RAD51 nuclear foci. Oncogene 22, 1115–1122 (2003).
  CAS PubMed Google Scholar
• Sharan, S. K. et al. Embryonic lethality and radiation hypersensitivity mediated by RAD51 in mice lacking BRCA2. Nature 386, 804–810 (1997).
  CAS PubMed Google Scholar
• Wong, A. K. C., Pero, R., Ormonde, P. A., Tavtigian, S. V. & Bartel, P. L. RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene BRCA2. J. Biol. Chem. 272, 31941–31944 (1997).
  CAS PubMed Google Scholar
• Moynahan, M. E., Chiu, J. W., Koller, B. H. & Jasin, M. BRCA1 controls homology-directed DNA repair. Mol. Cell 4, 511–518 (1999).
  CAS PubMed Google Scholar
• Moynahan, M. E., Pierce, A. J. & Jasin, M. BRCA2 is required for homology-directed repair of chromosomal breaks. Mol. Cell 7, 263–272 (2001).
  CAS PubMed Google Scholar
• Xia, F. et al. Deficiency of human BRCA2 leads to impaired homologous recombination but maintains normal nonhomologous end joining. Proc. Natl Acad. Sci. USA 98, 8644–8649 (2001). References 67 and 68 provide the first direct evidence that BRCA2 -defective cells are compromised in their ability to promote double-strand-break repair by homologous recombination.
  CAS PubMed PubMed Central Google Scholar
• Xu, X. et al. Centrosome amplification and a defective G2–M cell cycle checkpoint induce genetic instability in BRCA1 exon 11 isoform-deficient cells. Mol. Cell 3, 389–395 (1999).
  CAS PubMed Google Scholar
• Yu, V. P. C. C. et al. Gross chromosomal rearrangements and genetic exchange between non-homologous chromosomes following BRCA2 inactivation. Genes. Dev. 14, 1400–1406 (2000).
  CAS PubMed Central PubMed Google Scholar
• Rahman, N. & Stratton, M. R. The genetics of breast cancer susceptibility. Annu. Rev. Genet. 32, 95–121 (1998).
  CAS PubMed Google Scholar
• Welcsh, P. L. & King, M. C. BRCA1 and BRCA2 and the genetics of breast and ovarian cancer. Hum. Mol. Genet. 10, 705–713 (2001).
  CAS PubMed Google Scholar
• Kerr, P. & Ashworth, A. New complexities for BRCA1 and BRCA2. Curr. Biol. 11, R668–R676 (2001).
  CAS PubMed Google Scholar
• Wang, Y. et al. BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14, 927–939 (2000).
  CAS PubMed Central PubMed Google Scholar
• Anderson, S. E., Schlegel, B. P., Nakajima, T., Wolpin, E. S. & Parvin, J. D. BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nature Genet. 19, 254–256 (1998).
  CAS PubMed Google Scholar
• Yarden, R. I. & Brody, L. C. BRCA1 interacts with components of the histone deacetylase complex. Proc. Natl Acad. Sci. USA 96, 4983–4988 (1999).
  CAS PubMed PubMed Central Google Scholar
• Zhong, Q. et al. Association of BRCA1 with the RAD50–MRE11–p95 complex and the DNA damage response. Science 285, 747–750 (1999).
  CAS PubMed Google Scholar
• Bochar, D. A. et al. BRCA1 is associated with a human SWI/SNF-related complex: linking chromatin remodeling to breast cancer. Cell 102, 257–265 (2000).
  CAS PubMed Google Scholar
• Marmorstein, L. Y. et al. A human BRCA2 complex containing a structural DNA binding component influences cell cycle progression. Cell 104, 247–257 (2001).
  CAS PubMed Google Scholar
• Chiba, N. & Parvin, J. D. Redistribution of BRCA1 among four different protein complexes following replication blockage. J. Biol. Chem. 276, 38549–38554 (2001).
  CAS PubMed Google Scholar
• Wu, L. C. et al. Identification of a RING protein that can interact in vivo with the BRCA1 gene product. Nature Genet. 14, 430–440 (1996).
  CAS PubMed Google Scholar
• Ruffner, H., Joazeiro, C. A. P., Hemmati, D., Hunter, T. & Verma, I. M. Cancer-predisposing mutations within the RING domain of BRCA1: loss of ubiquitin protein ligase activity and protection from radiation hypersensitivity. Proc. Natl Acad. Sci. USA 98, 5134–5139 (2001).
