메뉴 건너뛰기




Volumn 585, Issue 1, 2011, Pages 7-17

Helicobacter pylori chromosomal DNA replication: Current status and future perspectives

Author keywords

Elongation; Helicobacter pylori; Recombinational repair; Replication initiation; Replication restart; Termination

Indexed keywords

DNA; DNAC HELICASE; HELICASE; REPLICATION INITIATOR PROTEIN DNAA; REPLISOME; UNCLASSIFIED DRUG;

EID: 78650871483     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.11.018     Document Type: Review
Times cited : (21)

References (136)
  • 1
    • 14544285951 scopus 로고    scopus 로고
    • Helicobacter pylori infection, glandular atrophy and intestinal metaplasia in superficial gastritis, gastric erosion, erosive gastritis, gastric ulcer and early gastric cancer
    • C. Zhang, N. Yamada, Y.L. Wu, M. Wen, T. Matsuhisa, and N. Matsukura Helicobacter pylori infection, glandular atrophy and intestinal metaplasia in superficial gastritis, gastric erosion, erosive gastritis, gastric ulcer and early gastric cancer World J. Gastroenterol. 11 6 2005 791 796
    • (2005) World J. Gastroenterol. , vol.11 , Issue.6 , pp. 791-796
    • Zhang, C.1    Yamada, N.2    Wu, Y.L.3    Wen, M.4    Matsuhisa, T.5    Matsukura, N.6
  • 2
    • 0036370334 scopus 로고    scopus 로고
    • Helicobacter pylori and gastrointestinal tract adenocarcinomas
    • R.M. Peek, and M.J. Blaser Helicobacter pylori and gastrointestinal tract adenocarcinomas Nat. Rev. Cancer 2 29 2002 28 37
    • (2002) Nat. Rev. Cancer , vol.2 , Issue.29 , pp. 28-37
    • Peek, R.M.1    Blaser, M.J.2
  • 3
    • 33645740999 scopus 로고    scopus 로고
    • The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases
    • J.C. Atherton The pathogenesis of Helicobacter pylori-induced gastro-duodenal diseases Annu. Rev. Pathol. 1 2006 63 96
    • (2006) Annu. Rev. Pathol. , vol.1 , pp. 63-96
    • Atherton, J.C.1
  • 8
    • 34248370213 scopus 로고    scopus 로고
    • Spiral structure of Escherichia coli HU alpha beta provides foundation for DNA supercoiling
    • F. Guo, and S. Adhya Spiral structure of Escherichia coli HU alpha beta provides foundation for DNA supercoiling Proc. Natl. Acad. Sci. USA 104 2007 4309 4314
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4309-4314
    • Guo, F.1    Adhya, S.2
  • 9
    • 0036035581 scopus 로고    scopus 로고
    • IHF and HU stimulate assembly of pre-replication complexes at Escherichia coli oriC by two different mechanisms
    • V.T. Ryan, J.E. Grimwade, C.J. Nievera, and A.C. Leonard IHF and HU stimulate assembly of pre-replication complexes at Escherichia coli oriC by two different mechanisms Mol. Microbiol. 46 1 2002 113 124
    • (2002) Mol. Microbiol. , vol.46 , Issue.1 , pp. 113-124
    • Ryan, V.T.1    Grimwade, J.E.2    Nievera, C.J.3    Leonard, A.C.4
  • 10
    • 18344385508 scopus 로고    scopus 로고
    • Protein-protein interactions in the eubacterial replisome
    • P.M. Schaeffer, M.J. Headlam, and N.E. Dixon Protein-protein interactions in the eubacterial replisome IUBMB Life 57 1 2005 5 12
    • (2005) IUBMB Life , vol.57 , Issue.1 , pp. 5-12
    • Schaeffer, P.M.1    Headlam, M.J.2    Dixon, N.E.3
  • 11
    • 34548348945 scopus 로고    scopus 로고
    • MukB colocalizes with the oriC region and is required for organization of the two Escherichia coli chromosome arms into separate cell halves
    • O. Danilova, R. Reyes-Lamothe, M. Pinskaya, D. Sherrat, and C. Possoz MukB colocalizes with the oriC region and is required for organization of the two Escherichia coli chromosome arms into separate cell halves Mol. Microbiol. 65 2007 1485 1492
    • (2007) Mol. Microbiol. , vol.65 , pp. 1485-1492
    • Danilova, O.1    Reyes-Lamothe, R.2    Pinskaya, M.3    Sherrat, D.4    Possoz, C.5
  • 12
    • 0015506453 scopus 로고
    • Origin and sequence of chromosome replication in Escherichia coli
    • R.E. Bird, J. Louarn, J. Martuscelli, and L. Caro Origin and sequence of chromosome replication in Escherichia coli J. Mol. Biol. 70 1972 549 566
    • (1972) J. Mol. Biol. , vol.70 , pp. 549-566
    • Bird, R.E.1    Louarn, J.2    Martuscelli, J.3    Caro, L.4
  • 13
    • 0016176519 scopus 로고
    • More precise mapping of the replication origin in Escherichia coli K-12
    • J. Louarn, M. Funderburgh, and R.E. Bird More precise mapping of the replication origin in Escherichia coli K-12 J. Bacteriol. 120 1 1974 1 5
    • (1974) J. Bacteriol. , vol.120 , Issue.1 , pp. 1-5
    • Louarn, J.1    Funderburgh, M.2    Bird, R.E.3
  • 14
    • 0017711419 scopus 로고
    • A DNA fragment containing the origin of replication of the Escherichia coli chromosome
    • R.C. Marsh, and A. Worcel A DNA fragment containing the origin of replication of the Escherichia coli chromosome Proc. Natl. Acad. Sci. USA 74 7 1977 2720 2724
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , Issue.7 , pp. 2720-2724
    • Marsh, R.C.1    Worcel, A.2
  • 16
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • A. Johnson, and M. O'Donnell Cellular DNA replicases: components and dynamics at the replication fork Annu. Rev. Biochem. 74 2005 283 315
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 17
    • 34047149973 scopus 로고    scopus 로고
    • Replisome mechanics: Insights into a twin DNA polymerase machine
    • R.T. Pomerantz, and M. O'Donnell Replisome mechanics: insights into a twin DNA polymerase machine Trends Microbiol. 15 4 2007 156 164
    • (2007) Trends Microbiol. , vol.15 , Issue.4 , pp. 156-164
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 19
    • 77953710831 scopus 로고    scopus 로고
    • SnapShot: The replisome
    • N.Y. Yao, and M. O'Donnell SnapShot: the replisome Cell 141 6 2010 1088.e1
    • (2010) Cell , vol.141 , Issue.6
    • Yao, N.Y.1    O'Donnell, M.2
  • 21
    • 0019492805 scopus 로고
    • Growth rate-dependent control of chromosome replication initiation in Escherichia coli
    • G. Churchward, E. Estiva, and H. Bremer Growth rate-dependent control of chromosome replication initiation in Escherichia coli J. Bacteriol. 145 1981 1232 1238 (Pubitemid 11097339)
    • (1981) Journal of Bacteriology , vol.145 , Issue.3 , pp. 1232-1238
    • Churchward, G.1    Estiva, E.2    Bremer, H.3
  • 24
    • 0025876510 scopus 로고
    • The Escherichia coli cell cycle: One cycle or multiple independent processes that are co-ordinated?
