메뉴 건너뛰기




Volumn 525, Issue 7569, 2015, Pages 394-398

Replisome speed determines the efficiency of the Tus-Ter replication termination barrier

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; PROTEIN TUS; UNCLASSIFIED DRUG; DNA DIRECTED DNA POLYMERASE; DNA SYNTHESOME; ESCHERICHIA COLI PROTEIN; MULTIENZYME COMPLEX; TUS PROTEIN, E COLI;

EID: 84942047816     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature14866     Document Type: Article
Times cited : (41)

References (36)
  • 1
    • 68349133945 scopus 로고    scopus 로고
    • Random and site-specific replication termination
    • Dalgaard, J. Z. et al. Random and site-specific replication termination. Methods Mol. Biol. 521, 35-53 (2009).
    • (2009) Methods Mol. Biol. , vol.521 , pp. 35-53
    • Dalgaard, J.Z.1
  • 2
    • 0023126267 scopus 로고
    • The terminus region of the Escherichia coli chromosome contains two separate loci that exhibit polar inhibition of replication
    • Hill, T. M., Henson, J. M. & Kuempel, P. L. The terminus region of the Escherichia coli chromosome contains two separate loci that exhibit polar inhibition of replication. Proc. Natl Acad. Sci. USA 84, 1754-1758 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1754-1758
    • Hill, T.M.1    Henson, J.M.2    Kuempel, P.L.3
  • 3
    • 0030704679 scopus 로고    scopus 로고
    • Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli
    • Coskun-Ari, F. F. & Hill, T. M. Sequence-specific interactions in the Tus-Ter complex and the effect of base pair substitutions on arrest of DNA replication in Escherichia coli. J. Biol. Chem. 272, 26448-26456 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 26448-26456
    • Coskun-Ari, F.F.1    Hill, T.M.2
  • 4
    • 24944550999 scopus 로고    scopus 로고
    • Replication termination in Escherichia coli: Structure and antihelicase activity of the Tus-Ter complex
    • Neylon, C., Kralicek, A. V., Hill, T. M. & Dixon, N. E. Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex. Microbiol. Mol. Biol. Rev. 69, 501-526 (2005).
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 501-526
    • Neylon, C.1    Kralicek, A.V.2    Hill, T.M.3    Dixon, N.E.4
  • 5
    • 56749098227 scopus 로고    scopus 로고
    • The replication fork trap and termination of chromosome replication
    • Duggin, I. G., Wake, R. G., Bell, S. D. & Hill, T. M. The replication fork trap and termination of chromosome replication. Mol. Microbiol. 70, 1323-1333 (2008).
    • (2008) Mol. Microbiol. , vol.70 , pp. 1323-1333
    • Duggin, I.G.1    Wake, R.G.2    Bell, S.D.3    Hill, T.M.4
  • 6
    • 33745260902 scopus 로고    scopus 로고
    • A molecular mousetrap determines polarity of termination of DNA replication in E. coli
    • Mulcair, M. D. et al. A molecular mousetrap determines polarity of termination of DNA replication in E. coli. Cell 125, 1309-1319 (2006).
    • (2006) Cell , vol.125 , pp. 1309-1319
    • Mulcair, M.D.1
  • 7
    • 64149106045 scopus 로고    scopus 로고
    • Mechanisms of polar arrest of a replication fork
    • Kaplan, D. L. & Bastia, D. Mechanisms of polar arrest of a replication fork.Mol. Microbiol. 72, 279-285 (2009).
    • (2009) Mol. Microbiol. , vol.72 , pp. 279-285
    • Kaplan, D.L.1    Bastia, D.2
  • 8
    • 27444442749 scopus 로고    scopus 로고
    • Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling
    • Valjavec-Gratian, M., Henderson, T. A. & Hill, T. M. Tus-mediated arrest of DNA replication in Escherichia coli is modulated by DNA supercoiling. Mol. Microbiol. 58, 758-773 (2005).
    • (2005) Mol. Microbiol. , vol.58 , pp. 758-773
    • Valjavec-Gratian, M.1    Henderson, T.A.2    Hill, T.M.3
  • 9
    • 62049085766 scopus 로고    scopus 로고
    • Termination structures in the Escherichia coli chromosome replication fork trap
    • Duggin, I. G. & Bell, S. D. Termination structures in the Escherichia coli chromosome replication fork trap. J. Mol. Biol. 387, 532-539 (2009).