  CAS PubMed PubMed Central Google Scholar
• Mallery, D. L., Vandenberg, C. J. & Hiom, K. Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. EMBO J. 21, 6755–6762 (2002).
  CAS PubMed Central PubMed Google Scholar
• Baer, R. & Ludwig, T. The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity. Curr. Opin. Genet. Dev. 12, 86–91 (2002).
  CAS PubMed Google Scholar
• D'Andrea, A. D. & Grompe, M. The Fanconi anaemia/BRCA pathway. Nature Rev. Cancer 3, 23–34 (2002).
  Google Scholar
• Grompe, M. & D'Andrea, A. D. Fanconi anemia and DNA repair. Hum. Mol. Genet. 10, 2253–2259 (2001).
  CAS PubMed Google Scholar
• Joenje, H. & Patel, K. J. The emerging genetic and molecular basis of Fanconi anaemia. Nature Rev. Genet. 2, 446–457 (2001).
  CAS PubMed Google Scholar
• Garcia-Higuera, I. et al. Interaction of the Fanconi anemia proteins and BRCA1 in a common pathway. Mol. Cell 7, 249–262 (2001). The first indication of the inter-relationship between Fanconi anaemia and BRCA gene products.
  CAS PubMed Google Scholar
• Ekblad, C. M. S. et al. Characterisation of the BRCT domains of the breast cancer susceptibility gene product BRCA1. J. Mol. Biol. 320, 431–442 (2002).
  CAS PubMed Google Scholar
• Williams, R. S., Green, R. & Glover, J. N. M. Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. Nature Struct. Biol. 8, 838–842 (2001).
  CAS PubMed Google Scholar
• Cantor, S. B. et al. BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. Cell 105, 149–160 (2001).
  CAS PubMed Google Scholar
• Bork, P., Blomberg, N. & Nilges, M. Internal repeats in the BRCA2 protein sequence. Nature Genet. 13, 22–23 (1996).
  CAS PubMed Google Scholar
• Chen, P. L. et al. The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment. Proc. Natl Acad. Sci. USA 95, 5287–5292 (1998).
  CAS PubMed PubMed Central Google Scholar
• Takata, M. et al. Conserved domains in the chicken homologue of BRCA2. Oncogene 21, 1130–1134 (2002).
  CAS PubMed Google Scholar
• Kojic, M., Kostrub, C. F., Buchman, A. R. & Holloman, W. K. BRCA2 homolog required for proficiency in DNA repair, recombination, and genome stability in Ustilago maydis. Mol. Cell 10, 683–691 (2002). A BRCA2-like protein found in a smut fungus provides evidence for the universality of BRCA2 and its potential role in the control of RAD51 recombinase.
  CAS PubMed Google Scholar
• Chen, C. F., Chen, P. L., Zhong, Q., Sharp, Z. D. & Lee, W. H. Expression of BRC repeats in breast cancer cells disrupts the BRCA2–RAD51 complex and leads to radiation hypersensitivity and loss of G2/M checkpoint control. J. Biol. Chem. 274, 32931–32935 (1999).
  CAS PubMed Google Scholar
• Davies, A. A. et al. Role of BRCA2 in control of the RAD51 recombination and DNA repair protein. Mol. Cell 7, 273–282 (2001). The first indication that interactions between RAD51 and a BRC repeat could block nucleoprotein-filament formation and thereby inhibit recombinase activity.
  CAS PubMed Google Scholar
• Cortez, D., Wang, Y., Qin, J. & Elledge, S. J. Requirement of ATM-dependent phosphorylation of BRCA1 in the DNA damage response to double-strand breaks. Science 286, 1162–1166 (1999).
  CAS PubMed Google Scholar
• Yuan, Z. M. et al. Regulation of RAD51 function by c-Abl in response to DNA damage. J. Biol. Chem. 273, 3799–3802 (1998).
  CAS PubMed Google Scholar
• Chen, G. et al. Radiation-induced assembly of RAD51 and RAD52 recombination complex requires ATP and c-Abl. J. Biol. Chem. 274, 12748–12752 (1999).
  CAS PubMed Google Scholar
• Saintigny, Y., Dumay, A., Lambert, S. & Lopez, B. S. A novel role for the Bcl-2 protein family: specific suppression of the RAD51 recombination pathway. EMBO J. 20, 2596–2607 (2001).