    • K. Nordström, R. Bernander, and S. Dasgupta The Escherichia coli cell cycle: one cycle or multiple independent processes that are co-ordinated? Mol. Microbiol. 5 4 1991 769 774
    • (1991) Mol. Microbiol. , vol.5 , Issue.4 , pp. 769-774
    • Nordström, K.1    Bernander, R.2    Dasgupta, S.3
  • 25
    • 42049099692 scopus 로고    scopus 로고
    • The great divide: Coordinating cell cycle events during bacterial growth and division
    • D.P. Haeusser, and P.A. Levin The great divide: coordinating cell cycle events during bacterial growth and division Curr. Opin. Microbiol. 2 2008 94 99
    • (2008) Curr. Opin. Microbiol. , Issue.2 , pp. 94-99
    • Haeusser, D.P.1    Levin, P.A.2
  • 26
    • 77957262782 scopus 로고    scopus 로고
    • Synchronization of chromosome dynamics and cell division in bacteria
    • M. Thanbichler Synchronization of chromosome dynamics and cell division in bacteria Cold Spring Harb. Perspect. Biol. 2 2009 a000331
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.2 , pp. 000331
    • Thanbichler, M.1
  • 27
    • 77955039647 scopus 로고    scopus 로고
    • Cell division intersects with cell geometry
    • J.B. Moseley, and P. Nurse Cell division intersects with cell geometry Cell 142 2 2010 189 193
    • (2010) Cell , vol.142 , Issue.2 , pp. 189-193
    • Moseley, J.B.1    Nurse, P.2
  • 28
    • 0018355620 scopus 로고
    • Origin of replication, oriC, of the Escherichia coli K12 chromosome: Nucleotide sequence
    • W. Messer, M. Meijer, H.E.N. Bergmans, F.G. Hansen, K.V. Meyenburg, E. Beck, and H. Schaller Origin of replication, oriC, of the Escherichia coli K-12 chromosome: Nucleotide sequence Cold Spring Harb. Symp. Quant. Biol. 43 1979 139 145 (Pubitemid 9230262)
    • (1979) Cold Spring Harbor Symposia on Quantitative Biology , vol.43 , Issue.1 , pp. 139-145
    • Messer, W.1    Meijer, M.2    Bergmans, H.E.N.3
  • 29
    • 0023766613 scopus 로고
    • A model for initiation at origins of DNA replication
    • D. Bramhill, and A. Kornberg A model for initiation at origins of DNA replication Cell 54 1988 915 918
    • (1988) Cell , vol.54 , pp. 915-918
    • Bramhill, D.1    Kornberg, A.2
  • 30
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • J. Marszalek, and J.M. Kaguni DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli J. Biol. Chem. 269 7 1994 4883 4890
    • (1994) J. Biol. Chem. , vol.269 , Issue.7 , pp. 4883-4890
    • Marszalek, J.1    Kaguni, J.M.2
  • 31
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • H. Seitz, C. Weigel, and W. Messer The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli Mol. Microbiol. 37 5 2000 1270 1279
    • (2000) Mol. Microbiol. , vol.37 , Issue.5 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 32
    • 0037222240 scopus 로고    scopus 로고
    • Strategies for helicase recruitment and loading in bacteria
    • I. Konieczny Strategies for helicase recruitment and loading in bacteria EMBO Rep. 4 2003 37 41
    • (2003) EMBO Rep. , vol.4 , pp. 37-41
    • Konieczny, I.1
  • 33
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA and oriC, the bacterial mode to initiate DNA replication
    • W. Messer The bacterial replication initiator DnaA and oriC, the bacterial mode to initiate DNA replication FEMS Microbiol. Rev. 26 2002 355 374
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 355-374
    • Messer, W.1
  • 34
    • 29744452137 scopus 로고    scopus 로고
    • Regulatory network of the initiation of chromosomal replication in Escherichia coli
    • J. Kato Regulatory network of the initiation of chromosomal replication in Escherichia coli Crit. Rev. Biochem. Mol. Biol. 40 2005 331 342
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 331-342
    • Kato, J.1
  • 35
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: Controlling the initiation of bacterial DNA replication and more
    • J.M. Kaguni DnaA: controlling the initiation of bacterial DNA replication and more Annu. Rev. Microbiol. 60 2006 351 375
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 351-375
    • Kaguni, J.M.1
  • 36
    • 0022977660 scopus 로고
    • The Escherichia coli DnaB protein is a DNA helicase
    • J.H. Lebowitz, and R. McMacken The Escherichia coli DnaB protein is a DNA helicase J. Biol. Chem. 261 1986 4738 4748
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 37
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes molecular
    • D.L. Kaplan, and M. O'Donnell Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes molecular Cell 15 2004 453 465
    • (2004) Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 38
    • 0029803922 scopus 로고    scopus 로고
    • Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA
    • Y.B. Lu, V. Pillarisetty, A.L. Ratnakar, B.K. Mohanty, and D. Bastia Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA Proc. Natl. Acad. Sci. USA 93 1996 12902 12907
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12902-12907
    • Lu, Y.B.1    Pillarisetty, V.2    Ratnakar, A.L.3    Mohanty, B.K.4    Bastia, D.5
  • 40
    • 0033213720 scopus 로고    scopus 로고
    • Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin
    • L.H. Fang, M.J. Davey, and M. O'Donnell Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin Mol. Cell 4 1999 541 553
    • (1999) Mol. Cell , vol.4 , pp. 541-553
    • Fang, L.H.1    Davey, M.J.2    O'Donnell, M.3
  • 41
    • 0742269690 scopus 로고    scopus 로고
    • Identification of two origins of replication in the single chromosome of the archaeon Sulfolobus solfataricus