    • (2009) J. Mol. Biol. , vol.387 , pp. 532-539
    • Duggin, I.G.1    Bell, S.D.2
  • 10
    • 0028101938 scopus 로고
    • Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli
    • Coskun-Ari, F. F., Skokotas, A., Moe, G. R. & Hill, T. M. Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli. J. Biol. Chem. 269, 4027-4034 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 4027-4034
    • Coskun-Ari, F.F.1    Skokotas, A.2    Moe, G.R.3    Hill, T.M.4
  • 11
    • 0029908981 scopus 로고    scopus 로고
    • Structure of a replication-terminator protein complexed with DNA
    • Kamada, K., Horiuchi, T., Ohsumi, K., Shimamoto, N. & Morikawa, K. Structure of a replication-terminator protein complexed with DNA. Nature 383, 598-603 (1996).
    • (1996) Nature , vol.383 , pp. 598-603
    • Kamada, K.1    Horiuchi, T.2    Ohsumi, K.3    Shimamoto, N.4    Morikawa, K.5
  • 12
    • 31844453991 scopus 로고    scopus 로고
    • DNA primase acts as a molecular brake in DNA replication
    • Lee, J. B. et al. DNA primase acts as a molecular brake in DNA replication. Nature 439, 621-624 (2006).
    • (2006) Nature , vol.439 , pp. 621-624
    • Lee, J.B.1
  • 13
    • 38849174361 scopus 로고    scopus 로고
    • Single-molecule studies of fork dynamics in Escherichiacoli DNA replication
    • Tanner, N. A. et al. Single-molecule studies of fork dynamics in Escherichiacoli DNA replication. Nat. Struct. Mol. Biol. 15, 170-176 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 170-176
    • Tanner, N.A.1
  • 14
    • 84877631000 scopus 로고    scopus 로고
    • A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode
    • Jergic, S. et al. A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode. EMBO J. 32, 1322-1333 (2013).
    • (2013) EMBO J. , vol.32 , pp. 1322-1333
    • Jergic, S.1
  • 15
    • 62549122138 scopus 로고    scopus 로고
    • Real-time single-molecule observation of rolling-circle DNA replication
    • Tanner, N. A. et al. Real-time single-molecule observation of rolling-circle DNA replication. Nucleic Acids Res. 37, e27 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. e27
    • Tanner, N.A.1
  • 16
    • 58249114971 scopus 로고    scopus 로고
    • Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis
    • Hamdan, S. M., Loparo, J. J., Takahashi, M., Richardson, C. C. & van Oijen, A. M. Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis. Nature 457, 336-339 (2009).
    • (2009) Nature , vol.457 , pp. 336-339
    • Hamdan, S.M.1    Loparo, J.J.2    Takahashi, M.3    Richardson, C.C.4    Van Oijen, A.M.5
  • 17
    • 69449095740 scopus 로고    scopus 로고
    • Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression
    • Yao, N. Y., Georgescu, R. E., Finkelstein, J. & O'Donnell, M. E. Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression. Proc. Natl Acad. Sci. USA 106, 13236-13241 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 13236-13241
    • Yao, N.Y.1    Georgescu, R.E.2    Finkelstein, J.3    O'Donnell, M.E.4
  • 18
    • 84887111642 scopus 로고    scopus 로고
    • A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed
    • Pham, T. M. et al. A single-molecule approach to DNA replication in Escherichia coli cells demonstrated that DNA polymerase III is a major determinant of fork speed.Mol. Microbiol. 90, 584-596 (2013).
    • (2013) Mol. Microbiol. , vol.90 , pp. 584-596
    • Pham, T.M.1
  • 19
    • 84865725040 scopus 로고    scopus 로고
    • Differential Tus-Ter binding and lock formation: Implications for DNA replication termination in Escherichia coli
    • Moreau, M. J. & Schaeffer, P. M. Differential Tus-Ter binding and lock formation: implications for DNA replication termination in Escherichia coli. Mol. Biosyst. 8, 2783-2791 (2012).
    • (2012) Mol. Biosyst , vol.8 , pp. 2783-2791
    • Moreau, M.J.1    Schaeffer, P.M.2
  • 20
    • 0034601780 scopus 로고    scopus 로고
    • Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: A model derived from DNA-binding studies of mutant proteins by surface plasmon resonance
    • Neylon, C. et al. Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance. Biochemistry 39, 11989-11999 (2000).
    • (2000) Biochemistry , vol.39 , pp. 11989-11999
    • Neylon, C.1
  • 21
    • 51349146628 scopus 로고    scopus 로고
    • Replication termination mechanism as revealed by Tus-mediated polar arrest of a sliding helicase
    • Bastia, D. et al. Replication termination mechanism as revealed by Tus-mediated polar arrest of a sliding helicase. Proc. Natl Acad. Sci. USA 105, 12831-12836 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 12831-12836
    • Bastia, D.1
  • 22
    • 77958475756 scopus 로고    scopus 로고
    • DnaB helicase activity is modulated by DNA geometry and force
    • Ribeck, N., Kaplan, D. L., Bruck, I. & Saleh, O. A. DnaB helicase activity is modulated by DNA geometry and force. Biophys. J. 99, 2170-2179 (2010).
    • (2010) Biophys. J. , vol.99 , pp. 2170-2179
    • Ribeck, N.1    Kaplan, D.L.2    Bruck, I.3    Saleh, O.A.4
  • 23
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A t-DnaB interaction mediates rapid replication fork movement
    • Kim, S., Dallmann, H. G., McHenry, C. S. & Marians, K. J. Coupling of a replicative polymerase and helicase: a t-DnaB interaction mediates rapid replication fork movement. Cell 84, 643-650 (1996).
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 25
    • 0038455931 scopus 로고    scopus 로고
    • Flexibility revealed by the 1.85 Å crystal structure of the β sliding-clamp subunit of Escherichia coli DNA polymerase III
    • Oakley, A. J. et al. Flexibility revealed by the 1.85 Å crystal structure of the β sliding-clamp subunit of Escherichia coli DNA polymerase III. Acta Crystallogr. D 59, 1192-1199 (2003).
    • (2003) Acta Crystallogr. D , vol.59 , pp. 1192-1199
    • Oakley, A.J.1
  • 26
    • 0028868621 scopus 로고
    • φX174-type primosomal proteins: Purification and assay
    • Marians, K. J. φX174-type primosomal proteins: purification and assay. Methods Enzymol. 262, 507-521 (1995).
    • (1995) Methods Enzymol. , vol.262 , pp. 507-521
    • Marians, K.J.1
  • 27
    • 0036849859 scopus 로고    scopus 로고
    • Blu-Ice and the Distributed Control System: Software for data acquisition and instrument control at macromolecular crystallography beamlines
    • McPhillips, T. M. et al. Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines. J. Synchrotron Radiat. 9, 401-406 (2002).
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 401-406
    • McPhillips, T.M.1
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (1997).
    • (1997) J. Appl. Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 30
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255 (1997).
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 31
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N. & Murshudov, G. N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D 57, 122-133 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 34
    • 84942068460 scopus 로고    scopus 로고
    • Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex
    • Pandey, M. et al. Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex. Nucleic Acids Res. 43, 5924-5935 (2015).
    • (2015) Nucleic Acids Res. , vol.43 , pp. 5924-5935
    • Pandey, M.1
  • 35
    • 0041821716 scopus 로고    scopus 로고
    • Single-molecule kinetics of lambda exonuclease reveal base dependence and dynamic disorder
    • van Oijen, A. M. et al. Single-molecule kinetics of lambda exonuclease reveal base dependence and dynamic disorder. Science 301, 1235-1238 (2003).
    • (2003) Science , vol.301 , pp. 1235-1238
    • Van Oijen, A.M.1
  • 36
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • Bustamante, C., Marko, J. F., Siggia, E. D. & Smith, S. Entropic elasticity of lambda-phage DNA. Science 265, 1599-1600 (1994).
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.