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Volumn 393, Issue 5, 2009, Pages 1007-1012

Cancer-Associated Mutations in BRC Domains of BRCA2 Affect Homologous Recombination Induced by Rad51

Author keywords

BRC domains; BRCA2; homologous recombination; mutations; Rad51

Indexed keywords

BRCA2 PROTEIN; DOUBLE STRANDED DNA; RAD51 PROTEIN; SINGLE STRANDED DNA;

EID: 70350034015     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.011     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 33749037701 scopus 로고    scopus 로고
    • Mechanism of homologous recombination: mediators and helicases take on regulatory functions
    • Sung P., and Klein H. Mechanism of homologous recombination: mediators and helicases take on regulatory functions. Nat. Rev., Mol. Cell Biol. 7 (2006) 739-750
    • (2006) Nat. Rev., Mol. Cell Biol. , vol.7 , pp. 739-750
    • Sung, P.1    Klein, H.2
  • 3
    • 36949026476 scopus 로고    scopus 로고
    • BRCA2: a universal recombinase regulator
    • Thorslund T., and West S.C. BRCA2: a universal recombinase regulator. Oncogene 26 (2007) 7720-7730
    • (2007) Oncogene , vol.26 , pp. 7720-7730
    • Thorslund, T.1    West, S.C.2
  • 4
    • 14144253362 scopus 로고    scopus 로고
    • Cancer: catalyst of a catalyst
    • Kowalczykowski S.C. Cancer: catalyst of a catalyst. Nature 433 (2005) 591-592
    • (2005) Nature , vol.433 , pp. 591-592
    • Kowalczykowski, S.C.1
  • 6
    • 0035030368 scopus 로고    scopus 로고
    • Breast cancer genetics: what we know and what we need
    • Nathanson K.L., Wooster R., and Weber B.L. Breast cancer genetics: what we know and what we need. Nat. Med. 7 (2001) 552-556
    • (2001) Nat. Med. , vol.7 , pp. 552-556
    • Nathanson, K.L.1    Wooster, R.2    Weber, B.L.3
  • 7
    • 0035099044 scopus 로고    scopus 로고
    • BRCA2 is required for homology-directed repair of chromosomal breaks
    • Moynahan M.E., Pierce A.J., and Jasin M. BRCA2 is required for homology-directed repair of chromosomal breaks. Mol. Cell 7 (2001) 263-272
    • (2001) Mol. Cell , vol.7 , pp. 263-272
    • Moynahan, M.E.1    Pierce, A.J.2    Jasin, M.3
  • 8
    • 0037115914 scopus 로고    scopus 로고
    • Homologous repair of DNA damage and tumorigenesis: the BRCA connection
    • Jasin M. Homologous repair of DNA damage and tumorigenesis: the BRCA connection. Oncogene 21 (2002) 8981-8993
    • (2002) Oncogene , vol.21 , pp. 8981-8993
    • Jasin, M.1
  • 9
    • 0041378027 scopus 로고    scopus 로고
    • Sequence fingerprints in BRCA2 and RAD51: implications for DNA repair and cancer
    • Lo T., Pellegrini L., Venkitaraman A.R., and Blundell T.L. Sequence fingerprints in BRCA2 and RAD51: implications for DNA repair and cancer. DNA Repair (Amst.) 2 (2003) 1015-1028
    • (2003) DNA Repair (Amst.) , vol.2 , pp. 1015-1028
    • Lo, T.1    Pellegrini, L.2    Venkitaraman, A.R.3    Blundell, T.L.4
  • 11
    • 0030140414 scopus 로고    scopus 로고
    • Internal repeats in the BRCA2 protein sequence
    • Bork P., Blomberg N., and Nilges M. Internal repeats in the BRCA2 protein sequence. Nat. Genet. 13 (1996) 22-23
    • (1996) Nat. Genet. , vol.13 , pp. 22-23
    • Bork, P.1    Blomberg, N.2    Nilges, M.3
  • 12
    • 42449098062 scopus 로고    scopus 로고
    • Inhibition of filament formation of human Rad51 protein by a small peptide derived from the BRC-motif of the BRCA2 protein
    • Nomme J., Takizawa Y., Martinez S.F., Renodon-Corniere A., Fleury F., Weigel P., et al. Inhibition of filament formation of human Rad51 protein by a small peptide derived from the BRC-motif of the BRCA2 protein. Genes Cells 13 (2008) 471-481
    • (2008) Genes Cells , vol.13 , pp. 471-481
    • Nomme, J.1    Takizawa, Y.2    Martinez, S.F.3    Renodon-Corniere, A.4    Fleury, F.5    Weigel, P.6