    • N.P. Robinson, I. Dionne, M. Lundgren, V.L. Marsh, R. Bernarder, and S.D. Bell Identification of two origins of replication in the single chromosome of the archaeon Sulfolobus solfataricus Cell 116 2004 25 38
    • (2004) Cell , vol.116 , pp. 25-38
    • Robinson, N.P.1    Dionne, I.2    Lundgren, M.3    Marsh, V.L.4    Bernarder, R.5    Bell, S.D.6
  • 42
    • 0035997368 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic cells
    • S.P. Bell, and A. Dutta Initiation of DNA replication in eukaryotic cells Annu. Rev. Biochem. 71 2002 333 374
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 47
    • 34250632433 scopus 로고    scopus 로고
    • The domain structure of Helicobacter pylori DnaB helicase: The N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function
    • R.G. Nitharwal, S. Paul, A. Dar, N.R. Choudhury, S. Sinha, T. Kashav, G. Mukhopadhyay, T.K. Chaudhuri, S. Gourinath, and S.K. Dhar The domain structure of Helicobacter pylori DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function Nucl. Acids Res. 35 2007 2861 2874
    • (2007) Nucl. Acids Res. , vol.35 , pp. 2861-2874
    • Nitharwal, R.G.1    Paul, S.2    Dar, A.3    Choudhury, N.R.4    Sinha, S.5    Kashav, T.6    Mukhopadhyay, G.7    Chaudhuri, T.K.8    Gourinath, S.9    Dhar, S.K.10
  • 48
    • 22544460494 scopus 로고    scopus 로고
    • Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo
    • R.K. Soni, P. Mehra, G. Mukhopadhyay, and S.K. Dhar Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo Biochem. J. 389 2005 541 548
    • (2005) Biochem. J. , vol.389 , pp. 541-548
    • Soni, R.K.1    Mehra, P.2    Mukhopadhyay, G.3    Dhar, S.K.4
  • 50
    • 70449570532 scopus 로고    scopus 로고
    • Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori
    • T. Kashav, R. Nitharwal, S.A. Abdulrehman, A. Gabdoulkhakov, W. Saenger, S.K. Dhar, and S. Gourinath Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori PLoS ONE 4 10 2009 e7515
    • (2009) PLoS ONE , vol.4 , Issue.10 , pp. 7515
    • Kashav, T.1    Nitharwal, R.2    Abdulrehman, S.A.3    Gabdoulkhakov, A.4    Saenger, W.5    Dhar, S.K.6    Gourinath, S.7
  • 51
    • 0347993077 scopus 로고    scopus 로고
    • Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis
    • A.V. Mitkova, S.M. Khopde, and S.B. Biswas Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis J. Biol. Chem. 278 2003 52253 52261
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 52
    • 0029832926 scopus 로고    scopus 로고
    • The extreme C terminus of primase is required for interaction with DnaB at the replication fork
    • DOI 10.1074/jbc.271.35.21391
    • K. Tougu, and K.J. Marians The extreme C terminus of primase is required for interaction with DnaB at the replication fork J. Biol. Chem. 271 35 1996 21391 21397 (Pubitemid 26293002)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.35 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 53
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: Studies of subunit arrangement and functional consequences
    • C.S. McHenry Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences Mol. Microbiol. 49 2003 1157 1165
    • (2003) Mol. Microbiol. , vol.49 , pp. 1157-1165
    • McHenry, C.S.1
  • 54
    • 0032483511 scopus 로고    scopus 로고
    • The χψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template
    • B.P. Glover, and C.S. McHenry The χψ subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template J. Biol. Chem. 273 1998 23476 23484
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 55
    • 0027298689 scopus 로고
    • DNA polymerase III accessory proteins. II. Characterization of δ and δ'
    • R. Onrust, and M. O'Donnell DNA polymerase III accessory proteins. II. Characterization of δ and δ′ J. Biol. Chem. 268 1993 11766 11772 (Pubitemid 23168128)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.16 , pp. 11766-11772
    • Onrust, R.1    O'Donnell, M.2
  • 56
    • 0036091247 scopus 로고    scopus 로고
    • Primosome assembly requirement for replication restart in the Escherichia coli holDQ10 replication mutant
    • M.J. Flores, S.D. Ehrlich, and B. Michel Primosome assembly requirement for replication restart in the Escherichia coli holDQ10 replication mutant Mol. Microbiol. 44 2002 783 792
    • (2002) Mol. Microbiol. , vol.44 , pp. 783-792
    • Flores, M.J.1    Ehrlich, S.D.2    Michel, B.3
  • 57
    • 77951537332 scopus 로고    scopus 로고
    • Stoichiometry and architecture of active DNA replication machinery in Escherichia coli
    • R. Reyes-Lamothe, D.J. Sherratt, and M.C. Leake Stoichiometry and architecture of active DNA replication machinery in Escherichia coli Science 328 2010 498 501
    • (2010) Science , vol.328 , pp. 498-501
    • Reyes-Lamothe, R.1    Sherratt, D.J.2    Leake, M.C.3
  • 58
    • 0019223518 scopus 로고
    • Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system
    • N.K. Sinha, C.F. Morris, and B.M. Alberts Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system J. Biol. Chem. 255 9 1980 4290 4293
    • (1980) J. Biol. Chem. , vol.255 , Issue.9 , pp. 4290-4293
    • Sinha, N.K.1    Morris, C.F.2    Alberts, B.M.3
  • 59
    • 0029788209 scopus 로고    scopus 로고
    • The interaction between helicase and primase sets the replication fork clock
    • DOI 10.1074/jbc.271.35.21398
    • K. Tougu, and K.J. Marians The interaction between helicase and primase sets the replication fork clock J. Biol. Chem. 271 35 1996 21398 21405 (Pubitemid 26293003)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.35 , pp. 21398-21405
    • Tougu, K.1    Marians, K.J.2
  • 61
