메뉴 건너뛰기




Volumn 288, Issue 37, 2013, Pages 26397-26409

Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair

Author keywords

[No Author keywords available]

Indexed keywords

ATP-ASE ACTIVITY; DNA HELICASES; DNA REPLICATION FORKS; HOLLIDAY JUNCTIONS; STALLED FORKS;

EID: 84884193802     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.500223     Document Type: Article
Times cited : (37)

References (74)
  • 1
    • 0030737725 scopus 로고    scopus 로고
    • Stable DNA replication: Interplay between DNA replication, homologous recombination, and transcription
    • Kogoma, T. (1997) Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription. Microbiol. Mol. Biol. Rev. 61, 212-238
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 212-238
    • Kogoma, T.1
  • 2
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophageγ
    • Kuzminov, A. (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophageγ. Microbiol. Mol. Biol. Rev. 63, 751-813
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 3
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination- dependent replication
    • Kowalczykowski, S. C. (2000) Initiation of genetic recombination and recombination- dependent replication. Trends Biochem. Sci. 25, 156-165
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 4
    • 0032582794 scopus 로고    scopus 로고
    • RuvAB acts at arrested replication forks
    • Seigneur, M., Bidnenko, V., Ehrlich, S. D., and Michel, B. (1998) RuvAB acts at arrested replication forks. Cell 95, 419-430
    • (1998) Cell , vol.95 , pp. 419-430
    • Seigneur, M.1    Bidnenko, V.2    Ehrlich, S.D.3    Michel, B.4
  • 6
    • 0035679232 scopus 로고    scopus 로고
    • Recombinational DNA repair of damaged replication forks in Escherichia coli: Questions
    • Cox, M. M. (2001) Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu. Rev. Genet. 35, 53-82
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 53-82
    • Cox, M.M.1
  • 7
    • 0036809865 scopus 로고    scopus 로고
    • Replicating past lesions in DNA
    • McGlynn, P., and Lloyd, R. (2002) Replicating past lesions in DNA. Mol. Cell 10, 700-701
    • (2002) Mol. Cell , vol.10 , pp. 700-701
    • McGlynn, P.1    Lloyd, R.2
  • 8
    • 1642443168 scopus 로고    scopus 로고
    • Mechanisms of replication fork restart in Escherichia coli
    • Marians, K. J. (2004) Mechanisms of replication fork restart in Escherichia coli. Philos. Trans. R. Soc. Lond. B Biol. Sci. 359, 71-77
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.359 , pp. 71-77
    • Marians, K.J.1
  • 10
    • 0036683338 scopus 로고    scopus 로고
    • Genome stability and the processing of damaged replication forks by RecG
    • McGlynn, P., and Lloyd, R. (2002) Genome stability and the processing of damaged replication forks by RecG. Trends Genet. 18, 413-419
    • (2002) Trends Genet. , vol.18 , pp. 413-419
    • McGlynn, P.1    Lloyd, R.2
  • 11
    • 0034026997 scopus 로고    scopus 로고
    • Replication and recombination intersect
    • Marians, K. J. (2000) Replication and recombination intersect. Curr. Opin. Genet. Dev. 10, 151-156
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 151-156
    • Marians, K.J.1
  • 12
    • 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
  • 14
    • 0035834755 scopus 로고    scopus 로고
    • Action of RuvAB at replication fork structures
    • McGlynn, P., and Lloyd, R. (2001) Action of RuvAB at replication fork structures. J. Biol. Chem. 276, 41938-41944
    • (2001) J. Biol. Chem. , vol.276 , pp. 41938-41944
    • McGlynn, P.1    Lloyd, R.2
  • 15
    • 1642524465 scopus 로고    scopus 로고
    • Situational repair of replication forks: Roles of RecG and RecA proteins
    • Robu, M. E., Inman, R. B., and Cox, M. M. (2004) Situational repair of replication forks: roles of RecG and RecA proteins. J. Biol. Chem. 279, 10973-10981
    • (2004) J. Biol. Chem. , vol.279 , pp. 10973-10981
