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Volumn 383, Issue 3, 2008, Pages 575-587

Structural Analysis of the Human Rad51 Protein-DNA Complex Filament by Tryptophan Fluorescence Scanning Analysis: Transmission of Allosteric Effects between ATP Binding and DNA Binding

Author keywords

allosteric effect; homologous recombination; protein filament; Rad51 protein; tryptophan fluorescence

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; HISTIDINE; PHENYLALANINE; RAD51 PROTEIN; TRYPTOPHAN;

EID: 52949150762     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.08.030     Document Type: Article
Times cited : (9)

References (47)
  • 1
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Shinohara A., Ogawa H., and 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0030334895 scopus 로고    scopus 로고
    • Purification and characterization of XRad51.1 protein, Xenopus RAD51 homologue: recombinant XRad51.1 promotes strand exchange reaction
    • Maeshima K., Morimatsu K., and Horii T. Purification and characterization of XRad51.1 protein, Xenopus RAD51 homologue: recombinant XRad51.1 promotes strand exchange reaction. Genes Cells 1 (1996) 1057-1068
    • (1996) Genes Cells , vol.1 , pp. 1057-1068
    • Maeshima, K.1    Morimatsu, K.2    Horii, T.3
  • 6
    • 0028957889 scopus 로고
    • Nuclear foci of mammalian Rad51 recombination protein in somatic cells after DNA damage and its localization in synaptonemal complexes
    • Haaf T., Golub E.I., Reddy G., Radding C.M., and 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 (1995) 2298-2302
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2298-2302
    • Haaf, T.1    Golub, E.I.2    Reddy, G.3    Radding, C.M.4    Ward, D.C.5
  • 7
    • 0032526320 scopus 로고    scopus 로고
    • Overexpression of Rad51 protein stimulates homologous recombination and increases resistance of mammalian cells to ionizing radiation
    • Vispe S., Cazaux C., Lesca C., and Defais M. Overexpression of Rad51 protein stimulates homologous recombination and increases resistance of mammalian cells to ionizing radiation. Nucleic Acids Res. 26 (1998) 2859-2864
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2859-2864
    • Vispe, S.1    Cazaux, C.2    Lesca, C.3    Defais, M.4
  • 8
    • 0032518657 scopus 로고    scopus 로고
    • Rad51-deficient vertebrate cells accumulate chromosomal breaks prior to cell death
    • Sonoda E., Sasaki M.S., Buerstedde J.M., Bezzubova O., Shinohara A., Ogawa H., et al. Rad51-deficient vertebrate cells accumulate chromosomal breaks prior to cell death. EMBO J. 17 (1998) 598-608
    • (1998) EMBO J. , vol.17 , pp. 598-608
    • Sonoda, E.1    Sasaki, M.S.2    Buerstedde, J.M.3    Bezzubova, O.4    Shinohara, A.5    Ogawa, H.6
  • 9
    • 0242268056 scopus 로고    scopus 로고
    • Homologous recombination and cell checkpoints: Rad51 in tumour progression and therapy resistance
    • Henning W., and Sturzbecher H.W. Homologous recombination and cell checkpoints: Rad51 in tumour progression and therapy resistance. Toxicology 193 (2003) 91-109
    • (2003) Toxicology , vol.193 , pp. 91-109
    • Henning, W.1    Sturzbecher, H.W.2
  • 11
    • 0035312501 scopus 로고    scopus 로고
    • Ribozyme minigene-mediated RAD51 down-regulation increases radiosensitivity of human prostate cancer cells
    • Collis S.J., Tighe A., Scott S.D., Roberts S.A., Hendry J.H., and Margison G.P. Ribozyme minigene-mediated RAD51 down-regulation increases radiosensitivity of human prostate cancer cells. Nucleic Acids Res. 29 (2001) 1534-1538
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1534-1538
    • Collis, S.J.1    Tighe, A.2    Scott, S.D.3    Roberts, S.A.4    Hendry, J.H.5    Margison, G.P.6
  • 12
    • 0032540152 scopus 로고    scopus 로고
    • In vitro and in vivo potentiation of radiosensitivity of malignant gliomas by antisense inhibition of the RAD51 gene
    • Ohnishi T., Taki T., Hiraga T., Arita N., and Morita T. In vitro and in vivo potentiation of radiosensitivity of malignant gliomas by antisense inhibition of the RAD51 gene. Biochem. Biophys. Res. Commun. 245 (1998) 319-324