  CAS PubMed Central PubMed Google Scholar
• Yang, H. J. et al. BRCA2 function in DNA binding and recombination from a BRCA2–DSS1–ssDNA structure. Science 297, 1837–1848 (2002). Provided the first high-resolution structure of a segment of BRCA2 and showed that BRCA2 has the ability to bind DNA.
  CAS PubMed Google Scholar
• Marston, N. J. et al. Interaction between the product of the breast cancer susceptibility gene BRCA2 and DSS1, a protein functionally conserved from yeast to mammals. Mol. Cell. Biol. 19, 4633–4642 (1999).
  CAS PubMed Central PubMed Google Scholar
• Howlett, N. G. et al. Biallelic inactivation of BRCA2 in Fanconi anemia. Science 297, 606–609 (2002). Showed that the Fanconi anaemia D1 gene ( FANCD1 ) is the same as BRCA2.
  CAS PubMed Google Scholar
• Liang, F., Han, M. G., Romanienko, P. J. & Jasin, M. Homology-directed repair is a major double-strand break repair pathway in mammalian cells. Proc. Natl Acad. Sci. USA 95, 5172–5177 (1998).
  CAS PubMed PubMed Central Google Scholar
• Takata, M. et al. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J. 17, 5497–5508 (1998).
  CAS PubMed Central PubMed Google Scholar
• Essers, J. et al. Homologous and non-homologous recombination differentially affect DNA damage repair in mice. EMBO J. 19, 1703–1710 (2000).
  CAS PubMed Central PubMed Google Scholar
• Smith, G. C. M. & Jackson, S. P. The DNA-dependent protein kinase. Genes Dev. 13, 916–934 (1999).
  CAS PubMed Google Scholar
• Chu, G. Double-strand break repair. J. Biol. Chem. 272, 24097–24100 (1997).
  CAS PubMed Google Scholar
• Critchlow, S. E. & Jackson, S. P. DNA end-joining: from yeast to man. Trends Biochem. Sci. 23, 394–398 (1998).
  CAS PubMed Google Scholar
• Kanaar, R., Hoeijmakers, J. H. J. & van Gent, D. C. Molecular mechanisms of DNA double-strand break repair. Trends Cell Biol. 8, 483–489 (1998).
  CAS PubMed Google Scholar
• Dynan, W. S. & Yoo, S. Interaction of Ku protein and DNA-dependent protein kinase catalytic subunit with nucleic acids. Nucleic Acids Res. 26, 1551–1559 (1998).
  CAS PubMed Central PubMed Google Scholar
• Walker, J. R., Corpina, R. A. & Goldberg, J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 412, 607–614 (2001).
  CAS PubMed Google Scholar
• Hanakahi, L. A., Bartlet-Jones, M., Chappell, C., Pappin, D. & West, S. C. Binding of inositol phosphate to DNA-PK and stimulation of double-strand break repair. Cell 102, 721–729 (2000).
  CAS PubMed Google Scholar
• Hanakahi, L. A. & West, S. C. Specific interaction of IP6 with human Ku70/80, the DNA-binding subunit of DNA-PK. EMBO J. 21, 2038–2044 (2002).
  CAS PubMed Central PubMed Google Scholar
• Ma, Y. M. & Lieber, M. R. Binding of inositol hexakisphosphate (IP6) to Ku but not to DNA-PKcs . J. Biol. Chem. 277, 10756–10759 (2002).
  CAS PubMed Google Scholar
• Odom, A. R., Stahlberg, A., Wente, S. R. & York, J. D. A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. Science 287, 2026–2029 (2000).
  CAS PubMed Google Scholar
• York, J. D., Odom, A. R., Murphy, R., Ives, E. B. & Wente, S. R. A phospholipase C-dependent inositol polyphosphate kinase pathway required for efficient messenger RNA export. Science 285, 96–100 (1999).
  CAS PubMed Google Scholar
• Steger, D. J., Haswell, E. S., Miller, A. L., Wente, S. R. & O'Shea, E. K. Regulation of chromatin remodelling by inositol polyphosphates. Science 299, 114–116 (2003).
  CAS PubMed Google Scholar
• Shen, X., Xiao, H., Ranallo, R., Wu, W. -H. & Wu, C. Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates. Science 299, 112–114 (2003).