    • Robu, M.E.1    Inman, R.B.2    Cox, M.M.3
  • 16
    • 0035902453 scopus 로고    scopus 로고
    • RecA protein promotes the regression of stalled replication forks in vitro
    • Robu, M. E., Inman, R. B., and Cox, M. M. (2001) RecA protein promotes the regression of stalled replication forks in vitro. Proc. Natl. Acad. Sci. U.S.A. 98, 8211-8218
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8211-8218
    • Robu, M.E.1    Inman, R.B.2    Cox, M.M.3
  • 17
    • 0034659679 scopus 로고    scopus 로고
    • Characterisation of the catalytically active form of RecG helicase
    • McGlynn, P., Mahdi, A. A., and Lloyd, R. G. (2000) Characterisation of the catalytically active form of RecG helicase. Nucleic Acids Res. 28, 2324-2332
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2324-2332
    • McGlynn, P.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 18
    • 0033178272 scopus 로고    scopus 로고
    • RecG helicase activity at three- and four-strand DNA structures
    • McGlynn, P., and Lloyd, R. (1999) RecG helicase activity at three- and four-strand DNA structures. Nucleic Acids Res. 27, 3049-3056
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3049-3056
    • McGlynn, P.1    Lloyd, R.2
  • 19
    • 0026482604 scopus 로고
    • Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration
    • Iwasaki, H., Takahagi, M., Nakata, A., and Shinagawa, H. (1992) Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration. Genes Dev. 6, 2214-2220
    • (1992) Genes Dev. , vol.6 , pp. 2214-2220
    • Iwasaki, H.1    Takahagi, M.2    Nakata, A.3    Shinagawa, H.4
  • 20
    • 0026741832 scopus 로고
    • Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
    • Parsons, C. A., Tsaneva, I., Lloyd, R. G., and West, S. C. (1992) Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions. Proc. Natl. Acad. Sci. U.S.A. 89, 5452-5456
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 5452-5456
    • Parsons, C.A.1    Tsaneva, I.2    Lloyd, R.G.3    West, S.C.4
  • 21
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. Coli
    • Tsaneva, I. R., Müller, B., and West, S. C. (1992) ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. Coli. Cell 69, 1171-1180
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 22
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • Tsaneva, I. R., Illing, G., Lloyd, R. G., and West, S. C. (1992) Purification and properties of the RuvA and RuvB proteins of Escherichia coli. Mol. Gen. Genet. 235, 1-10
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 1-10
    • Tsaneva, I.R.1    Illing, G.2    Lloyd, R.G.3    West, S.C.4
  • 23
    • 0028295131 scopus 로고
    • Processing of Holliday junctions by the Escherichia coli RuvA, RuvB, RuvC and RecG proteins
    • Müller, B., and West, S. C. (1994) Processing of Holliday junctions by the Escherichia coli RuvA, RuvB, RuvC and RecG proteins. Experientia 50, 216-222
    • (1994) Experientia , vol.50 , pp. 216-222
    • Müller, B.1    West, S.C.2
  • 24
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton, M. R., Scaife, S., and Wigley, D. B. (2001) Structural analysis of DNA replication fork reversal by RecG. Cell 107, 79-89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 25
    • 0032584598 scopus 로고    scopus 로고
    • Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli
    • Whitby, M. C., and Lloyd, R. G. (1998) Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. J. Biol. Chem. 273, 19729-19739
    • (1998) J. Biol. Chem. , vol.273 , pp. 19729-19739
    • Whitby, M.C.1    Lloyd, R.G.2
  • 26
    • 0036184234 scopus 로고    scopus 로고
    • Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities
    • Gregg, A. V., McGlynn, P., Jaktaji, R. P., and Lloyd, R. G. (2002) Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Mol. Cell 9, 241-251
    • (2002) Mol. Cell , vol.9 , pp. 241-251
    • Gregg, A.V.1    McGlynn, P.2    Jaktaji, R.P.3    Lloyd, R.G.4
  • 27
  • 28