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • R.C. Heller, and K.J. Marians Replication fork reactivation downstream of a blocked nascent leading strand Nature 439 2006 557 562
    • (2006) Nature , vol.439 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 62
    • 33747332833 scopus 로고    scopus 로고
    • The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision
    • L. Amado, and A. Kuzminov The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision J. Biol. Chem. 281 32 2006 22635 22646
    • (2006) J. Biol. Chem. , vol.281 , Issue.32 , pp. 22635-22646
    • Amado, L.1    Kuzminov, A.2
  • 63
    • 58149175920 scopus 로고    scopus 로고
    • Helicobacter pylori single-stranded DNA binding protein-functional characterization and modulation of H. pylori DnaB helicase activity
    • A. Sharma, R.G. Nitharwal, A. Dar, S. Dasgupta, and S.K. Dhar Helicobacter pylori single-stranded DNA binding protein-functional characterization and modulation of H. pylori DnaB helicase activity FEBS J. 276 2009 519 531
    • (2009) FEBS J. , vol.276 , pp. 519-531
    • Sharma, A.1    Nitharwal, R.G.2    Dar, A.3    Dasgupta, S.4    Dhar, S.K.5
  • 64
    • 3142695077 scopus 로고    scopus 로고
    • Untangling intracellular DNA topology
    • O. Espeli, and K.J. Marians Untangling intracellular DNA topology Mol. Microbiol. 52 4 2004 925 931
    • (2004) Mol. Microbiol. , vol.52 , Issue.4 , pp. 925-931
    • Espeli, O.1    Marians, K.J.2
  • 66
    • 0024785354 scopus 로고
    • Purification of a DNA replication terminus (ter) site-binding protein in Escherichia coli and identification of the structural gene
    • M. Hidakas, T. Kobayashis, S. Takenakab, and H. Takeyaq Purification of a DNA replication terminus (ter) site-binding protein in Escherichia coli and identification of the structural gene Biochemistry 264 35 1989 21031 21037
    • (1989) Biochemistry , vol.264 , Issue.35 , pp. 21031-21037
    • Hidakas, M.1    Kobayashis, T.2    Takenakab, S.3    Takeyaq, H.4
  • 67
    • 0028101938 scopus 로고
    • Biophysical characteristics of Tus, the replication arrest protein of Escherichia coli
    • F.F. Coskun-Ari, A. Skokotas, G.R. Moe, and T.M. Hill Biophysical characterization of Tus, the replication arrest protein of Escherechia coli J. Biol. Chem. 269 1994 4027 4034 (Pubitemid 24237750)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.6 , pp. 4027-4034
    • Coskun-Ari, F.F.1    Skokotas, A.2    Moe, G.R.3    Hill, T.M.4
  • 68
    • 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
    • F.F. Coskun-Ari, and T.M. Hill 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 1997 26448 26456
    • (1997) J. Biol. Chem. , vol.272 , pp. 26448-26456
    • Coskun-Ari, F.F.1    Hill, T.M.2
  • 69
    • 0023126267 scopus 로고
    • The terminus region of the Escherichia coli chromosome contains two separate loci that exhibit polar inhibition of replication
    • T.M. Hill, J.M. Henson, and P.L. Kuempel The terminus region of the Escherichia coli chromosome contains two separate loci that exhibit polar inhibition of replication Proc. Natl. Acad. Sci. USA 84 1987 1754 1758
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1754-1758
    • Hill, T.M.1    Henson, J.M.2    Kuempel, P.L.3
  • 70
    • 0026794488 scopus 로고
    • Arrest of bacterial DNA replication
    • T.M. Hill Arrest of bacterial DNA replication Annu. Rev. Microbiol. 46 1992 603 633
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 603-633
    • Hill, T.M.1
  • 71
    • 0031756520 scopus 로고    scopus 로고
    • Sister chromatid exchange frequencies in Escherichia coli analyzed by recombination at the dif resolvase site
    • W.W. Steiner, and P.L. Kuempel Sister chromatid exchange frequencies in Escherichia coli analyzed by recombination at the dif resolvase site J. Bacteriol. 180 1998 6269 6275
    • (1998) J. Bacteriol. , vol.180 , pp. 6269-6275
    • Steiner, W.W.1    Kuempel, P.L.2
  • 72
    • 0034115179 scopus 로고    scopus 로고
    • Functional polarization of the Escherichia coli chromosome terminus: The dif site acts in chromosome dimer resolution only when located between long stretches of opposite polarity
    • K. Perals, F. Cornet, Y. Merlet, I. Delon, and J.M. Louarn Functional polarization of the Escherichia coli chromosome terminus: the dif site acts in chromosome dimer resolution only when located between long stretches of opposite polarity Mol. Microbiol. 36 2000 33 43
    • (2000) Mol. Microbiol. , vol.36 , pp. 33-43
    • Perals, K.1    Cornet, F.2    Merlet, Y.3    Delon, I.4    Louarn, J.M.5
  • 75
    • 0026712869 scopus 로고
    • The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication
    • D.E. Adams, E.M. Shekhtman, E.L. Zechiedrich, M.B. Schmid, and N.R. Cozzarelli The role of topoisomerase IV in partitioning bacterial replicons and the structure of catenated intermediates in DNA replication Cell 71 1992 277 288
    • (1992) Cell , vol.71 , pp. 277-288
    • Adams, D.E.1    Shekhtman, E.M.2    Zechiedrich, E.L.3    Schmid, M.B.4    Cozzarelli, N.R.5
  • 76
    • 0027171678 scopus 로고
    • Decatenation activity of topoisomerase IV during oriC and pBR322 DNA replication in vitro
    • H. Peng, and K.J. Marians Decatenation activity of topoisomerase IV during oriC and pBR322 DNA replication in vitro Proc. Natl. Acad. Sci. USA 90 1993 8571 8575
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8571-8575
    • Peng, H.1    Marians, K.J.2
  • 77
    • 3242699635 scopus 로고    scopus 로고
    • Fast, DNA-sequence independent translocation by FtsK in a single-molecule experiment