  CAS PubMed Google Scholar
• Yamada, K. et al. Crystal structure of the RuvA–RuvB complex: a structural basis for the Holliday junction migrating motor machinery. Mol. Cell 10, 671–681 (2002).
  CAS PubMed Google Scholar
• Parsons, C. A., Stasiak, A., Bennett, R. J. & West, S. C. Structure of a multisubunit complex that promotes DNA branch migration. Nature 374, 375–378 (1995). The first visualization of the E. coli RuvAB–Holliday-junction complex, which led to the proposal of a model for branch migration mediated by two opposing motor proteins.
  CAS PubMed Google Scholar
• Rafferty, J. B. et al. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science 274, 415–421 (1996).
  CAS PubMed Google Scholar
• Hargreaves, D. et al. Crystal structure of E. coli RuvA with bound DNA Holliday junction at 6Å resolution. Nature Struct. Biol. 5, 441–446 (1998).
  CAS PubMed Google Scholar
• Roe, S. M. et al. Crystal structure of an octameric RuvA–Holliday junction complex. Mol. Cell 2, 361–372 (1998).
  CAS PubMed Google Scholar
• Ariyoshi, M., Nishino, T., Iwasaki, H., Shinagawa, H. & Morikawa, K. Crystal structure of the Holliday junction DNA in complex with a single RuvA tetramer. Proc. Natl Acad. Sci. USA 97, 8257–8262 (2000).
  CAS PubMed Central PubMed Google Scholar
• Yamada, K. et al. Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8. Proc. Natl Acad. Sci. USA 98, 1442–1447 (2001).
  CAS PubMed PubMed Central Google Scholar
• Ingleston, S. M., Sharples, G. J. & Lloyd, R. G. The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome. EMBO J. 19, 6266–6274 (2000).
  CAS PubMed Central PubMed Google Scholar
• Whitby, M. C., Bolt, E. L., Chan, S. N. & Lloyd, R. G. Interactions between RuvA and RuvC at Holliday junctions: inhibition of junction cleavage and formation of a RuvA–RuvC–DNA complex. J. Mol. Biol. 264, 878–890 (1996).
  CAS PubMed Google Scholar
• van Gool, A. J., Shah, R., Mézard, C. & West, S. C. Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli. EMBO J. 17, 1838–1845 (1998).
  CAS PubMed Central PubMed Google Scholar
• Interthal, H. & Heyer, W. D. MUS81 encodes a novel helix-hairpin-helix protein involved in the response to UV- and methylation-induced DNA damage in Saccharomyces cerevisiae. Mol. Gen. Genet. 263, 812–827 (2000).
  CAS PubMed Google Scholar
• Boddy, M. N. et al. Damage tolerance protein Mus81 associates with the FHA1 domain of checkpoint kinase Cds1. Mol. Cell. Biol. 20, 8758–8766 (2000).
  CAS PubMed Central PubMed Google Scholar
• Mullen, J. R., Kaliraman, V., Ibrahim, S. S. & Brill, S. J. Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae. Genetics 157, 103–118 (2001).
  CAS PubMed Central PubMed Google Scholar
• West, S. C. The RuvABC proteins and Holliday junction processing in Escherichia coli. J. Bacteriol. 178, 1237–1241 (1996).
  CAS PubMed Central PubMed Google Scholar
• de los Santos, T., Loidl, J., Larkin, B. & Hollingsworth, N. M. A role for MMS4 in the processing of recombination intermediates during meiosis in Saccharomyces cerevisiae. Genetics 159, 1511–1525 (2001).
  CAS PubMed Central PubMed Google Scholar
• Ranatunga, W. et al. Human RAD52 exhibits two modes of self-association. J. Biol. Chem. 276, 15876–15880 (2001).
  CAS PubMed Google Scholar
• Lloyd, J. A., Fiorget, A. L. & Knight, K. L. Correlation of biochemical properties with the oligomeric state of human RAD52 protein. J. Biol. Chem. 277, 46172–46178 (2002).
  CAS PubMed Google Scholar
• Houtsmuller, A. B. et al. Action of DNA repair endonuclease ERCC1/XPF in living cells. Science 284, 958–961 (1999).
  CAS PubMed Google Scholar
• West, S. C. Cross-links between Fanconi anaemia and BRCA2. DNA Repair (Amst.) 2, 281–284 (2003).
  Google Scholar