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Volumn 288, Issue 25, 2013, Pages 18110-18120

Cooperative assembly of a protein-DNA filament for nonhomologous end joining

Author keywords

[No Author keywords available]

Indexed keywords

CO-OPERATIVE ASSEMBLY; COOPERATIVE BINDING; MISMATCHED DNA; NONHOMOLOGOUS END JOINING; PROTEIN-DNA COMPLEXES;

EID: 84880079338     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.464115     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0023424487 scopus 로고
    • Developmental stage specificity of the lymphoid V (D) J recombination activity
    • Lieber, M. R., Hesse, J. E., Mizuuchi, K., and Gellert, M. (1987) Developmental stage specificity of the lymphoid V(D)J recombination activity. Genes Dev. 1, 751-761
    • (1987) Genes Dev. , vol.1 , pp. 751-761
    • Lieber, M.R.1    Hesse, J.E.2    Mizuuchi, K.3    Gellert, M.4
  • 2
    • 84865620494 scopus 로고    scopus 로고
    • Recognition, signaling, and repair of DNA double-strand breaks produced by ionizing radiation in mammalian cells: The molecular choreography
    • Thompson, L. H. (2012) Recognition, signaling, and repair of DNA double-strand breaks produced by ionizing radiation in mammalian cells: The molecular choreography. Mutat. Res. 751, 158-246
    • (2012) Mutat. Res. , vol.751 , pp. 158-246
    • Thompson, L.H.1
  • 3
    • 0028112944 scopus 로고
    • Restoration of X-ray resistance and V(D)J recombination in mutant cells by Ku cDNA
    • Smider, V., Rathmell, W. K., Lieber, M. R., and Chu, G. (1994) Restoration of x-ray resistance and V(D)J recombination in mutant cells by Ku cDNA. Science 266, 288-291 (Pubitemid 24343516)
    • (1994) Science , vol.266 , Issue.5183 , pp. 288-291
    • Smider, V.1    Rathmell, W.K.2    Lieber, M.R.3    Chu, G.4
  • 6
    • 0037124373 scopus 로고    scopus 로고
    • Synapsis of DNA ends by DNA-dependent protein kinase
    • DOI 10.1093/emboj/cdf299
    • DeFazio, L. G., Stansel, R. M., Griffith, J. D., and Chu, G. (2002) Synapsis of DNA ends by the DNA-dependent protein kinase. EMBO J. 21, 3192-3200 (Pubitemid 34670402)
    • (2002) EMBO Journal , vol.21 , Issue.12 , pp. 3192-3200
    • DeFazio, L.G.1    Stansel, R.M.2    Griffith, J.D.3    Chu, G.4
  • 7
    • 0030743386 scopus 로고    scopus 로고
    • Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells
    • DOI 10.1038/41358
    • Grawunder, U., Wilm, M., Wu, X., Kulesza, P., Wilson, T. E., Mann, M., and Lieber, M. R. (1997) Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature 388, 492-495 (Pubitemid 27328929)
    • (1997) Nature , vol.388 , Issue.6641 , pp. 492-495
    • Grawunder, U.1    Wilm, M.2    Wu, X.3    Kulesza, P.4    Wilson, T.E.5    Mann, M.6    Lieber, M.R.7
  • 10
    • 49349083288 scopus 로고    scopus 로고
    • Lymphocyte-specific compensation for XLF/Cernunnos end-joining functions in V(D) J recombination
    • Li, G., Alt, F. W., Cheng, H. L., Brush, J. W., Goff, P. H., Murphy, M. M., Franco, S., Zhang, Y., and Zha, S. (2008) Lymphocyte-specific compensation for XLF/Cernunnos end-joining functions in V(D)J recombination. Mol. Cell 31, 631-640
    • (2008) Mol Cell , vol.31 , pp. 631-640
    • Li, G.1    Alt, F.W.2    Cheng, H.L.3    Brush, J.W.4    Goff, P.H.5    Murphy, M.M.6    Franco, S.7    Zhang, Y.8    Zha, S.9
  • 12
