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Volumn 35, Issue 17, 2007, Pages 5646-5657

Real-time assembly and disassembly of human RAD51 filaments on individual DNA molecules

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; RAD51 PROTEIN; SINGLE STRANDED DNA;

EID: 34848835235     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm629     Document Type: Article
Times cited : (93)

References (45)
  • 1
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West,S.C. (2003) Molecular views of recombination proteins and their control. Nat. Rev. Mol. Cell Biol., 4, 435-445.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 435-445
    • West, S.C.1
  • 2
    • 4143079350 scopus 로고    scopus 로고
    • Homologous recombination: Down to the wire
    • Wyman,C. and Kanaar,R. (2004) Homologous recombination: Down to the wire. Curr. Biol, 14, R629-R631.
    • (2004) Curr. Biol , vol.14
    • Wyman, C.1    Kanaar, R.2
  • 4
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • S
    • Yu,X., Jacobs,S.A., West,S.C., Ogawa,T. and Egelman,E.H. (2001) Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc. Natl Acad. Sci. USA, 98, 8419-8424.S
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8419-8424
    • Yu, X.1    Jacobs, S.A.2    West, S.C.3    Ogawa, T.4    Egelman, E.H.5
  • 6
    • 20844461121 scopus 로고    scopus 로고
    • Human Rad51 filaments on double- and single-stranded DNA: Correlating regular and irregular forms with recombination function
    • Ristic,D., Modesti,M., van der Heijden,T., van Noort,J., Dekker,C., Kanaar,R. and Wyman,C. (2005) Human Rad51 filaments on double- and single-stranded DNA: Correlating regular and irregular forms with recombination function. Nucleic Acids Res., 33, 3292-3302.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3292-3302
    • Ristic, D.1    Modesti, M.2    van der Heijden, T.3    van Noort, J.4    Dekker, C.5    Kanaar, R.6    Wyman, C.7
  • 8
    • 0027167689 scopus 로고
    • Similarity of the yeast Rad51 filament to the bacterial RecA filament
    • Ogawa,T., Yu,X., Shinohara,A. and Egelman,E.H. (1993) Similarity of the yeast Rad51 filament to the bacterial RecA filament. Science, 259, 1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 9
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analog of Escherichia coli RecA
    • Benson,F.E., Stasiak,A. and West,S.C. (1994) Purification and characterization of the human Rad51 protein, an analog of Escherichia coli RecA. EMBO J., 13, 5764-5771.
    • (1994) EMBO J , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 10
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a Rad51-ssdna nucleoprotein filament with polarity opposite to that of RecA
    • Sung,P. and Robberson,D.L. (1995) DNA strand exchange mediated by a Rad51-ssdna nucleoprotein filament with polarity opposite to that of RecA. Cell, 82, 453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 12
    • 0033529216 scopus 로고    scopus 로고
    • RecA polymerization on double-stranded DNA by using single-molecule manipulation: The role of ATP hydrolysis
    • Shivashankar,G.V., Feingold,M., Kricheysky,O. and Libchaber,A. (1999) RecA polymerization on double-stranded DNA by using single-molecule manipulation: The role of ATP hydrolysis. Proc. Natl Acad. Sci. USA 96, 7916-7921.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7916-7921
    • Shivashankar, G.V.1    Feingold, M.2    Kricheysky, O.3    Libchaber, A.4
  • 13
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: Structure, function, and role in recombinational DNA repair
    • Roca,A.I. and Cox,M.M. (1997) RecA protein: Structure, function, and role in recombinational DNA repair. Prog. Nucleic Acid Res. Mol. Biol., 56, 129-223.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2
  • 14
    • 33750296934 scopus 로고    scopus 로고
    • Direct observation of individual RecA filaments assembling on single DNA molecules
    • Galletto,R., Amitani,I., Baskin,R.J. and Kowalczykowski,S.C. (2006) Direct observation of individual RecA filaments assembling on single DNA molecules. Nature, 443, 875-878.
    • (2006) Nature , vol.443 , pp. 875-878
    • Galletto, R.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 15
    • 33746713745 scopus 로고    scopus 로고
    • Real-time observation of RecA filament dynamics with single monomer resolution
    • Joo,C., McKinney,S.A., Nakamura,M., Rasnik,I., Myong,S. and Ha,T. (2006) Real-time observation of RecA filament dynamics with single monomer resolution. Cell, 126, 515-527.
    • (2006) Cell , vol.126 , pp. 515-527
    • Joo, C.1    McKinney, S.A.2    Nakamura, M.3    Rasnik, I.4    Myong, S.5    Ha, T.6
  • 16
    • 1642264199 scopus 로고    scopus 로고