    • 0025332556 scopus 로고
    • Molecular and functional analysis of the ruv region of Escherichia coli K-12 reveals three genes involved in DNA repair and recombination
    • Sharples, G. J., Benson, F. E., Illing, G. T., and Lloyd, R. G. (1990) Molecular and functional analysis of the ruv region of Escherichia coli K-12 reveals three genes involved in DNA repair and recombination. Mol. Gen. Genet. 221, 219-226
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 219-226
    • Sharples, G.J.1    Benson, F.E.2    Illing, G.T.3    Lloyd, R.G.4
  • 31
    • 0027236769 scopus 로고
    • Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. I. Comparison of RuvAB- and RuvB-mediated reactions
    • Müller, B., Tsaneva, I. R., and West, S. C. (1993) Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. I. Comparison of RuvAB- and RuvB-mediated reactions. J. Biol. Chem. 268, 17179-17184
    • (1993) J. Biol. Chem. , vol.268 , pp. 17179-17184
    • Müller, B.1    Tsaneva, I.R.2    West, S.C.3
  • 32
    • 0027184479 scopus 로고
    • Branch migration of holliday junctions promoted by the escherichia coli RuvA and RuvB proteins. II. Interaction of RuvB with DNA
    • Müller, B., Tsaneva, I. R., and West, S. C. (1993) Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. II. Interaction of RuvB with DNA. J. Biol. Chem. 268, 17185-17189
    • (1993) J. Biol. Chem. , vol.268 , pp. 17185-17189
    • Müller, B.1    Tsaneva, I.R.2    West, S.C.3
  • 33
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • Tsaneva, I. R., Müller, B., and West, S. C. (1993) RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc. Natl. Acad. Sci. U.S.A. 90, 1315-1319
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 34
    • 79959371375 scopus 로고    scopus 로고
    • Formation of a stable RuvA protein double tetramer is required for efficient branch migration in vitro and for replication fork reversal in vivo
    • Bradley, A. S., Baharoglu, Z., Niewiarowski, A., Michel, B., and Tsaneva, I. R. (2011) Formation of a stable RuvA protein double tetramer is required for efficient branch migration in vitro and for replication fork reversal in vivo. J. Biol. Chem. 286, 22372-22383
    • (2011) J. Biol. Chem. , vol.286 , pp. 22372-22383
    • Bradley, A.S.1    Baharoglu, Z.2    Niewiarowski, A.3    Michel, B.4    Tsaneva, I.R.5
  • 36
    • 0028050325 scopus 로고
    • Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase
    • Dunderdale, H. J., Sharples, G. J., Lloyd, R. G., and West, S. C. (1994) Cloning, overexpression, purification, and characterization of the Escherichia coli RuvC Holliday junction resolvase. J. Biol. Chem. 269, 5187-5194
    • (1994) J. Biol. Chem. , vol.269 , pp. 5187-5194
    • Dunderdale, H.J.1    Sharples, G.J.2    Lloyd, R.G.3    West, S.C.4
  • 37
    • 0029914126 scopus 로고    scopus 로고
    • Resolution of Holliday junctions in genetic recombination: RuvC protein nicks DNA at the point of strand exchange
    • Bennett, R. J., and West, S. C. (1996) Resolution of Holliday junctions in genetic recombination: RuvC protein nicks DNA at the point of strand exchange. Proc. Natl. Acad. Sci. U.S.A. 93, 12217-12222
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12217-12222
    • Bennett, R.J.1    West, S.C.2
  • 38
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the Ruv- ABC proteins
    • West, S. C. (1997) Processing of recombination intermediates by the Ruv- ABC proteins. Annu. Rev. Genet. 31, 213-244
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 39
    • 0032873606 scopus 로고    scopus 로고
    • Holliday junction processing in bacteria: Insights from the evolutionary conservation of RuvABC, RecG, and RusA
    • Sharples, G. J., Ingleston, S. M., and Lloyd, R. G. (1999) Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA. J. Bacteriol. 181, 5543-5550
    • (1999) J. Bacteriol. , vol.181 , pp. 5543-5550
    • Sharples, G.J.1    Ingleston, S.M.2    Lloyd, R.G.3