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 319-324
    • Ohnishi, T.1    Taki, T.2    Hiraga, T.3    Arita, N.4    Morita, T.5
  • 13
    • 23344453535 scopus 로고    scopus 로고
    • Rad51 siRNA delivered by HVJ envelope vector enhances the anti-cancer effect of cisplatin
    • Ito M., Yamamoto S., Nimura K., Hiraoka K., Tamai K., and Kaneda Y. Rad51 siRNA delivered by HVJ envelope vector enhances the anti-cancer effect of cisplatin. J. Gene Med. 7 (2005) 1044-1052
    • (2005) J. Gene Med. , vol.7 , pp. 1044-1052
    • Ito, M.1    Yamamoto, S.2    Nimura, K.3    Hiraoka, K.4    Tamai, K.5    Kaneda, Y.6
  • 14
    • 33746866350 scopus 로고    scopus 로고
    • Targeted gene repair: the ups and downs of a promising gene therapy approach
    • de Semir D., and Aran J.M. Targeted gene repair: the ups and downs of a promising gene therapy approach. Curr. Gene Ther. 6 (2006) 481-504
    • (2006) Curr. Gene Ther. , vol.6 , pp. 481-504
    • de Semir, D.1    Aran, J.M.2
  • 15
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD51 filament to the bacterial RecA filament
    • Ogawa T., Yu X., Shinohara A., and 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
  • 16
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson F.E., Stasiak A., and 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
  • 17
    • 2642537689 scopus 로고    scopus 로고
    • Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange
    • Sehorn M.G., Sigurdsson S., Bussen W., Unger V.M., and Sung P. Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange. Nature 429 (2004) 433-437
    • (2004) Nature , vol.429 , pp. 433-437
    • Sehorn, M.G.1    Sigurdsson, S.2    Bussen, W.3    Unger, V.M.4    Sung, P.5
  • 18
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story R.M., Weber I.T., and 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.T.2    Steitz, T.A.3
  • 19
    • 0042738069 scopus 로고    scopus 로고
    • Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2
    • Shin D.S., Pellegrini L., Daniels D.S., Yelent B., Craig L., Bates D., et al. Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2. EMBO J. 22 (2003) 4566-4576
    • (2003) EMBO J. , vol.22 , pp. 4566-4576
    • Shin, D.S.1    Pellegrini, L.2    Daniels, D.S.3    Yelent, B.4    Craig, L.5    Bates, D.6
  • 21
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation
    • Wu Y., He Y., Moya I.A., Qian X., and Luo Y. Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation. Mol. Cell 15 (2004) 423-435
    • (2004) Mol. Cell , vol.15 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5
  • 22
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Chen Z., Yang H., and Pavletich N.P. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 453 (2008) 489-494
    • (2008) Nature , vol.453 , pp. 489-494
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 24
    • 0033538424 scopus 로고    scopus 로고
    • The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR
    • Aihara H., Ito Y., Kurumizaka H., Yokoyama S., and Shibata T. The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR. J. Mol. Biol. 290 (1999) 495-504
    • (1999) J. Mol. Biol. , vol.290 , pp. 495-504
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Yokoyama, S.4    Shibata, T.5
  • 26
    • 2542496073 scopus 로고    scopus 로고
    • Location of tyrosine 315, a target for phosphorylation by cAbl tyrosine kinase, at the edge of the subunit-subunit interface of the human Rad51 filament
    • Conilleau S., Takizawa Y., Tachiwana H., Fleury F., Kurumizaka H., and Takahashi M. Location of tyrosine 315, a target for phosphorylation by cAbl tyrosine kinase, at the edge of the subunit-subunit interface of the human Rad51 filament. J. Mol. Biol. 339 (2004) 797-804
    • (2004) J. Mol. Biol. , vol.339 , pp. 797-804
    • Conilleau, S.1    Takizawa, Y.2    Tachiwana, H.3    Fleury, F.4    Kurumizaka, H.5    Takahashi, M.6
  • 29
    • 33749327819 scopus 로고    scopus 로고
    • Visualizing the assembly of human Rad51 filaments on double-stranded DNA