    • 31044432090 scopus 로고    scopus 로고
    • XLF interacts with the XRCC4-DNA Ligase IV complex to promote DNA nonhomologous end-joining
    • DOI 10.1016/j.cell.2005.12.031, PII S0092867406000031
    • Ahnesorg, P., Smith, P., and Jackson, S. P. (2006) XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous endjoining. Cell 124, 301-313 (Pubitemid 43121979)
    • (2006) Cell , vol.124 , Issue.2 , pp. 301-313
    • Ahnesorg, P.1    Smith, P.2    Jackson, S.P.3
  • 13
    • 37349113779 scopus 로고    scopus 로고
    • Crystal Structure of Human XLF: A Twist in Nonhomologous DNA End-Joining
    • DOI 10.1016/j.molcel.2007.10.024, PII S1097276507007319
    • Andres, S. N., Modesti, M., Tsai, C. J., Chu, G., and Junop, M. S. (2007) Crystal structure of human XLF: A twist in nonhomologous DNA endjoining. Mol. Cell 28, 1093-1101 (Pubitemid 350297023)
    • (2007) Molecular Cell , vol.28 , Issue.6 , pp. 1093-1101
    • Andres, S.N.1    Modesti, M.2    Tsai, C.J.3    Chu, G.4    Junop, M.S.5
  • 14
    • 0034669204 scopus 로고    scopus 로고
    • Crystal structure of the Xrcc4 DNA repair protein and implications for end joining
    • Junop, M. S., Modesti, M., Guarné, A., Ghirlando, R., Gellert, M., and Yang, W. (2000) Crystal structure of the Xrcc4 DNA repair protein and implications for end joining. EMBO J. 19, 5962-5970
    • (2000) EMBO J. , vol.19 , pp. 5962-5970
    • Junop, M.S.1    Modesti, M.2    Guarné, A.3    Ghirlando, R.4    Gellert, M.5    Yang, W.6
  • 16
    • 80955133161 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray diffraction analysis of the human XRCC4-XLF complex
    • Andres, S. N., and Junop, M. S. (2011) Crystallization and preliminary x-ray diffraction analysis of the human XRCC4-XLF complex. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67, 1399-1402
    • (2011) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.67 , pp. 1399-1402
    • Andres, S.N.1    Junop, M.S.2
  • 19
    • 80053358977 scopus 로고    scopus 로고
    • Nonhomologous end-joining partners in a helical dance: Structural studies of XLF-Xrcc4 interactions
    • Wu, Q., Ochi, T., Matak-Vinkovic, D., Robinson, C. V., Chirgadze, D. Y., and Blundell, T. L. (2011) Nonhomologous end-joining partners in a helical dance: Structural studies of XLF-Xrcc4 interactions. Biochem. Soc. Trans. 39, 1387-1392
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 1387-1392
    • Wu, Q.1    Ochi, T.2    Matak-Vinkovic, D.3    Robinson, C.V.4    Chirgadze, D.Y.5    Blundell, T.L.6
  • 20
    • 78149459696 scopus 로고    scopus 로고
    • XLF regulates filament architecture of the XRCC4-ligase IV complex
    • Hammel, M., Yu, Y., Fang, S., Lees-Miller, S. P., and Tainer, J. A. (2010) XLF regulates filament architecture of the XRCC4-ligase IV complex. Structure 18, 1431-1442
    • (2010) Structure , vol.18 , pp. 1431-1442
    • Hammel, M.1    Yu, Y.2    Fang, S.3    Lees-Miller, S.P.4    Tainer, J.A.5
  • 21
    • 34848841930 scopus 로고    scopus 로고
    • Single-stranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: Influence of terminal DNA sequence
    • DOI 10.1093/nar/gkm579
    • Gu, J., Lu, H., Tsai, A. G., Schwarz, K., and Lieber, M. R. (2007) Singlestranded DNA ligation and XLF-stimulated incompatible DNA end ligation by the XRCC4-DNA ligase IV complex: Influence of terminal DNA sequence. Nucleic Acids Res. 35, 5755-5762 (Pubitemid 47506292)