    • O.A. Saleh, C. Perals, F.X. Barre, and J.F. Allemand Fast, DNA-sequence independent translocation by FtsK in a single-molecule experiment EMBO J. 23 2004 2430 2439
    • (2004) EMBO J. , vol.23 , pp. 2430-2439
    • Saleh, O.A.1    Perals, C.2    Barre, F.X.3    Allemand, J.F.4
  • 79
    • 33645462819 scopus 로고    scopus 로고
    • Dissection of a functional interaction between the DNA translocase, FtsK and the XerD recombinase
    • J. Yates, I. Zhekov, R. Baker, B. Eklund, D.J. Sherratt, and L.K. Arciszewska Dissection of a functional interaction between the DNA translocase, FtsK and the XerD recombinase Mol. Microbiol. 59 2006 1754 1766
    • (2006) Mol. Microbiol. , vol.59 , pp. 1754-1766
    • Yates, J.1    Zhekov, I.2    Baker, R.3    Eklund, B.4    Sherratt, D.J.5    Arciszewska, L.K.6
  • 81
    • 0036051167 scopus 로고    scopus 로고
    • The ParB protein of Streptomyces coelicolor A3(2) recognizes a cluster of parS sequences within the origin-proximal region of the linear chromosome
    • D. Jakimowicz, K. Chater, and J. Zakrzewska-Czerwinska The ParB protein of Streptomyces coelicolor A3(2) recognizes a cluster of parS sequences within the origin-proximal region of the linear chromosome Mol. Microbiol. 45 2007 1365 1377
    • (2007) Mol. Microbiol. , vol.45 , pp. 1365-1377
    • Jakimowicz, D.1    Chater, K.2    Zakrzewska-Czerwinska, J.3
  • 82
    • 0032489548 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial chromosome partitioning site
    • D.C.H. Lin, and A.D. Grossman Identification and characterization of a bacterial chromosome partitioning site Cell 92 1998 675 685
    • (1998) Cell , vol.92 , pp. 675-685
    • Lin, D.C.H.1    Grossman, A.D.2
  • 83
    • 33644625943 scopus 로고    scopus 로고
    • Characterization of the Soj/Spo0J chromosome segregation proteins and identification of putative parS sequences in Helicobacter pylori
    • M. Lee, C. Liu, S. Wang, C. Huang, and H. Huang Characterization of the Soj/Spo0J chromosome segregation proteins and identification of putative parS sequences in Helicobacter pylori Biochem. Biophys. Res. Commun. 342 2006 744 750
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 744-750
    • Lee, M.1    Liu, C.2    Wang, S.3    Huang, C.4    Huang, H.5
  • 84
    • 0028219947 scopus 로고
    • SeqA: A negative modulator of replication initiation in E. coli
    • M. Lu, J.L. Campbell, E. Boye, and N. Kleckner SeqA: a negative modulator of replication initiation in E. coli Cell 77 1994 413 426
    • (1994) Cell , vol.77 , pp. 413-426
    • Lu, M.1    Campbell, J.L.2    Boye, E.3    Kleckner, N.4
  • 85
    • 0025071856 scopus 로고
    • E. coli oriC and the dnaA gene promoter are sequestered from dam methyltransferase following the passage of the chromosomal replication fork
    • J.L. Campbell, and N. Kleckner E. coli oriC and the dnaA gene promoter are sequestered from dam methyltransferase following the passage of the chromosomal replication fork Cell 62 5 1990 967 979
    • (1990) Cell , vol.62 , Issue.5 , pp. 967-979
    • Campbell, J.L.1    Kleckner, N.2
  • 86
    • 33750987654 scopus 로고    scopus 로고
    • SeqA blocking of DnaA-oriC interactions ensures staged assembly of the E. coli pre-RC
    • C. Nievera, J.J. Torgue, J.E. Grimwade, and A.C. Leonard SeqA blocking of DnaA-oriC interactions ensures staged assembly of the E. coli pre-RC Mol. Cell 24 2006 581 592
    • (2006) Mol. Cell , vol.24 , pp. 581-592
    • Nievera, C.1    Torgue, J.J.2    Grimwade, J.E.3    Leonard, A.C.4
  • 87
    • 0030003443 scopus 로고    scopus 로고
    • A novel DnaA protein-binding site at 94.7 min on the Escherichia coli chromosome
    • R. Kitagawa, H. Mitsuki, T. Okazaki, and T. Ogawa A novel DnaA protein-binding site at 94.7 min on the Escherichia coli chromosome Mol. Microbiol. 19 1996 1137 1147
    • (1996) Mol. Microbiol. , vol.19 , pp. 1137-1147
    • Kitagawa, R.1    Mitsuki, H.2    Okazaki, T.3    Ogawa, T.4
  • 88
    • 0032190630 scopus 로고    scopus 로고
    • Negative control of replication initiation by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein
    • R. Kitagawa, T. Ozaki, S. Moriya, and T. Ogawa Negative control of replication initiation by a novel chromosomal locus exhibiting exceptional affinity for Escherichia coli DnaA protein Genes Dev. 12 1998 3032 3043
    • (1998) Genes Dev. , vol.12 , pp. 3032-3043
    • Kitagawa, R.1    Ozaki, T.2    Moriya, S.3    Ogawa, T.4
  • 89
    • 61349133630 scopus 로고    scopus 로고
    • Initiator titration complex formed at datA with the aid of IHF regulates replication timing in Escherichia coli
    • S. Nozaki, Y. Yamada, and T. Ogawa Initiator titration complex formed at datA with the aid of IHF regulates replication timing in Escherichia coli Genes Cells 14 2009 329 341
    • (2009) Genes Cells , vol.14 , pp. 329-341
    • Nozaki, S.1    Yamada, Y.2    Ogawa, T.3
  • 90
    • 0037628613 scopus 로고    scopus 로고
    • Controlled initiation of chromosomal replication in Escherichia coli requires functional Hda protein
    • J.E. Camara, K. Skarstad, and E. Crooke Controlled initiation of chromosomal replication in Escherichia coli requires functional Hda protein J. Bacteriol. 185 2003 3244 3248
    • (2003) J. Bacteriol. , vol.185 , pp. 3244-3248
    • Camara, J.E.1    Skarstad, K.2    Crooke, E.3
  • 91
    • 0032504050 scopus 로고    scopus 로고
    • The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase
    • T. Katayama, T. Kubota, K. Kurokawa, E. Crooke, and K. Sekimizu The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase Cell 94 1 1998 61 71
    • (1998) Cell , vol.94 , Issue.1 , pp. 61-71
