메뉴 건너뛰기




Volumn 141, Issue 2, 2007, Pages 147-156

Visualization of RecA filaments and DNA by fluorescence microscopy

Author keywords

DNA protein interaction; Fluorescence label of protein; Homologous recombination; Microscopic observations; RecA protein

Indexed keywords

CYSTEINE; DNA ANTIBODY; MONOCLONAL ANTIBODY; RECA PROTEIN;

EID: 34248674044     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm033     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco, P.R., Tracy, R.B., and Kowalczykowski, S.C. (1998) DNA strand exchange proteins: a biochemical and physical comparison. Front. Biosci. 3, D570-D603
    • (1998) Front. Biosci , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 2
    • 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
  • 3
    • 0024360742 scopus 로고
    • Helical RecA nucleoprotein filaments mediate homologous pairing and strand exchange
    • Radding, C.M. (1989) Helical RecA nucleoprotein filaments mediate homologous pairing and strand exchange. Biochim. Biophys. Acta 1008, 131-145
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 131-145
    • Radding, C.M.1
  • 4
    • 0000133316 scopus 로고
    • Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments
    • Shibata, T., DasGupta, C., Cunningham, R.P., and Radding, C.M. (1979) Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments. Proc. Natl Acad. Sci. USA 76, 1638-1642
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 1638-1642
    • Shibata, T.1    DasGupta, C.2    Cunningham, R.P.3    Radding, C.M.4
  • 5
    • 0346660225 scopus 로고
    • Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli
    • McEntee, K., Weinstock, G.M., and Lehman, I.R. (1979) Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli. Proc. Natl Acad. Sci. USA 76, 2615-2619
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 2615-2619
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 6
    • 0006704537 scopus 로고
    • Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA
    • Flory, J., Tsang, S.S., and Muniyappa, K. (1984) Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA. Proc. Natl Acad. Sci. USA 81, 7026-7030
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 7026-7030
    • Flory, J.1    Tsang, S.S.2    Muniyappa, K.3
  • 7
    • 0019955608 scopus 로고
    • Electron microscopic visualization of recA-DNA filaments: Evidence for a cyclic extension of duplex DNA
    • Dunn, K., Chrysogelos, S., and Griffith, J. (1982) Electron microscopic visualization of recA-DNA filaments: evidence for a cyclic extension of duplex DNA. Cell 28, 757-765
    • (1982) Cell , vol.28 , pp. 757-765
    • Dunn, K.1    Chrysogelos, S.2    Griffith, J.3
  • 8
    • 0023008741 scopus 로고
    • Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP
    • Egelman, E.H. and Stasiak, A. (1986) Structure of helical RecA-DNA complexes. Complexes formed in the presence of ATP-gamma-S or ATP. J. Mol. Biol. 191, 677-697
    • (1986) J. Mol. Biol , vol.191 , pp. 677-697
    • Egelman, E.H.1    Stasiak, A.2
  • 9
    • 0019888429 scopus 로고
    • Elongation of duplex DNA by recA protein
    • Stasiak, A., Di Capua, E., and Koller, T. (1981) Elongation of duplex DNA by recA protein. J. Mol. Biol. 151, 557-564
    • (1981) J. Mol. Biol , vol.151 , pp. 557-564
    • Stasiak, A.1    Di Capua, E.2    Koller, T.3
  • 10
    • 0025886164 scopus 로고
    • Activation of recA protein: The pitch of the helical complex with single-stranded DNA
    • Hewat, E.A., Ruigrok, R.W., and DiCapua, E. (1991) Activation of recA protein: the pitch of the helical complex with single-stranded DNA. EMBO J. 10, 2695-2698
    • (1991) EMBO J , vol.10 , pp. 2695-2698
    • Hewat, E.A.1    Ruigrok, R.W.2    DiCapua, E.3
  • 11
    • 0025079221 scopus 로고
    • Complexes of RecA protein in solution. A study by small angle neutron scattering
    • DiCapua, E., Schnarr, M., Ruigrok, R.W., Lindner, P., and Timmins, P.A. (1990) Complexes of RecA protein in solution. A study by small angle neutron scattering. J. Mol. Biol. 214, 557-570
    • (1990) J. Mol. Biol , vol.214 , pp. 557-570
    • DiCapua, E.1    Schnarr, M.2    Ruigrok, R.W.3    Lindner, P.4    Timmins, P.A.5
  • 12
    • 0022360935 scopus 로고
    • The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange
    • Register, J.C., 3rd and Griffith, J. (1985) The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange. J. Biol. Chem. 260, 12308-12312
    • (1985) J. Biol. Chem , vol.260 , pp. 12308-12312
    • Register 3rd, J.C.1    Griffith, J.2
  • 13
    • 0035824581 scopus 로고    scopus 로고
    • RecA protein filaments disassemble in the 5′ to 3′ direction on single-stranded DNA