    • (2007) Nucleic Acids Research , vol.35 , Issue.17 , pp. 5755-5762
    • Gu, J.1    Lu, H.2    Tsai, A.G.3    Schwarz, K.4    Lieber, M.R.5
  • 23
    • 34250670453 scopus 로고    scopus 로고
    • Site-specific protein labeling by Sfp phosphopantetheinyl transferase
    • Yin, J., Lin, A. J., Golan, D. E., and Walsh, C. T. (2006) Site-specific protein labeling by Sfp phosphopantetheinyl transferase. Nat. Protoc. 1, 280-285
    • (2006) Nat. Protoc. , vol.1 , pp. 280-285
    • Yin, J.1    Lin, A.J.2    Golan, D.E.3    Walsh, C.T.4
  • 24
    • 15444370124 scopus 로고    scopus 로고
    • Processing of DNA for nonhomologous end-joining by cell-free extract
    • DOI 10.1038/sj.emboj.7600563
    • Budman, J., and Chu, G. (2005) Processing of DNA for nonhomologous end-joining by cell-free extract. EMBO J. 24, 849-860 (Pubitemid 40396113)
    • (2005) EMBO Journal , vol.24 , Issue.4 , pp. 849-860
    • Budman, J.1    Chu, G.2
  • 26
    • 36148957874 scopus 로고    scopus 로고
    • Interplay between Cernunnos-XLF and nonhomologous end-joining proteins at DNA ends in the cell
    • DOI 10.1074/jbc.M704554200
    • Wu, P. Y., Frit, P., Malivert, L., Revy, P., Biard, D., Salles, B., and Calsou, P. (2007) Interplay between Cernunnos-XLF and nonhomologous end-joining proteins at DNA ends in the cell. J. Biol. Chem. 282, 31937-31943 (Pubitemid 350106409)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.44 , pp. 31937-31943
    • Wu, P.-Y.1    Frit, P.2    Malivert, L.3    Revy, P.4    Biard, D.5    Salles, B.6    Calsou, P.7
  • 27
    • 79952573454 scopus 로고    scopus 로고
    • Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF
    • Yano, K., Morotomi-Yano, K., Lee, K. J., and Chen, D. J. (2011) Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF. FEBS Lett. 585, 841-846
    • (2011) FEBS Lett. , vol.585 , pp. 841-846
    • Yano, K.1    Morotomi-Yano, K.2    Lee, K.J.3    Chen, D.J.4
  • 28
    • 34249702972 scopus 로고    scopus 로고
    • Processing of DNA for nonhomologous end-joining is controlled by kinase activity and XRCC4/ligase IV
    • DOI 10.1074/jbc.M610058200
    • Budman, J., Kim, S. A., and Chu, G. (2007) Processing of DNA for nonhomologous end-joining is controlled by kinase activity and XRCC4/ligase IV. J. Biol. Chem. 282, 11950-11959 (Pubitemid 47100661)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.16 , pp. 11950-11959
    • Budman, J.1    Kim, S.A.2    Chu, G.3
  • 29
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to dna and its implications for double-strand break repair
    • DOI 10.1038/35088000
    • Walker, J. R., Corpina, R. A., and Goldberg, J. (2001) Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 412, 607-614 (Pubitemid 32772267)
    • (2001) Nature , vol.412 , Issue.6847 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3
  • 31
    • 0028342645 scopus 로고
    • A DNA end-binding factor involved in double-strand break repair and V(D)J recombination
    • Rathmell, W. K., and Chu, G. (1994) A DNA end-binding factor involved in double-strand break repair and V(D)J recombination. Mol. Cell. Biol. 14, 4741-4748 (Pubitemid 24196824)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.7 , pp. 4741-4748
    • Rathmell, W.K.1    Chu, G.2
  • 32
    • 0019878376 scopus 로고
