메뉴 건너뛰기




Volumn 290, Issue 2, 1999, Pages 495-504

The N-terminal domain of the human Rad51 protein binds DNA: Structure and a DNA binding surface as revealed by NMR

Author keywords

DNA binding; Genetic recombination; NMR spectroscopy; Rad51 protein; Solution structure

Indexed keywords

DNA BINDING PROTEIN; DOUBLE STRANDED DNA; SINGLE STRANDED DNA;

EID: 0033538424     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2904     Document Type: Article
Times cited : (120)

References (56)
  • 1
    • 0030664070 scopus 로고    scopus 로고
    • An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing
    • Aihara H., Ito Y., Kurumizaka H., Terada T., Yokoyama S., Shibata T. An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing. J. Mol. Biol. 274:1997;213-221.
    • (1997) J. Mol. Biol. , vol.274 , pp. 213-221
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Terada, T.4    Yokoyama, S.5    Shibata, T.6
  • 3
    • 0025339406 scopus 로고
    • Solution structure of phage λ half-operator DNA by use of NMR, restrained molecular dynamics, and NOE-based refinement
    • Baleja J. D., Pon R. T., Sykes B. D. Solution structure of phage λ half-operator DNA by use of NMR, restrained molecular dynamics, and NOE-based refinement. Biochemistry. 29:1990;4828-4839.
    • (1990) Biochemistry , vol.29 , pp. 4828-4839
    • Baleja, J.D.1    Pon, R.T.2    Sykes, B.D.3
  • 4
    • 0030766963 scopus 로고    scopus 로고
    • The human Rad51 protein: Polarity of strand transfer and stimulation by hRP-A
    • Baumann P., West S. C. The human Rad51 protein: polarity of strand transfer and stimulation by hRP-A. EMBO J. 16:1997;5198-5206.
    • (1997) EMBO J. , vol.16 , pp. 5198-5206
    • Baumann, P.1    West, S.C.2
  • 5
    • 0032127849 scopus 로고    scopus 로고
    • Role of the human RAD51 protein in homologous recombination and double- stranded-break repair
    • Baumann P., West S. C. Role of the human RAD51 protein in homologous recombination and double- stranded-break repair. Trends Biochem. Sci. 23:1998;247-251.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 247-251
    • Baumann, P.1    West, S.C.2
  • 6
    • 0030584084 scopus 로고    scopus 로고
    • Human rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann P., Benson F. E., 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
  • 8
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson F. E., Stasiak A., West S. C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 13:1994;5764-5771.
    • (1994) EMBO J. , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 9
    • 0032556865 scopus 로고    scopus 로고
    • Synergistic actions of Rad51 and Rad52 in recombination and DNA repair
    • Benson F. E., Baumann P., West S. C. Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. Nature. 391:1998;401-404.
    • (1998) Nature , vol.391 , pp. 401-404
    • Benson, F.E.1    Baumann, P.2    West, S.C.3
  • 10
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen G., Ruben D. J. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Letters. 69:1980;185-189.
    • (1980) Chem. Phys. Letters , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 13
    • 0032574733 scopus 로고    scopus 로고
    • The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment
    • Chen P. L., Chen C. F., Chen Y., Xiao J., Sharp Z. D., Lee W. H. The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment. Proc. Natl Acad. Sci. USA. 95:1998;5287-5292.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5287-5292
    • Chen, P.L.1    Chen, C.F.2    Chen, Y.3    Xiao, J.4    Sharp, Z.D.5    Lee, W.H.6
  • 15
    • 0028105106 scopus 로고
    • Homotypic and heterotypic protein associations control rad51 function in double-strand break repair
    • Donovan J. W., Milne G. T., Weaver D. T. Homotypic and heterotypic protein associations control rad51 function in double-strand break repair. Gene Dev. 8:1994;2552-2562.
    • (1994) Gene Dev. , vol.8 , pp. 2552-2562
    • Donovan, J.W.1    Milne, G.T.2    Weaver, D.T.3
  • 18
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S., Bax A. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114:1992;6291-6293.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 19
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115:1993;12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 22
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L., Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:1993;123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 23
    • 0021272696 scopus 로고
    • Separation of the presynaptic and synaptic phases of homologous pairing promoted by recA protein
    • Kahn R., Radding C. M. Separation of the presynaptic and synaptic phases of homologous pairing promoted by recA protein. J. Biol. Chem. 259:1984;7495-7503.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7495-7503
    • Kahn, R.1    Radding, C.M.2
  • 26
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A., Ernst R. R., Wuthrich K. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1980;1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 28
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski R. A., Rullmann J. A. C., MacArthur M. W., Kaptein R., Thornton J. M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR. 8:1996;477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 32
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges M., Clore G. M., Gronenborn A. M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters. 229:1988;317-324.