  • 40
    • 0035902573 scopus 로고    scopus 로고
    • Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled
    • McGlynn, P., Lloyd, R. G., and Marians, K. J. (2001) Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled. Proc. Natl. Acad. Sci. U.S.A. 98, 8235-8240
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8235-8240
    • McGlynn, P.1    Lloyd, R.G.2    Marians, K.J.3
  • 41
    • 0030727120 scopus 로고    scopus 로고
    • In vitro reconstitution of the late steps of genetic recombination in E. Coli
    • Eggleston, A. K., Mitchell, A. H., and West, S. C. (1997) In vitro reconstitution of the late steps of genetic recombination in E. Coli. Cell 89, 607-617
    • (1997) Cell , vol.89 , pp. 607-617
    • Eggleston, A.K.1    Mitchell, A.H.2    West, S.C.3
  • 43
    • 58749113648 scopus 로고    scopus 로고
    • RecG interacts directly with SSB: Implications for stalled replication fork regression
    • Buss, J. A., Kimura, Y., and Bianco, P. R. (2008) RecG interacts directly with SSB: implications for stalled replication fork regression. Nucleic Acids Res. 36, 7029-7042
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7029-7042
    • Buss, J.A.1    Kimura, Y.2    Bianco, P.R.3
  • 44
    • 76749101865 scopus 로고    scopus 로고
    • Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival
    • Gabbai, C. B., and Marians, K. J. (2010) Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival. DNA Repair 9, 202-209
    • (2010) DNA Repair , vol.9 , pp. 202-209
    • Gabbai, C.B.1    Marians, K.J.2
  • 45
    • 0037352498 scopus 로고    scopus 로고
    • PriA mediates DNA replication pathway choice at recombination intermediates
    • Xu, L., and Marians, K. J. (2003) PriA mediates DNA replication pathway choice at recombination intermediates. Mol. Cell 11, 817-826
    • (2003) Mol. Cell , vol.11 , pp. 817-826
    • Xu, L.1    Marians, K.J.2
  • 46
    • 0033988501 scopus 로고    scopus 로고
    • Role of PriA in replication fork reactivation in Escherichia coli
    • Sandler, S. J., and Marians, K. J. (2000) Role of PriA in replication fork reactivation in Escherichia coli. J. Bacteriol. 182, 9-13
    • (2000) J. Bacteriol. , vol.182 , pp. 9-13
    • Sandler, S.J.1    Marians, K.J.2
  • 47
    • 34249071349 scopus 로고    scopus 로고
    • Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA
    • Sasaki, K., Ose, T., Okamoto, N., Maenaka, K., Tanaka, T., Masai, H., Saito, M., Shirai, T., and Kohda, D. (2007) Structural basis of the 3′-end recognition of a leading strand in stalled replication forks by PriA. EMBO J. 26, 2584-2593
    • (2007) EMBO J , vol.26 , pp. 2584-2593
    • Sasaki, K.1    Ose, T.2    Okamoto, N.3    Maenaka, K.4    Tanaka, T.5    Masai, H.6    Saito, M.7    Shirai, T.8    Kohda, D.9
  • 48
    • 84884190957 scopus 로고    scopus 로고
    • RecG and UvsW catalyze efficient DNA rewinding reactions critical to stalledDNAreplication fork rescue
    • in press
    • Manosas, M., Perumal, S., Bianco, P. R., Benkovic, S. J., Ritort, F., and Croquette, V. (2013) RecG and UvsW catalyze efficient DNA rewinding reactions critical to stalledDNAreplication fork rescue. Nat. Commun., in press
    • (2013) Nat. Commun.
    • Manosas, M.1    Perumal, S.2    Bianco, P.R.3    Benkovic, S.J.4    Ritort, F.5    Croquette, V.6
  • 49
    • 33847306350 scopus 로고    scopus 로고
    • Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA
    • Slocum, S. L., Buss, J. A., Kimura, Y., and Bianco, P. R. (2007) Characterization of the ATPase activity of the Escherichia coli RecG protein reveals that the preferred cofactor is negatively supercoiled DNA. J. Mol. Biol. 367, 647-664
    • (2007) J. Mol. Biol. , vol.367 , pp. 647-664
    • Slocum, S.L.1    Buss, J.A.2    Kimura, Y.3    Bianco, P.R.4
  • 50
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 51
    • 84884176797 scopus 로고
    • Correction
    • Correction (1990) Anal. Biochem. 189, 283 51.