    • Prasad T.K., Yeykal C.C., and Greene E.C. Visualizing the assembly of human Rad51 filaments on double-stranded DNA. J. Mol. Biol. 363 (2006) 713-728
    • (2006) J. Mol. Biol. , vol.363 , pp. 713-728
    • Prasad, T.K.1    Yeykal, C.C.2    Greene, E.C.3
  • 30
    • 0025955453 scopus 로고
    • Cofactor induced orientation of the DNA bases in single-stranded DNA, complexed with RecA protein: a fluorescence anisotropy and time-decay study
    • Chabbert M., Lami H., and Takahashi M. Cofactor induced orientation of the DNA bases in single-stranded DNA, complexed with RecA protein: a fluorescence anisotropy and time-decay study. J. Biol. Chem. 266 (1991) 5395-5400
    • (1991) J. Biol. Chem. , vol.266 , pp. 5395-5400
    • Chabbert, M.1    Lami, H.2    Takahashi, M.3
  • 31
    • 0032484229 scopus 로고    scopus 로고
    • Nucleotide dependent structural and kinetic changes in Xenopus rad51.1-DNA complex stimulating the strand exchange reaction: destacking of DNA bases and restriction of their local motion
    • Maeshima K., Maraboeuf F., Morimatsu K., Horii T., and Takahashi M. Nucleotide dependent structural and kinetic changes in Xenopus rad51.1-DNA complex stimulating the strand exchange reaction: destacking of DNA bases and restriction of their local motion. J. Mol. Biol. 284 (1998) 689-697
    • (1998) J. Mol. Biol. , vol.284 , pp. 689-697
    • Maeshima, K.1    Maraboeuf, F.2    Morimatsu, K.3    Horii, T.4    Takahashi, M.5
  • 32
    • 37549051303 scopus 로고    scopus 로고
    • Real time measurements of the nucleation, growth and dissociation of single Rad51-DNA nucleoprotein filaments
    • Mine J., Disseau L., Cappello G., Takahashi M., Dutreix M., and Viovy J.L. Real time measurements of the nucleation, growth and dissociation of single Rad51-DNA nucleoprotein filaments. Nucleic Acids Res. 35 (2007) 7171-7187
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7171-7187
    • Mine, J.1    Disseau, L.2    Cappello, G.3    Takahashi, M.4    Dutreix, M.5    Viovy, J.L.6
  • 33
    • 3042791448 scopus 로고    scopus 로고
    • 2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity
    • 2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc. Natl Acad. Sci. USA 101 (2004) 9988-9993
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9988-9993
    • Bugreev, D.V.1    Mazin, A.V.2
  • 34
    • 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-Cornière 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-Cornière, A.4    Fleury, F.5    Weigel, P.6
  • 35
    • 0028921350 scopus 로고
    • Interaction of Tyr103 and Tyr264 of the RecA protein with DNA and nucleotide cofactors. Fluorescence study of engineered proteins
    • Morimatsu K., Horii T., and Takahashi M. Interaction of Tyr103 and Tyr264 of the RecA protein with DNA and nucleotide cofactors. Fluorescence study of engineered proteins. Eur. J. Biochem. 228 (1995) 779-785
    • (1995) Eur. J. Biochem. , vol.228 , pp. 779-785
    • Morimatsu, K.1    Horii, T.2    Takahashi, M.3
  • 36
    • 0026584599 scopus 로고
    • Structure of the E. coli recA protein-ADP complex
    • Story R.M., and Steitz T.A. Structure of the E. coli recA protein-ADP complex. Nature 355 (1992) 374-376
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 37
    • 0025344113 scopus 로고
    • Characterization of the DNA binding activity of stable RecA-DNA complexes. Interaction between the two DNA binding sites within RecA helical filaments
    • Müller B., Koller T., and Stasiak A. Characterization of the DNA binding activity of stable RecA-DNA complexes. Interaction between the two DNA binding sites within RecA helical filaments. J. Mol. Biol. 212 (1990) 97-112
    • (1990) J. Mol. Biol. , vol.212 , pp. 97-112
    • Müller, B.1    Koller, T.2    Stasiak, A.3
  • 38
    • 0035157386 scopus 로고    scopus 로고
    • Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA filament
    • De Zutter J.K., Forget A.L., Logan K.M., and Knight K.L. Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA filament. Structure 9 (2001) 47-55