    • Conformational changes modulate the activity of human RAD51 protein
    • Liu,Y.L., Stasiak,A.Z., Mcllwraith,M.J., Stasiak,A. and West,S.C. (2004) Conformational changes modulate the activity of human RAD51 protein. J. Mol. Biol., 337, 817-827.
    • (2004) J. Mol. Biol , vol.337 , pp. 817-827
    • Liu, Y.L.1    Stasiak, A.Z.2    Mcllwraith, M.J.3    Stasiak, A.4    West, S.C.5
  • 17
    • 0033527668 scopus 로고    scopus 로고
    • The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA
    • De Zutter,S.K. and Knight,K.L. (1999) The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA. J. Mol. Biol., 293, 769-780.
    • (1999) J. Mol. Biol , vol.293 , pp. 769-780
    • De Zutter, S.K.1    Knight, K.L.2
  • 18
    • 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, 9988-9993.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9988-9993
    • Bugreev, D.V.1    Mazin, A.V.2
  • 20
  • 21
    • 0034088461 scopus 로고    scopus 로고
    • Two time constants for the binding of proteins to DNA from micromechanical data
    • Turner,M.S. (2000) Two time constants for the binding of proteins to DNA from micromechanical data. Biophys. J., 78, 600-607.
    • (2000) Biophys. J , vol.78 , pp. 600-607
    • Turner, M.S.1
  • 23
    • 0035812601 scopus 로고    scopus 로고
    • Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently
    • Yang,S.X., VanLoock,M.S., Yu,X. and Egelman,E.H. (2001) Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently. J. Mol. Biol., 312, 999-1009.
    • (2001) J. Mol. Biol , vol.312 , pp. 999-1009
    • Yang, S.X.1    VanLoock, M.S.2    Yu, X.3    Egelman, E.H.4
  • 24
    • 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. (2006) Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair, 5, 381-391.
    • (2006) DNA Repair , vol.5 , pp. 381-391
    • Chi, P.1    Van Komen, S.2    Sehorn, M.G.3    Sigurdsson, S.4    Sung, P.5
  • 25
    • 0032513226 scopus 로고    scopus 로고
    • Binding of Rad51p to DNA - interaction of Rad51p with single- and double-stranded DNA
    • Namsaraev,E.A. and Berg,P. (1998) Binding of Rad51p to DNA - interaction of Rad51p with single- and double-stranded DNA. J. Biol. Chem., 273, 6177-6182.
    • (1998) J. Biol. Chem , vol.273 , pp. 6177-6182
    • Namsaraev, E.A.1    Berg, P.2
  • 26
    • 0030768931 scopus 로고    scopus 로고
    • The Hill equation revisited: Uses and misuses
    • Weiss,J.N. (1997) The Hill equation revisited: Uses and misuses. FASEB J., 11, 835-841.
    • (1997) FASEB J , vol.11 , pp. 835-841
    • Weiss, J.N.1
  • 28
    • 0037177845 scopus 로고    scopus 로고
    • Biochemical characterization of the human RAD51 protein - II. Adenosine nucleotide binding and competition
    • Tombline,G., Shim,K.S. and Fishel,R. (2002) Biochemical characterization of the human RAD51 protein - II. Adenosine nucleotide binding and competition. J. Biol. Chem., 277, 14426-14433.
    • (2002) J. Biol. Chem , vol.277 , pp. 14426-14433
    • Tombline, G.1    Shim, K.S.2    Fishel, R.3
  • 29
    • 0032937079 scopus 로고    scopus 로고
    • Estimating the persistence length of a worm-like chain molecule from force-extension measurements
    • Bouchiat,C., Wang,M.D., Allemand,J.F., Strick,T., Block,S.M. and Croquette,V. (1999) Estimating the persistence length of a worm-like chain molecule from force-extension measurements. Biophys. J., 76, 409-413.
    • (1999) Biophys. J , vol.76 , pp. 409-413
    • Bouchiat, C.1    Wang, M.D.2    Allemand, J.F.3    Strick, T.4    Block, S.M.5    Croquette, V.6
  • 30
    • 0033621088 scopus 로고    scopus 로고
    • Polymerization and mechanical properties of single RecA-DNA filaments
    • Hegner,M., Smith,S.B. and Bustamante,C. (1999) Polymerization and mechanical properties of single RecA-DNA filaments. Proc. Natl Acad. Sci. USA, 96, 10109-10114.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 10109-10114
    • Hegner, M.1    Smith, S.B.2    Bustamante, C.3
  • 31
    • 33749522198 scopus 로고    scopus 로고
    • Dissecting elastic heterogeneity along DNA molecules coated partly with Rad51 using concurrent fluorescence microscopy and optical tweezers
    • van Mameren,J., Modesti,M., Kanaar,R., Wyman,C., Wuite,G.J.L. and Peterman,E.J.G. (2006) Dissecting elastic heterogeneity along DNA molecules coated partly with Rad51 using concurrent fluorescence microscopy and optical tweezers. Biophys. J., 91, L78-L80.
    • (2006) Biophys. J , vol.91
    • van Mameren, J.1    Modesti, M.2    Kanaar, R.3    Wyman, C.4    Wuite, G.J.L.5    Peterman, E.J.G.6
  • 33
    • 0034711381 scopus 로고    scopus 로고
    • Reconstitution of the strand invasion step of double-strand break repair using human Rad51 Rad52 and RPA proteins