    • (1988) FEBS Letters , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 33
    • 0031566434 scopus 로고    scopus 로고
    • Automated NOESY interpretation with ambiguous distance restraints: The refined NMR solution structure of the pleckstrin homology domain from beta-spectrin
    • Nilges M., Macias M. J., O'Donoghue S. I., Oschkinat H. Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin. J. Mol. Biol. 269:1997;408-422.
    • (1997) J. Mol. Biol. , vol.269 , pp. 408-422
    • Nilges, M.1    Macias, M.J.2    O'Donoghue, S.I.3    Oschkinat, H.4
  • 34
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD51 filament to the bacterial RecA filament
    • Ogawa T., Yu X., Shinohara A., Egelman E. H. Similarity of the yeast RAD51 filament to the bacterial RecA filament. Science. 259:1993;1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 36
    • 0032492853 scopus 로고    scopus 로고
    • Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins
    • Petukhova G., Stratton S., Sung P. Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature. 393:1998;91-94.
    • (1998) Nature , vol.393 , pp. 91-94
    • Petukhova, G.1    Stratton, S.2    Sung, P.3
  • 37
    • 0001800866 scopus 로고
    • Investigating the genetic control of biochemical events in meiotic recombination
    • London: Academic Press
    • Resnick M. A. Investigating the genetic control of biochemical events in meiotic recombination. Meiosis. 1987;Academic Press, London.
    • (1987) Meiosis
    • Resnick, M.A.1
  • 40
    • 0030047343 scopus 로고    scopus 로고
    • Specific interactions between the human RAD51 and RAD52 proteins
    • Shen Z., Cloud K. G., Chen D. J., Park M. S. Specific interactions between the human RAD51 and RAD52 proteins. J. Biol. Chem. 271:1996;148-152.
    • (1996) J. Biol. Chem. , vol.271 , pp. 148-152
    • Shen, Z.1    Cloud, K.G.2    Chen, D.J.3    Park, M.S.4
  • 41
  • 42
    • 0026751113 scopus 로고
    • RAD51 protein involved in repair and recombination in S. cerevisiae is a recA-like protein
    • Shinohara A., Ogawa H., Ogawa T. RAD51 protein involved in repair and recombination in S. cerevisiae is a recA-like protein. Cell. 69:1992;457-470.
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 43
    • 0027325816 scopus 로고
    • Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA
    • Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nature Genet. 4:1993;239-243.
    • (1993) Nature Genet. , vol.4 , pp. 239-243
    • Shinohara, A.1    Ogawa, H.2    Matsuda, Y.3    Ushio, N.4    Ikeo, K.5    Ogawa, T.6
  • 45
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story R. M., Weber I., Steitz T. A. The structure of the E. coli recA protein monomer and polymer. Nature. 355:1992;318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.2    Steitz, T.A.3
  • 46
    • 0029969418 scopus 로고    scopus 로고
    • P53 is linked directly to homologous recombination processes via RAD51/RecA protein interaction
    • Sturzbecher H. W., Donzelmann B., Henning W., Knippschild U., Buchhop S. p53 is linked directly to homologous recombination processes via RAD51/RecA protein interaction. EMBO J. 15:1996;1992-2002.
    • (1996) EMBO J. , vol.15 , pp. 1992-2002
    • Sturzbecher, H.W.1    Donzelmann, B.2    Henning, W.3    Knippschild, U.4    Buchhop, S.5
  • 47
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein
    • Sung P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science. 265:1994;1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 48
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer M. M., Ahern H., Xing D. X., Cunningham R. P., Tainer J. A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14:1995;4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.X.3    Cunningham, R.P.4    Tainer, J.A.5
  • 50
    • 0031449639 scopus 로고    scopus 로고
    • Mammalian Rad51 protein: A RecA homologue with pleiotropic functions
    • Vispe S., Defais M. Mammalian Rad51 protein: a RecA homologue with pleiotropic functions. Biochimie. 79:1997;587-592.
    • (1997) Biochimie , vol.79 , pp. 587-592
    • Vispe, S.1    Defais, M.2
  • 53
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-protein and nitrogen resonances with the alpha-and beta-carbon resonances in proteins
    • Wittekind M., Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-protein and nitrogen resonances with the alpha-and beta-carbon resonances in proteins. J. Magn. Reson. ser. B. 101:1993;201-205.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 54
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility genebrca2
    • 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 genebrca2. J. Biol. Chem. 272:1997;31941-31944.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31941-31944
    • Wong, A.K.C.1    Pero, R.2    Ormonde, P.A.3    Tavtigian, S.V.4    Bartel, P.L.5
  • 55
    • 0032514951 scopus 로고    scopus 로고
    • Identification of a defined epitope on the surface of the active RecA-DNA filament using a monoclonal antibody and three-dimensional reconstruction
    • Yu X., Shibata T., Egelman E. H. Identification of a defined epitope on the surface of the active RecA-DNA filament using a monoclonal antibody and three-dimensional reconstruction. J. Mol. Biol. 283:1998;985-992.
    • (1998) J. Mol. Biol. , vol.283 , pp. 985-992
    • Yu, X.1    Shibata, T.2    Egelman, E.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.