    • Bork, J.M., Cox, M.M., and Inman, R.B. (2001) RecA protein filaments disassemble in the 5′ to 3′ direction on single-stranded DNA. J. Biol. Chem. 276, 45740-45743
    • (2001) J. Biol. Chem , vol.276 , pp. 45740-45743
    • Bork, J.M.1    Cox, M.M.2    Inman, R.B.3
  • 14
    • 0031556955 scopus 로고    scopus 로고
    • RecA protein filaments: End-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins
    • Shan, Q., Bork, J.M., Webb, B.L., Inman, R.B., and Cox, M.M. (1997) RecA protein filaments: end-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins. J. Mol. Biol. 265, 519-540
    • (1997) J. Mol. Biol , vol.265 , pp. 519-540
    • Shan, Q.1    Bork, J.M.2    Webb, B.L.3    Inman, R.B.4    Cox, M.M.5
  • 15
    • 34248636947 scopus 로고    scopus 로고
    • Koller, T., Di Capua, E., and Stasiak, A. (1983) Complexes of recA protein with single stranded DNA in Mechanisms of DNA Replication and Recombination (Cozzarelli, N.R., ed.) pp. 723-729. Alan R. Liss, New York
    • Koller, T., Di Capua, E., and Stasiak, A. (1983) Complexes of recA protein with single stranded DNA in Mechanisms of DNA Replication and Recombination (Cozzarelli, N.R., ed.) pp. 723-729. Alan R. Liss, New York
  • 17
    • 0023041833 scopus 로고
    • Fibers of RecA protein and complexes of RecA protein and single-stranded phi X174 DNA as visualized by negative-stain electron microscopy
    • Williams, R.C. and Spengler, S.J. (1986) Fibers of RecA protein and complexes of RecA protein and single-stranded phi X174 DNA as visualized by negative-stain electron microscopy. J. Mol. Biol. 187, 109-118
    • (1986) J. Mol. Biol , vol.187 , pp. 109-118
    • Williams, R.C.1    Spengler, S.J.2
  • 18
    • 0026666652 scopus 로고
    • Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible
    • Yu, X. and Egelman, E.H. (1992) Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible. J. Mol. Biol. 227, 334-346
    • (1992) J. Mol. Biol , vol.227 , pp. 334-346
    • Yu, X.1    Egelman, E.H.2
  • 19
    • 0024843435 scopus 로고
    • Visualization of RecA protein and its complexes with DNA by quick-freeze/ deep-etch electron microscopy
    • Heuser, J. and Griffith, J. (1989) Visualization of RecA protein and its complexes with DNA by quick-freeze/ deep-etch electron microscopy. J. Mol. Biol. 210, 473-484
    • (1989) J. Mol. Biol , vol.210 , pp. 473-484
    • Heuser, J.1    Griffith, J.2
  • 20
    • 8544258063 scopus 로고    scopus 로고
    • Crystal structure of RecA from Deinococcus radiodurans: Insights into the structural basis of extreme radioresistance
    • Rajan, E. and Bell, C.E. (2004) Crystal structure of RecA from Deinococcus radiodurans: insights into the structural basis of extreme radioresistance. J. Mol. Biol. 344, 951-963
    • (2004) J. Mol. Biol , vol.344 , pp. 951-963
    • Rajan, E.1    Bell, C.E.2
  • 21
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R.M., Weber, I.T., and Steitz, T.A. (1992) The structure of the E. coli recA protein monomer and polymer. Nature 355, 318-325
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 22
    • 0034671684 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AIF(4): Implications for decreased ATPase activity and molecular aggregation
    • Datta, S., Prabu, M.M., Vaze, M.B., Ganesh, N., Chandra, N.R., Muniyappa, K., and Vijayan, M. (2000) Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AIF(4): implications for decreased ATPase activity and molecular aggregation. Nucleic Acids Res. 28, 4964-4973
    • (2000) Nucleic Acids Res , vol.28 , pp. 4964-4973
    • Datta, S.1    Prabu, M.M.2    Vaze, M.B.3    Ganesh, N.4    Chandra, N.R.5    Muniyappa, K.6    Vijayan, M.7
  • 23
    • 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. (2004) Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation. Mol. Cell 15, 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
  • 24
    • 12844272179 scopus 로고    scopus 로고
    • Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence
    • Wu, Y., Qian, X., He, Y., Moya, I.A., and Luo, Y. (2005) Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence. J. Biol. Chem. 280, 722-728
    • (2005) J. Biol. Chem , vol.280 , pp. 722-728
    • Wu, Y.1    Qian, X.2    He, Y.3    Moya, I.A.4    Luo, Y.5
  • 28
    • 0031940556 scopus 로고    scopus 로고
    • RecA protein has extremely high cooperativity for substrate in its ATPase activity
    • Mikawa, T., Masui, R., and Kuramitsu, S. (1998) RecA protein has extremely high cooperativity for substrate in its ATPase activity. J. Biochem. (Tokyo) 123, 450-457
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 450-457
    • Mikawa, T.1    Masui, R.2    Kuramitsu, S.3
  • 29
    • 0022341552 scopus 로고