    • (2001) Structure , vol.9 , pp. 47-55
    • De Zutter, J.K.1    Forget, A.L.2    Logan, K.M.3    Knight, K.L.4
  • 39
    • 27144526413 scopus 로고    scopus 로고
    • Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change
    • Qian X., Wu Y., He Y., and Luo Y. Crystal structure of Methanococcus voltae RadA in complex with ADP: hydrolysis-induced conformational change. Biochemistry 44 (2005) 13753-13761
    • (2005) Biochemistry , vol.44 , pp. 13753-13761
    • Qian, X.1    Wu, Y.2    He, Y.3    Luo, Y.4
  • 40
    • 0030772339 scopus 로고    scopus 로고
    • Nucleotide cofactor-dependent structural change of Xenopus laevis Rad51 protein filament detected by small-angle neutron scattering measurements in solution
    • Ellouze C., Kim H.K., Maeshima K., Tuite E., Morimatsu K., Horii T., et al. Nucleotide cofactor-dependent structural change of Xenopus laevis Rad51 protein filament detected by small-angle neutron scattering measurements in solution. Biochemistry 36 (1997) 13524-13529
    • (1997) Biochemistry , vol.36 , pp. 13524-13529
    • Ellouze, C.1    Kim, H.K.2    Maeshima, K.3    Tuite, E.4    Morimatsu, K.5    Horii, T.6
  • 41
    • 32644466860 scopus 로고    scopus 로고
    • Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function
    • Chi P., Van Komen S., Sehorn M.G., Sigurdsson S., and Sung P. Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair (Amst) 5 (2006) 381-391
    • (2006) DNA Repair (Amst) , vol.5 , pp. 381-391
    • Chi, P.1    Van Komen, S.2    Sehorn, M.G.3    Sigurdsson, S.4    Sung, P.5
  • 42
    • 35748953402 scopus 로고    scopus 로고
    • Altered DNA repair and recombination responses in mouse cells expressing wildtype or mutant forms of RAD51
    • Rukść A., Birmingham E.C., and Baker M.D. Altered DNA repair and recombination responses in mouse cells expressing wildtype or mutant forms of RAD51. DNA Repair (Amst) 6 (2007) 1876-1889
    • (2007) DNA Repair (Amst) , vol.6 , pp. 1876-1889
    • Rukść, A.1    Birmingham, E.C.2    Baker, M.D.3
  • 43
    • 33947396376 scopus 로고    scopus 로고
    • The human Rad51 K133A mutant is functional for DNA double-strand break repair in human cells
    • Forget A.L., Loftus M.S., McGrew D.A., Bennett B.T., and Knight K.L. The human Rad51 K133A mutant is functional for DNA double-strand break repair in human cells. Biochemistry 46 (2007) 3566-3575
    • (2007) Biochemistry , vol.46 , pp. 3566-3575
    • Forget, A.L.1    Loftus, M.S.2    McGrew, D.A.3    Bennett, B.T.4    Knight, K.L.5
  • 44
    • 0020997753 scopus 로고
    • Binding of RecA protein to single-stranded nucleic acids: spectroscopic studies using fluorescent polynucleotides
    • Cazenave C., Toulme J.J., and Helene C. Binding of RecA protein to single-stranded nucleic acids: spectroscopic studies using fluorescent polynucleotides. EMBO J. 2 (1983) 2247-2251
    • (1983) EMBO J. , vol.2 , pp. 2247-2251
    • Cazenave, C.1    Toulme, J.J.2    Helene, C.3
  • 45
    • 0018034008 scopus 로고
    • Interaction of tobacco mosaic virus protein with synthetic polynucleotides containing a fluorescent label
    • Ledneva R.K., Razjivim A.P., Kost A.A., and Bogdanov A.A. Interaction of tobacco mosaic virus protein with synthetic polynucleotides containing a fluorescent label. Nucleic Acids Res. 5 (1978) 4225-4243
    • (1978) Nucleic Acids Res. , vol.5 , pp. 4225-4243
    • Ledneva, R.K.1    Razjivim, A.P.2    Kost, A.A.3    Bogdanov, A.A.4
  • 46
    • 0035945250 scopus 로고    scopus 로고
    • Structural study of DNA duplexes containing the (6-4) photoproduct by fluorescence resonance energy transfer
    • Mizukoshi T., Kodama T.S., Fujiwara Y., Furuno T., Nakanishi M., and Iwai S. Structural study of DNA duplexes containing the (6-4) photoproduct by fluorescence resonance energy transfer. Nucleic Acids Res. 29 (2001) 4948-4954
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4948-4954
    • Mizukoshi, T.1    Kodama, T.S.2    Fujiwara, Y.3    Furuno, T.4    Nakanishi, M.5    Iwai, S.6


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