    • (1990) Anal. Biochem. , vol.189 , Issue.283 , pp. 51
  • 52
    • 0029779956 scopus 로고    scopus 로고
    • Allosteric effects of RuvA protein, ATP, and DNA on RuvB protein-mediated ATP hydrolysis
    • Marrione, P. E., and Cox, M. M. (1996) Allosteric effects of RuvA protein, ATP, and DNA on RuvB protein-mediated ATP hydrolysis. Biochemistry 35, 11228-11238
    • (1996) Biochemistry , vol.35 , pp. 11228-11238
    • Marrione, P.E.1    Cox, M.M.2
  • 53
    • 0029154926 scopus 로고
    • RuvB protein-mediated ATP hydrolysis: Functional asymmetry in the RuvB hexamer
    • Marrione, P. E., and Cox, M. M. (1995) RuvB protein-mediated ATP hydrolysis: functional asymmetry in the RuvB hexamer. Biochemistry 34, 9809-9818
    • (1995) Biochemistry , vol.34 , pp. 9809-9818
    • Marrione, P.E.1    Cox, M.M.2
  • 54
    • 0028067935 scopus 로고
    • RuvA and RuvB proteins facilitate the bypass of heterologousDNAinsertions during RecA protein-mediated DNA strand exchange
    • Iype, L. E., Wood, E. A., Inman, R. B., and Cox, M. M. (1994) RuvA and RuvB proteins facilitate the bypass of heterologousDNAinsertions during RecA protein-mediated DNA strand exchange. J. Biol. Chem. 269, 24967-24978
    • (1994) J. Biol. Chem. , vol.269 , pp. 24967-24978
    • Iype, L.E.1    Wood, E.A.2    Inman, R.B.3    Cox, M.M.4
  • 56
    • 0022493915 scopus 로고
    • Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under lambda PL control
    • Lohman, T. M., Green, J. M., and Beyer, R. S. (1986) Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under lambda PL control. Biochemistry 25, 21-25
    • (1986) Biochemistry , vol.25 , pp. 21-25
    • Lohman, T.M.1    Green, J.M.2    Beyer, R.S.3
  • 57
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • Lohman, T. M., and Overman, L. B. (1985) Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration. J. Biol. Chem. 260, 3594-3603
    • (1985) J. Biol. Chem. , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 58
    • 0004217575 scopus 로고
    • 2nd Ed., John Wiley and Sons, Hoboken, NJ
    • Segel, I. H. (1976) Biochemical Calculations, 2nd Ed., John Wiley and Sons, Hoboken, NJ
    • (1976) Biochemical Calculations
    • Segel, I.H.1
  • 59
    • 0029911566 scopus 로고    scopus 로고
    • The RuvABC proteins and Holliday junction processing in Escherichia coli
    • West, S. C. (1996) The RuvABC proteins and Holliday junction processing in Escherichia coli. J. Bacteriol. 178, 1237-1241
    • (1996) J. Bacteriol. , vol.178 , pp. 1237-1241
    • West, S.C.1
  • 60
    • 0033980541 scopus 로고    scopus 로고
    • RuvAB-mediated branch migration does not involve extensiveDNAopening within the RuvB hexamer
    • George, H., Kuraoka, I., Nauman, D. A., Kobertz, W. R., Wood, R. D., and West, S. C. (2000) RuvAB-mediated branch migration does not involve extensiveDNAopening within the RuvB hexamer. Curr. Biol. 10, 103-106
    • (2000) Curr. Biol. , vol.10 , pp. 103-106
    • George, H.1    Kuraoka, I.2    Nauman, D.A.3    Kobertz, W.R.4    Wood, R.D.5    West, S.C.6
  • 61
    • 33645636759 scopus 로고    scopus 로고
    • Stabilization of a stalled replication fork by concerted actions of two helicases
    • Tanaka, T., and Masai, H. (2006) Stabilization of a stalled replication fork by concerted actions of two helicases. J. Biol. Chem. 281, 3484-3493
    • (2006) J. Biol. Chem. , vol.281 , pp. 3484-3493
    • Tanaka, T.1    Masai, H.2
  • 62
    • 41949084372 scopus 로고    scopus 로고
    • RuvA Mutants that resolve Holliday junctions but do not reverse replication forks
    • Baharoglu, Z., Bradley, A. S., Le Masson, M., Tsaneva, I., and Michel, B. (2008) ruvA Mutants that resolve Holliday junctions but do not reverse replication forks. PLoS Genet. 4, e1000012
    • (2008) PLoS Genet. , vol.4
    • Baharoglu, Z.1    Bradley, A.S.2    Le Masson, M.3    Tsaneva, I.4    Michel, B.5
  • 63
    • 0029103324 scopus 로고
    • Characterisation of RuvAB-Holliday junction complexes by glycerol gradient sedimentation
    • Hiom, K., and West, S. (1995) Characterisation of RuvAB-Holliday junction complexes by glycerol gradient sedimentation. Nucleic Acids Res. 23, 3621-3626
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3621-3626