    • Equilibrium and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis
    • Fried, M., and Crothers, D. M. (1981) Equilibrium and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res. 9, 6505-6525
    • (1981) Nucleic Acids Res. , vol.9 , pp. 6505-6525
    • Fried, M.1    Crothers, D.M.2
  • 33
    • 0019877067 scopus 로고
    • A gel electrophoresis method for quantifying the binding of proteins to specificDNAregions: Application to the components of the E. coli lactose operon regulatory system
    • Garner, M. M., and Revzin, A. (1981) A gel electrophoresis method for quantifying the binding of proteins to specificDNAregions: Application to the components of the E. coli lactose operon regulatory system. Nucleic Acids Res. 9, 3047-3060
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3047-3060
    • Garner, M.M.1    Revzin, A.2
  • 35
    • 0026787523 scopus 로고
    • Global features of DNA structure by comparative gel electrophoresis
    • Crothers, D. M., and Drak, J. (1992) Global features of DNA structure by comparative gel electrophoresis. Methods Enzymol. 212, 46-71
    • (1992) Methods Enzymol. , vol.212 , pp. 46-71
    • Crothers, D.M.1    Drak, J.2
  • 36
    • 0024323026 scopus 로고
    • Measurement of protein-DNA interaction parameters by electrophoresis mobility shift assay
    • DOI 10.1002/elps.1150100515
    • Fried, M. G. (1989) Measurement of protein-DNA interaction parameters by electrophoresis mobility shift assay. Electrophoresis 10, 366-376 (Pubitemid 19159680)
    • (1989) Electrophoresis , vol.10 , Issue.5-6 , pp. 366-376
    • Fried, M.G.1
  • 37
    • 0035834743 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA
    • Hong, E. L., Shinohara, A., and Bishop, D. K. (2001) Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA. J. Biol. Chem. 276, 41906-41912
    • (2001) J. Biol. Chem. , vol.276 , pp. 41906-41912
    • Hong, E.L.1    Shinohara, A.2    Bishop, D.K.3
  • 38
    • 45749124305 scopus 로고    scopus 로고
    • Live cell imaging of XLF and XRCC4 reveals a novel view of protein assembly in the non-homologous end-joining pathway
    • Yano, K., and Chen, D. J. (2008) Live cell imaging of XLF and XRCC4 reveals a novel view of protein assembly in the nonhomologous end-joining pathway. Cell Cycle 7, 1321-1325 (Pubitemid 351872567)
    • (2008) Cell Cycle , vol.7 , Issue.10 , pp. 1321-1325
    • Yano, K.-I.1    Chen, D.J.2
  • 39
    • 0033572709 scopus 로고    scopus 로고
    • Geometry of a complex formed by double strand break repair proteins at a single DNA end: Recruitment of DNA-PKcs induces inward translocation of Ku protein
    • Yoo, S., and Dynan, W. S. (1999) Geometry of a complex formed by double strand break repair proteins at a single DNA end: Recruitment of DNAPKcs induces inward translocation of Ku protein. Nucleic Acids Res. 27, 4679-4686 (Pubitemid 30006656)
    • (1999) Nucleic Acids Research , vol.27 , Issue.24 , pp. 4679-4686
    • Yoo, S.1    Dynan, W.S.2
  • 40
    • 57949116437 scopus 로고    scopus 로고
    • DNA-PK: The means to justify the ends?
    • Meek, K., Dang, V., and Lees-Miller, S. P. (2008) DNA-PK: The means to justify the ends? Adv. Immunol. 99, 33-58
    • (2008) Adv. Immunol. , vol.99 , pp. 33-58
    • Meek, K.1    Dang, V.2    Lees-Miller, S.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.