  • 13
    • 34249887673 scopus 로고    scopus 로고
    • Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats
    • Davies O.R., and Pellegrini L. Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats. Nat. Struct. Mol. Biol. 14 (2007) 475-483
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 475-483
    • Davies, O.R.1    Pellegrini, L.2
  • 14
    • 34249878748 scopus 로고    scopus 로고
    • Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2
    • Esashi F., Galkin V.E., Yu X., Egelman E.H., and West S.C. Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2. Nat. Struct. Mol. Biol. 14 (2007) 468-474
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 468-474
    • Esashi, F.1    Galkin, V.E.2    Yu, X.3    Egelman, E.H.4    West, S.C.5
  • 17
    • 63049108452 scopus 로고    scopus 로고
    • Linking the cellular functions of BRCA genes to cancer pathogenesis and treatment
    • Venkitaraman A.R. Linking the cellular functions of BRCA genes to cancer pathogenesis and treatment. Ann. Rev. Pathol. Mech. Dis. 4 (2009) 461-487
    • (2009) Ann. Rev. Pathol. Mech. Dis. , vol.4 , pp. 461-487
    • Venkitaraman, A.R.1
  • 18
    • 0035979246 scopus 로고    scopus 로고
    • Effects of DNA sequence and structure on binding of RecA to single-stranded DNA
    • Bar-Ziv R., and Libchaber A. Effects of DNA sequence and structure on binding of RecA to single-stranded DNA. Proc. Natl Acad. Sci. USA 98 (2001) 9068-9073
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9068-9073
    • Bar-Ziv, R.1    Libchaber, A.2
  • 19
    • 0035053510 scopus 로고    scopus 로고
    • Effect of ions and nucleotides on the interactions of yeast Rad51 protein with single-stranded oligonucleotides
    • Kim J.M., Maraboeuf F., Kim S.K., Shinohara A., and Takahashi M. Effect of ions and nucleotides on the interactions of yeast Rad51 protein with single-stranded oligonucleotides. J. Biochem. 129 (2001) 469-475
    • (2001) J. Biochem. , vol.129 , pp. 469-475
    • Kim, J.M.1    Maraboeuf, F.2    Kim, S.K.3    Shinohara, A.4    Takahashi, M.5
  • 20
    • 0035937811 scopus 로고    scopus 로고
    • Basis for avid homologous DNA strand exchange by human Rad51 and RPA
    • Sigurdsson S., Trujillo K., Song B., Stratton S., and Sung P. Basis for avid homologous DNA strand exchange by human Rad51 and RPA. J. Biol. Chem. 276 (2001) 8798-8806
    • (2001) J. Biol. Chem. , vol.276 , pp. 8798-8806
    • Sigurdsson, S.1    Trujillo, K.2    Song, B.3    Stratton, S.4    Sung, P.5
  • 21
    • 0030584084 scopus 로고    scopus 로고
    • Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann P., Benson F.E., and West S.C. Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87 (1996) 757-766
    • (1996) Cell , vol.87 , pp. 757-766
    • Baumann, P.1    Benson, F.E.2    West, S.C.3
  • 22
    • 0034161571 scopus 로고    scopus 로고
    • Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing
    • Mazin A.V., Zaitseva E., Sung P., and Kowalczykowski S.C. Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing. EMBO J. 19 (2000) 1148-1156
    • (2000) EMBO J. , vol.19 , pp. 1148-1156
    • Mazin, A.V.1    Zaitseva, E.2    Sung, P.3    Kowalczykowski, S.C.4
  • 23
    • 40749090377 scopus 로고    scopus 로고
    • DNA bending stiffness on small length scales
    • Yuan C., Chen H., Lou X.W., and Archer L.A. DNA bending stiffness on small length scales. Phys. Rev. Lett. 100 (2008) 018102
    • (2008) Phys. Rev. Lett. , vol.100 , pp. 018102
    • Yuan, C.1    Chen, H.2    Lou, X.W.3    Archer, L.A.4
  • 24
    • 0029398141 scopus 로고
    • Hybridization of fluorescein-labeled DNA oligomers detected by fluorescence anisotropy with protein binding enhancement