    • Hiom, K.1    West, S.2
  • 64
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB-Holliday junction complex
    • Yu, X., West, S. C., and Egelman, E. H. (1997) Structure and subunit composition of the RuvAB-Holliday junction complex. J. Mol. Biol. 266, 217-222
    • (1997) J. Mol. Biol. , vol.266 , pp. 217-222
    • Yu, X.1    West, S.C.2    Egelman, E.H.3
  • 65
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer, R. R., and Laine, P. S. (1990) The single-stranded DNA-binding protein of Escherichia coli. Microbiol. Rev. 54, 342-380
    • (1990) Microbiol. Rev. , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 66
    • 0028788048 scopus 로고
    • The E. Coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB
    • Parsons, C. A., Stasiak, A., and West, S. C. (1995) The E. Coli RuvAB proteins branch migrate Holliday junctions through heterologous DNA sequences in a reaction facilitated by SSB. EMBO J. 14, 5736-5744
    • (1995) EMBO J , vol.14 , pp. 5736-5744
    • Parsons, C.A.1    Stasiak, A.2    West, S.C.3
  • 68
    • 0020024650 scopus 로고
    • Damage to DNA induces expression of the ruv gene of Escherichia coli
    • Shurvinton, C. E., and Lloyd, R. G. (1982) Damage to DNA induces expression of the ruv gene of Escherichia coli. Mol. Gen. Genet. 185, 352-355
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 352-355
    • Shurvinton, C.E.1    Lloyd, R.G.2
  • 69
    • 0025790082 scopus 로고
    • Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12
    • Lloyd, R. G., and Sharples, G. J. (1991) Molecular organization and nucleotide sequence of the recG locus of Escherichia coli K-12. J. Bacteriol. 173, 6837-6843
    • (1991) J. Bacteriol. , vol.173 , pp. 6837-6843
    • Lloyd, R.G.1    Sharples, G.J.2
  • 70
    • 0033520395 scopus 로고    scopus 로고
    • Role of walker motif A of RuvB protein in promoting branch migration of Holliday junctions. Walker motif a mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB
    • Hishida, T., Iwasaki, H., Yagi, T., and Shinagawa, H. (1999) Role of walker motif A of RuvB protein in promoting branch migration of Holliday junctions. Walker motif a mutations affect ATP binding, ATP hydrolyzing, and DNA binding activities of RuvB. J. Biol. Chem. 274, 25335-25342
    • (1999) J. Biol. Chem. , vol.274 , pp. 25335-25342
    • Hishida, T.1    Iwasaki, H.2    Yagi, T.3    Shinagawa, H.4
  • 71
    • 32544441919 scopus 로고    scopus 로고
    • RuvAB is essential for replication forks reversal in certain replication mutants
    • Baharoglu, Z., Petranovic, M., Flores, M. J., and Michel, B. (2006) RuvAB is essential for replication forks reversal in certain replication mutants. EMBO J. 25, 596-604
    • (2006) EMBO J , vol.25 , pp. 596-604
    • Baharoglu, Z.1    Petranovic, M.2    Flores, M.J.3    Michel, B.4
  • 72
    • 0034737294 scopus 로고    scopus 로고
    • Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression
    • McGlynn, P., and Lloyd, R. (2000) Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression. Cell 101, 35-45
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.2
  • 73
    • 0035902591 scopus 로고    scopus 로고
    • Rescue of stalled replication forks by RecG: Simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation
    • McGlynn, P., and Lloyd, R. (2001) Rescue of stalled replication forks by RecG: simultaneous translocation on the leading and lagging strand templates supports an active DNA unwinding model of fork reversal and Holliday junction formation. Proc. Natl. Acad. Sci. U.S.A. 98, 8227-8234
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8227-8234
    • McGlynn, P.1    Lloyd, R.2
  • 74
    • 79851477029 scopus 로고    scopus 로고
    • Singlestranded DNA binding proteins unwind the newly synthesized doublestranded DNA of model miniforks
    • Delagoutte, E., Heneman-Masurel, A., and Baldacci, G. (2011) Singlestranded DNA binding proteins unwind the newly synthesized doublestranded DNA of model miniforks. Biochemistry 50, 932-944
    • (2011) Biochemistry , vol.50 , pp. 932-944
    • Delagoutte, E.1    Heneman-Masurel, A.2    Baldacci, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.