    • Katayama, T.1    Kubota, T.2    Kurokawa, K.3    Crooke, E.4    Sekimizu, K.5
  • 92
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • J. Kato, and T. Katayama Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli EMBO J. 15 2001 4253 4262
    • (2001) EMBO J. , vol.15 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 93
    • 33644861714 scopus 로고    scopus 로고
    • A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli
    • S. Gon, J.E. Camara, H.K. Klungsøyr, E. Crooke, K. Skarstad, and B.J. Jon A novel regulatory mechanism couples deoxyribonucleotide synthesis and DNA replication in Escherichia coli EMBO J. 25 2006 1137 1147
    • (2006) EMBO J. , vol.25 , pp. 1137-1147
    • Gon, S.1    Camara, J.E.2    Klungsøyr, H.K.3    Crooke, E.4    Skarstad, K.5    Jon, B.J.6
  • 94
    • 23644456331 scopus 로고    scopus 로고
    • Coordinated replication and sequestration of oriC and dnaA are required for maintaining controlled once-per-cell-cycle initiation in Escherichia coli
    • L. Riber, and A. Løbner-Olesen Coordinated replication and sequestration of oriC and dnaA are required for maintaining controlled once-per-cell-cycle initiation in Escherichia coli J. Bacteriol. 187 16 2005 5605 5613
    • (2005) J. Bacteriol. , vol.187 , Issue.16 , pp. 5605-5613
    • Riber, L.1    Løbner-Olesen, A.2
  • 96
    • 0026490232 scopus 로고
    • Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli
    • D.S. Hwang, and A. Kornberg Opposed actions of regulatory proteins, DnaA and IciA, in opening the replication origin of Escherichia coli J. Biol. Chem. 267 1992 23087 23091
    • (1992) J. Biol. Chem. , vol.267 , pp. 23087-23091
    • Hwang, D.S.1    Kornberg, A.2
  • 97
    • 14544286823 scopus 로고    scopus 로고
    • Building a bacterial orisome: Emergence of new regulatory features for replication origin unwinding
    • A.C. Leonard, and J.E. Grimwade Building a bacterial orisome: emergence of new regulatory features for replication origin unwinding Mol. Microbiol. 55 2005 978 985
    • (2005) Mol. Microbiol. , vol.55 , pp. 978-985
    • Leonard, A.C.1    Grimwade, J.E.2
  • 98
    • 0026451648 scopus 로고
    • HU, the major histone-like protein of E. coli, modulates the binding of IHF to oriC
    • E. Bonnefoy, and J. Rouviere-Yaniv HU, the major histone-like protein of E. coli, modulates the binding of IHF to oriC EMBO J. 11 1992 4489 4496
    • (1992) EMBO J. , vol.11 , pp. 4489-4496
    • Bonnefoy, E.1    Rouviere-Yaniv, J.2
  • 99
    • 61349133630 scopus 로고    scopus 로고
    • Initiator titration complex formed at datA with the aid of IHF regulates replication timing in Escherichia coli
    • S. Nozaki, Y. Yamadaa, and T. Ogawa Initiator titration complex formed at datA with the aid of IHF regulates replication timing in Escherichia coli Genes Cells 14 2009 329 341
    • (2009) Genes Cells , vol.14 , pp. 329-341
    • Nozaki, S.1    Yamadaa, Y.2    Ogawa, T.3
  • 100
    • 0027419803 scopus 로고
    • A novel binding protein of the origin of the Escherichia coli chromosome
    • K. Skarstad, B. Thony, D.S. Hwang, and A. Kornberg A novel binding protein of the origin of the Escherichia coli chromosome J. Biol. Chem. 268 1993 5365 5370
    • (1993) J. Biol. Chem. , vol.268 , pp. 5365-5370
    • Skarstad, K.1    Thony, B.2    Hwang, D.S.3    Kornberg, A.4
  • 101
    • 0035971081 scopus 로고    scopus 로고
    • The Arc two-component signal transduction system inhibits in vitro Escherichia coli chromosomal initiation
    • Y.S. Lee, J.S. Han, Y. Jeon, and D.S. Hwang The Arc two-component signal transduction system inhibits in vitro Escherichia coli chromosomal initiation J. Biol. Chem. 276 2001 9917 9923
    • (2001) J. Biol. Chem. , vol.276 , pp. 9917-9923
    • Lee, Y.S.1    Han, J.S.2    Jeon, Y.3    Hwang, D.S.4
  • 102
    • 8544240894 scopus 로고    scopus 로고
    • DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication
    • T. Ishida, N. Akimitsu, T. Kashioka, M. Hatano, T. Kubota, Y. Ogatam, K. Sekimizu, and T. Katayama DiaA, a novel DnaA-binding protein, ensures the timely initiation of Escherichia coli chromosome replication J. Biol. Chem. 279 2004 45546 45555
    • (2004) J. Biol. Chem. , vol.279 , pp. 45546-45555
    • Ishida, T.1    Akimitsu, N.2    Kashioka, T.3    Hatano, M.4    Kubota, T.5    Ogatam, Y.6    Sekimizu, K.7    Katayama, T.8
  • 103
    • 34547683989 scopus 로고    scopus 로고
    • HobA - A novel protein involved in initiation of chromosomal replication in Helicobacter pylori
    • A. Zawilak-pawlik, A. Kois, K. Stingl, I.G. Boneca, and P. Skrobuk HobA - a novel protein involved in initiation of chromosomal replication in Helicobacter pylori Mol. Microbiol. 65 4 2007 979 994
    • (2007) Mol. Microbiol. , vol.65 , Issue.4 , pp. 979-994
    • Zawilak-Pawlik, A.1    Kois, A.2    Stingl, K.3    Boneca, I.G.4    Skrobuk, P.5
  • 104
    • 34547676738 scopus 로고    scopus 로고
    • Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli
    • G. Natrajan, D.R. Hall, A.C. Thompson, I. Gutsche, and L. Terradot Structural similarity between the DnaA-binding proteins HobA (HP1230) from Helicobacter pylori and DiaA from Escherichia coli Mol. Microbiol. 65 2007 995 1005
    • (2007) Mol. Microbiol. , vol.65 , pp. 995-1005
    • Natrajan, G.1    Hall, D.R.2    Thompson, A.C.3    Gutsche, I.4    Terradot, L.5
  • 105
    • 0032553470 scopus 로고    scopus 로고
    • Localization of bacterial DNA polymerase: Evidence for a factory model of replication
    • K.P. Lemon, and A.D. Grossman Localization of bacterial DNA polymerase: evidence for a factory model of replication Science 282 1998 1516 1519