    • Kumke M.U., Li G., McGown L.B., Walker G.T., and Linn C.P. Hybridization of fluorescein-labeled DNA oligomers detected by fluorescence anisotropy with protein binding enhancement. Anal. Chem. 67 (1995) 3945-3951
    • (1995) Anal. Chem. , vol.67 , pp. 3945-3951
    • Kumke, M.U.1    Li, G.2    McGown, L.B.3    Walker, G.T.4    Linn, C.P.5
  • 25
    • 33744950933 scopus 로고    scopus 로고
    • Recombination mediator and Rad51 targeting activities of a human BRCA2 polypeptide
    • San Filippo J., Chi P., Sehorn M.G., Etchin J., Krejci L., and Sung P. Recombination mediator and Rad51 targeting activities of a human BRCA2 polypeptide. J. Biol. Chem. 281 (2006) 11649-11657
    • (2006) J. Biol. Chem. , vol.281 , pp. 11649-11657
    • San Filippo, J.1    Chi, P.2    Sehorn, M.G.3    Etchin, J.4    Krejci, L.5    Sung, P.6
  • 26
    • 0032702679 scopus 로고    scopus 로고
    • Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control
    • Chen C.F., Chen P.L., Zhong Q., Sharp Z.D., and Lee W.H. Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control. J. Biol. Chem. 274 (1999) 32931-32935
    • (1999) J. Biol. Chem. , vol.274 , pp. 32931-32935
    • Chen, C.F.1    Chen, P.L.2    Zhong, Q.3    Sharp, Z.D.4    Lee, W.H.5
  • 27
    • 34250879021 scopus 로고    scopus 로고
    • Interactions between human BRCA2 protein and the meiosis-specific recombinase DMC1
    • Thorslund T., Esashi F., and West S.C. Interactions between human BRCA2 protein and the meiosis-specific recombinase DMC1. EMBO J. 26 (2007) 2915-2922
    • (2007) EMBO J. , vol.26 , pp. 2915-2922
    • Thorslund, T.1    Esashi, F.2    West, S.C.3
  • 29
    • 49649088827 scopus 로고    scopus 로고
    • Classical molecular dynamics simulations of the complex between the RAD51 protein and the BRC hairpin loops of the BRCA2 protein
    • Buis N., Skylaris C.K., Grant G.H., Rajendra E., Payne M.C., and Venkitaraman A.R. Classical molecular dynamics simulations of the complex between the RAD51 protein and the BRC hairpin loops of the BRCA2 protein. Mol. Simul. 34 (2008) 749-759
    • (2008) Mol. Simul. , vol.34 , pp. 749-759
    • Buis, N.1    Skylaris, C.K.2    Grant, G.H.3    Rajendra, E.4    Payne, M.C.5    Venkitaraman, A.R.6
  • 31
    • 46249091563 scopus 로고    scopus 로고
    • The checkpoint kinases Chk1 and Chk2 regulate the functional associations between hBRCA2 and Rad51 in response to DNA damage
    • Bahassi E.M., Ovesen J.L., Riesenberg A.L., Bernstein W.Z., Hasty P.E., and Stambrook P.J. The checkpoint kinases Chk1 and Chk2 regulate the functional associations between hBRCA2 and Rad51 in response to DNA damage. Oncogene 27 (2008) 3977-3985
    • (2008) Oncogene , vol.27 , pp. 3977-3985
    • Bahassi, E.M.1    Ovesen, J.L.2    Riesenberg, A.L.3    Bernstein, W.Z.4    Hasty, P.E.5    Stambrook, P.J.6
  • 32
    • 18544372595 scopus 로고    scopus 로고
    • BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure
    • Yang H., Jeffrey P.D., Miller J., Kinnucan E., Sun Y., Thoma N.H., et al. BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Science 297 (2002) 1837-1848
    • (2002) Science , vol.297 , pp. 1837-1848
    • Yang, H.1    Jeffrey, P.D.2    Miller, J.3    Kinnucan, E.4    Sun, Y.5    Thoma, N.H.6
  • 33
    • 33745018564 scopus 로고    scopus 로고
    • Suppression of the DNA repair defects of BRCA2-deficient cells with heterologous protein fusions
    • Saeki H., Siaud N., Christ N., Wiegant W.W., van Buul P.P., Han M., et al. Suppression of the DNA repair defects of BRCA2-deficient cells with heterologous protein fusions. Proc. Natl Acad. Sci. USA 103 (2006) 8768-8773
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8768-8773
    • Saeki, H.1    Siaud, N.2    Christ, N.3    Wiegant, W.W.4    van Buul, P.P.5    Han, M.6


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