    • Monoclonal antibodies with specific effects on partial activities of recA protein of Escherichia coli
    • Makino, O., Shibata, Y., Maeda, H., Shibata, T., and Ando, T. (1985) Monoclonal antibodies with specific effects on partial activities of recA protein of Escherichia coli. J. Biol. Chem. 260, 15402-15405
    • (1985) J. Biol. Chem , vol.260 , pp. 15402-15405
    • Makino, O.1    Shibata, Y.2    Maeda, H.3    Shibata, T.4    Ando, T.5
  • 30
    • 0026671585 scopus 로고
    • Epitope mapping of anti-recA protein IgGs by region specified polymerase chain reaction mutagenesis
    • Ikeda, M., Hamano, K., and Shibata, T. (1992) Epitope mapping of anti-recA protein IgGs by region specified polymerase chain reaction mutagenesis. J. Biol. Chem. 267, 6291-6296
    • (1992) J. Biol. Chem , vol.267 , pp. 6291-6296
    • Ikeda, M.1    Hamano, K.2    Shibata, T.3
  • 31
    • 0022218737 scopus 로고
    • Intermediates in homologous pairing promoted by recA protein. Isolation and characterization of active presynaptic complexes
    • Tsang, S.S., Muniyappa, K., Azhderian, E., Gonda, D.K., Radding, C.M., Flory, J., and Chase, J.W. (1985) Intermediates in homologous pairing promoted by recA protein. Isolation and characterization of active presynaptic complexes. J. Mol. Biol. 185, 295-309
    • (1985) J. Mol. Biol , vol.185 , pp. 295-309
    • Tsang, S.S.1    Muniyappa, K.2    Azhderian, E.3    Gonda, D.K.4    Radding, C.M.5    Flory, J.6    Chase, J.W.7
  • 32
    • 0025301074 scopus 로고
    • Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure
    • Muniyappa, K., Williams, K., Chase, J.W., and Radding, J.M. (1990) Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure. Nucleic Acids Res. 18, 3967-3973
    • (1990) Nucleic Acids Res , vol.18 , pp. 3967-3973
    • Muniyappa, K.1    Williams, K.2    Chase, J.W.3    Radding, J.M.4
  • 33
    • 0023108585 scopus 로고
    • Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction
    • Kowalczykowski, S.C., Clow, J., Somani, R., and Varghese, A. (1987) Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction. J. Mol. Biol. 193, 81-95
    • (1987) J. Mol. Biol , vol.193 , pp. 81-95
    • Kowalczykowski, S.C.1    Clow, J.2    Somani, R.3    Varghese, A.4
  • 34
    • 0024378045 scopus 로고
    • Enhancement of Escherichia coli RecA protein enzymatic function by dATP
    • Menetski, J.P. and Kowalczykowski, S.C. (1989) Enhancement of Escherichia coli RecA protein enzymatic function by dATP. Biochemistry 28, 5871-5881
    • (1989) Biochemistry , vol.28 , pp. 5871-5881
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 35
    • 0023645170 scopus 로고
    • Translocation of Escherichia coli recA protein from a single-stranded tail to contiguous duplex DNA
    • Shaner, S.L. and Radding, C.M. (1987) Translocation of Escherichia coli recA protein from a single-stranded tail to contiguous duplex DNA. J. Biol. Chem. 262, 9211-9219
    • (1987) J. Biol. Chem , vol.262 , pp. 9211-9219
    • Shaner, S.L.1    Radding, C.M.2
  • 36
    • 0024539083 scopus 로고
    • Dissociation pathway for recA nucleoprotein filaments formed on linear duplex DNA
    • Lindsley, J.E. and Cox, M.M. (1989) Dissociation pathway for recA nucleoprotein filaments formed on linear duplex DNA. J. Mol. Biol. 205, 695-711
    • (1989) J. Mol. Biol , vol.205 , pp. 695-711
    • Lindsley, J.E.1    Cox, M.M.2
  • 37
    • 0025291850 scopus 로고
    • Assembly and disassembly of RecA protein filaments occur at opposite filament ends. Relationship to DNA strand exchange
    • Lindsley, J.E. and Cox, M.M. (1990) Assembly and disassembly of RecA protein filaments occur at opposite filament ends. Relationship to DNA strand exchange. J. Biol. Chem. 265, 9043-9054
    • (1990) J. Biol. Chem , vol.265 , pp. 9043-9054
    • Lindsley, J.E.1    Cox, M.M.2
  • 38
    • 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., and Egelman, E.H. (1998) 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, 985-992
    • (1998) J. Mol. Biol , vol.283 , pp. 985-992
    • Yu, X.1    Shibata, T.2    Egelman, E.H.3
  • 39
    • 0032514675 scopus 로고    scopus 로고
    • RecA binding to a single double-stranded DNA molecule: A possible role of DNA conformational fluctuations
    • Leger, J.F., Robert, J., Bourdieu, L., Chatenay, D., and Marko, J.F. (1998) RecA binding to a single double-stranded DNA molecule: a possible role of DNA conformational fluctuations. Proc. Natl Acad. Sci. USA 95, 12295-12299
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12295-12299
    • Leger, J.F.1    Robert, J.2    Bourdieu, L.3    Chatenay, D.4    Marko, J.F.5
  • 40
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.