    • McIlwraith,M.J., Van Dyck,E., Masson,J.Y., Stasiak,A.Z., Stasiak,A. and West,S.C. (2000) 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) J. Mol. Biol , vol.304 , pp. 151-164
    • McIlwraith, M.J.1    Van Dyck, E.2    Masson, J.Y.3    Stasiak, A.Z.4    Stasiak, A.5    West, S.C.6
  • 34
    • 0030811492 scopus 로고    scopus 로고
    • Purification of human Rad51 protein by selective spermidine precipitation
    • Baumann,P., Benson,F.E., Hajibagheri,N. and West,S.C. (1997) Purification of human Rad51 protein by selective spermidine precipitation. Mutat. Res. DNA Repair, 384, 65-72.
    • (1997) Mutat. Res. DNA Repair , vol.384 , pp. 65-72
    • Baumann, P.1    Benson, F.E.2    Hajibagheri, N.3    West, S.C.4
  • 35
    • 0037177859 scopus 로고    scopus 로고
    • Biochemical characterization of the human RAD51 protein - III. - Modulation of DNA binding by adenosine nucleotides
    • Tombline,G., Heinen,C.D., Shim,K.S. and Fishel,R. (2002) Biochemical characterization of the human RAD51 protein - III. - Modulation of DNA binding by adenosine nucleotides. J. Biol. Chem., 277, 14434-14442.
    • (2002) J. Biol. Chem , vol.277 , pp. 14434-14442
    • Tombline, G.1    Heinen, C.D.2    Shim, K.S.3    Fishel, R.4
  • 36
    • 0042738069 scopus 로고    scopus 로고
    • Shin,D.S., Pellegrini,L., Daniels,D.S., Yelent,B., Craig,L., Bates,D., Yu,D.S., Shivji,M.K., Hitomi, and C., (2003) Full-length archaeal Rad51 structure and mutants: Mechanisms for RAD51 assembly and control by BRCA2. EMBO J., 22, 4566-4576.
    • Shin,D.S., Pellegrini,L., Daniels,D.S., Yelent,B., Craig,L., Bates,D., Yu,D.S., Shivji,M.K., Hitomi, and C., (2003) Full-length archaeal Rad51 structure and mutants: Mechanisms for RAD51 assembly and control by BRCA2. EMBO J., 22, 4566-4576.
  • 37
    • 33845604556 scopus 로고    scopus 로고
    • DNA double-strand break repair: All's well that ends well
    • Wyman,C. and Kanaar,R. (2006) DNA double-strand break repair: All's well that ends well. Annu. Rev. Genet., 40, 363-383.
    • (2006) Annu. Rev. Genet , vol.40 , pp. 363-383
    • Wyman, C.1    Kanaar, R.2
  • 38
    • 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. (2007) Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2. Nat. Struct. Mol. Biol., 14, 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
  • 39
    • 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. (2007) Interaction with the BRCA2 C terminus protects RAD51-DNA filaments from disassembly by BRC repeats. Nat. Struct. Mol. Biol., 14, 475-483.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 475-483
    • Davies, O.R.1    Pellegrini, L.2
  • 40
    • 34249892132 scopus 로고    scopus 로고
    • Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2
    • Petalcorin,M.I., Galkin,V.E., Yu,X., Egelman,E.H. and Boulton,S.J. (2007) Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2. Proc. Natl Acad. Sci. USA, 104 8299-8304.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8299-8304
    • Petalcorin, M.I.1    Galkin, V.E.2    Yu, X.3    Egelman, E.H.4    Boulton, S.J.5
  • 41
    • 3242878504 scopus 로고    scopus 로고
    • DNA recombination, chromosomal stability and carcinogenesis: Insights into the role of BRCA2
    • Shivji,M.K.K. and Venkitaraman,A.R. (2004) DNA recombination, chromosomal stability and carcinogenesis: Insights into the role of BRCA2. DNA Repair, 3, 835-843.
    • (2004) DNA Repair , vol.3 , pp. 835-843
    • Shivji, M.K.K.1    Venkitaraman, A.R.2
  • 42
    • 33748681302 scopus 로고    scopus 로고
    • Some disassembly required: Role of DNA translocases in the disruption of recombination intermediates and dead-end complexes
    • Symington,L.S. and Heyer,W.D. (2006) Some disassembly required: Role of DNA translocases in the disruption of recombination intermediates and dead-end complexes. Genes Dev., 20, 2479-2486.
    • (2006) Genes Dev , vol.20 , pp. 2479-2486
    • Symington, L.S.1    Heyer, W.D.2
  • 43
    • 0035945241 scopus 로고    scopus 로고
    • Bypass of heterology during strand transfer by Saccharomyces cerevisiae Rad51 protein
    • Holmes,V.F., Benjamin,K.R., Crisona,N.J. and Cozzarelli,N.R. (2001) Bypass of heterology during strand transfer by Saccharomyces cerevisiae Rad51 protein. Nucleic Acids Res., 29, 5052-5057.
    • (2001) Nucleic Acids Res , vol.29 , pp. 5052-5057
    • Holmes, V.F.1    Benjamin, K.R.2    Crisona, N.J.3    Cozzarelli, N.R.4
  • 44
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • Lusetti,S.L. and Cox,M.M. (2002) The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. Annu. Rev. Biochem., 71, 71-100.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2


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