    • (1998) Science , vol.282 , pp. 1516-1519
    • Lemon, K.P.1    Grossman, A.D.2
  • 106
    • 0034509678 scopus 로고    scopus 로고
    • Movement of replicating DNA through a stationary replisome
    • K.P. Lemon, and A.D. Grossman Movement of replicating DNA through a stationary replisome Mol. Cell 6 2000 1321 1330
    • (2000) Mol. Cell , vol.6 , pp. 1321-1330
    • Lemon, K.P.1    Grossman, A.D.2
  • 107
    • 41149121779 scopus 로고    scopus 로고
    • Independent positioning and action of Escherichia coli replisomes in live cells
    • R. Reyes-Lamothe, C. Possoz, O. Danilova, and D.J. Sherratt Independent positioning and action of Escherichia coli replisomes in live cells Cell 133 2008 90 102
    • (2008) Cell , vol.133 , pp. 90-102
    • Reyes-Lamothe, R.1    Possoz, C.2    Danilova, O.3    Sherratt, D.J.4
  • 108
    • 0035801637 scopus 로고    scopus 로고
    • A moving DNA replication factory in Caulobacter crescentus
    • R.B. Jensen, S.C. Wang, and L. Shapiro A moving DNA replication factory in Caulobacter crescentus EMBO J. 20 17 2001 14952 14963
    • (2001) EMBO J. , vol.20 , Issue.17 , pp. 14952-14963
    • Jensen, R.B.1    Wang, S.C.2    Shapiro, L.3
  • 109
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • B. Michel, S.D. Ehrlich, and M. Uzest DNA double-strand breaks caused by replication arrest EMBO J. 16 2 1997 430 438
    • (1997) EMBO J. , vol.16 , Issue.2 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 110
    • 1642443168 scopus 로고    scopus 로고
    • Mechanisms of replication fork restart in Escherichia coli
    • K.J. Marians Mechanisms of replication fork restart in Escherichia coli Philos. Trans. R. Soc. Lond. 359 2004 71 77
    • (2004) Philos. Trans. R. Soc. Lond. , vol.359 , pp. 71-77
    • Marians, K.J.1
  • 111
    • 0034123356 scopus 로고    scopus 로고
    • Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12
    • S.J. Sandler Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12 Genetics 155 2000 487 497
    • (2000) Genetics , vol.155 , pp. 487-497
    • Sandler, S.J.1
  • 112
    • 0034893101 scopus 로고    scopus 로고
    • PriA mutations that affect PriA-PriC function during replication restart
    • S.J. Sandler, J.D. McCool, T.T. Do, and R.V. Johansen PriA mutations that affect PriA-PriC function during replication restart Mol. Microbiol. 41 2001 697 704
    • (2001) Mol. Microbiol. , vol.41 , pp. 697-704
    • Sandler, S.J.1    McCool, J.D.2    Do, T.T.3    Johansen, R.V.4
  • 113
    • 27744535816 scopus 로고    scopus 로고
    • Homologous recombination by RecBCD and RecF pathways
    • M. Spies, and S.C. Kowalczykowski Homologous recombination by RecBCD and RecF pathways N.P. Higgins, The Bacterial Chromosome 2005 ASM Press Washington, DC 389 403
    • (2005) The Bacterial Chromosome , pp. 389-403
    • Spies, M.1    Kowalczykowski, S.C.2
  • 114
    • 0037436108 scopus 로고    scopus 로고
    • DNA damage-induced replication fork regression and processing in Escherichia coli
    • J. Courcelle, J.R. Donaldson, K.H. Chow, and C.T. Courcelle DNA damage-induced replication fork regression and processing in Escherichia coli Science 299 2003 1064 1067
    • (2003) Science , vol.299 , pp. 1064-1067
    • Courcelle, J.1    Donaldson, J.R.2    Chow, K.H.3    Courcelle, C.T.4
  • 115
    • 0034760094 scopus 로고    scopus 로고
    • A step backward in advancing DNA replication: Rescue of stalled replication forks by RecG
    • M.S. Dillingham, and S.C. Kowalczykowski A step backward in advancing DNA replication: rescue of stalled replication forks by RecG Mol. Cell 8 2001 734 736
    • (2001) Mol. Cell , vol.8 , pp. 734-736
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 116
    • 0036184234 scopus 로고    scopus 로고
    • Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities
    • A.V. Gregg, P. McGlynn, R.P. Jaktaji, and R.G. Lloyd Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities Mol. Cell 9 2002 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
  • 117
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • M.R. Singleton, S. Scaife, and D.B. Wigley Structural analysis of DNA replication fork reversal by RecG Cell 107 2001 79 89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 119
    • 0036348154 scopus 로고    scopus 로고
    • Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo
    • E.L. Bolt, and R.G. Lloyd Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo Mol. Cell 10 2002 187 198
    • (2002) Mol. Cell , vol.10 , pp. 187-198
    • Bolt, E.L.1    Lloyd, R.G.2
  • 120
    • 0032873606 scopus 로고    scopus 로고
    • Holliday junction processing in bacteria: Insights from the evolutionary conservation of Ruv-ABC, RecG and RusA
    • G.J. Sharples, S.M. Ingleston, and R.G. Lloyd Holliday junction processing in bacteria: insights from the evolutionary conservation of Ruv-ABC, RecG and RusA J. Bacteriol. 181 1999 5543 5550
    • (1999) J. Bacteriol. , vol.181 , pp. 5543-5550
    • Sharples, G.J.1    Ingleston, S.M.2    Lloyd, R.G.3
  • 121
    • 58449088827 scopus 로고    scopus 로고
    • A RecB-like helicase in Helicobacter pylori is important for DNA repair and host colonization
    • G. Wang, and R.J. Maier A RecB-like helicase in Helicobacter pylori is important for DNA repair and host colonization Infect. Immun. 77 1 2009 286 291
    • (2009) Infect. Immun. , vol.77 , Issue.1 , pp. 286-291
    • Wang, G.1    Maier, R.J.2
  • 122
    • 26944475629 scopus 로고    scopus 로고
    • Mutation and recombination in Helicobacter pylori: Mechanisms and role in generating strain diversity
    • C. Kraft, and S. Suerbaum Mutation and recombination in Helicobacter pylori: mechanisms and role in generating strain diversity Int. J. Med. Microbiol. 295 2005 299 305
    • (2005) Int. J. Med. Microbiol. , vol.295 , pp. 299-305
    • Kraft, C.1    Suerbaum, S.2
  • 123
    • 34249048365 scopus 로고    scopus 로고
    • Helicobacter pylori evolution and phenotypic diversification in a changing host
    • S. Suerbaum, and C. Josenhans Helicobacter pylori evolution and phenotypic diversification in a changing host Nat. Rev. Microbiol. 5 2007 441 452
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 441-452
    • Suerbaum, S.1    Josenhans, C.2
  • 124
    • 50849122026 scopus 로고    scopus 로고
    • Unveiling novel RecO distant orthologues involved in homologous recombination
    • S. Marsin, A. Mathieu, T. Kortulewski, R. Guerois, and J.P. Radicella Unveiling novel RecO distant orthologues involved in homologous recombination PLoS Genet. 4 2008 e1000146
    • (2008) PLoS Genet. , vol.4 , pp. 1000146
    • Marsin, S.1    Mathieu, A.2    Kortulewski, T.3    Guerois, R.4    Radicella, J.P.5
  • 125
    • 0028860607 scopus 로고
    • Cloning of the Helicobacter pylori recA gene and functional characterization of its product
    • W. Schmitt, S. Odenbreit, D. Heuermann, and R. Haas Cloning of the Helicobacter pylori recA gene and functional characterization of its product Mol. Gen. Genet. 248 1995 563 572
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 563-572
    • Schmitt, W.1    Odenbreit, S.2    Heuermann, D.3    Haas, R.4
  • 126
    • 0029066974 scopus 로고
    • Isolation of the Helicobacter pylori recA gene and involvement of the recA region in resistance to low pH
    • S.A. Thompson, and M.J. Blaser Isolation of the Helicobacter pylori recA gene and involvement of the recA region in resistance to low pH Infect. Immun. 63 1995 2185 2193
    • (1995) Infect. Immun. , vol.63 , pp. 2185-2193
    • Thompson, S.A.1    Blaser, M.J.2
  • 127
    • 1642581485 scopus 로고    scopus 로고
    • The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity
    • W. Fischer, and R. Haas The RecA protein of Helicobacter pylori requires a posttranslational modification for full activity J. Bacteriol. 186 2004 777 784
    • (2004) J. Bacteriol. , vol.186 , pp. 777-784
    • Fischer, W.1    Haas, R.2
  • 128
    • 47749093168 scopus 로고    scopus 로고
    • Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization
    • S.K. Amundsen, J. Fero, L.M. Hansen, G.A. Cromie, J.V. Solnick, G.R. Smith, and N.R. Salama Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization Mol. Microbiol. 69 2008 994 1007
    • (2008) Mol. Microbiol. , vol.69 , pp. 994-1007
    • Amundsen, S.K.1    Fero, J.2    Hansen, L.M.3    Cromie, G.A.4    Solnick, J.V.5    Smith, G.R.6    Salama, N.R.7
  • 129
    • 0037295442 scopus 로고    scopus 로고
    • RecFOR function is required for DNA repair and recombination in a RecA loading-deficient recB mutant of Escherichia coli
    • I. Ivancic-Bace, P. Peharec, S. Moslavac, N. Skrobot, E. Salaj-Smic, and K. Brcic-Kostic RecFOR function is required for DNA repair and recombination in a RecA loading-deficient recB mutant of Escherichia coli Genetics 163 2003 485 494
    • (2003) Genetics , vol.163 , pp. 485-494
    • Ivancic-Bace, I.1    Peharec, P.2    Moslavac, S.3    Skrobot, N.4    Salaj-Smic, E.5    Brcic-Kostic, K.6
  • 130
    • 76749109918 scopus 로고    scopus 로고
    • A major role of the RecFOR pathway in DNA double-strand-break repair through ESDSA in Deinococcus radiodurans
    • E. Bentchikou, P. Servant, G. Coste, and S. Sommer A major role of the RecFOR pathway in DNA double-strand-break repair through ESDSA in Deinococcus radiodurans PLoS Genet. 6 1 2010 e1000774
    • (2010) PLoS Genet. , vol.6 , Issue.1 , pp. 1000774
    • Bentchikou, E.1    Servant, P.2    Coste, G.3    Sommer, S.4
  • 131
    • 44949256406 scopus 로고    scopus 로고
    • Repair and antirepair DNA helicases in Helicobacter pylori
    • J. Kang, and M.J. Blaser Repair and antirepair DNA helicases in Helicobacter pylori J. Bacteriol. 190 12 2008 4218 4224
    • (2008) J. Bacteriol. , vol.190 , Issue.12 , pp. 4218-4224
    • Kang, J.1    Blaser, M.J.2
  • 132
    • 7744228869 scopus 로고    scopus 로고
    • Effect of host species on RecG phenotypes in Helicobacter pylori and Escherichia coli
    • J. Kang, D. Tavakoli, A. Tschumi, R.A. Aras, and M.J. Blaser Effect of host species on RecG phenotypes in Helicobacter pylori and Escherichia coli J. Bacteriol. 186 2004 7704 7713
    • (2004) J. Bacteriol. , vol.186 , pp. 7704-7713
    • Kang, J.1    Tavakoli, D.2    Tschumi, A.3    Aras, R.A.4    Blaser, M.J.5
  • 133
    • 37749034749 scopus 로고    scopus 로고
    • Critical role of RecN in recombinational DNA repair and survival of Helicobacter pylori
    • G. Wang, and R.J. Maier Critical role of RecN in recombinational DNA repair and survival of Helicobacter pylori Infect. Immun. 76 1 2008 153 160
    • (2008) Infect. Immun. , vol.76 , Issue.1 , pp. 153-160
    • Wang, G.1    Maier, R.J.2
  • 134
    • 0033391298 scopus 로고    scopus 로고
    • Mutation as an origin of genetic variability in Helicobacter pylori
    • G. Wang, M.Z. Humayun, and D.E. Taylor Mutation as an origin of genetic variability in Helicobacter pylori Trends Microbiol. 7 1999 488 493
    • (1999) Trends Microbiol. , vol.7 , pp. 488-493
    • Wang, G.1    Humayun, M.Z.2    Taylor, D.E.3
  • 135
    • 77957673732 scopus 로고    scopus 로고
    • DNA damage triggers genetic exchange in Helicobacter pylori
    • S.D. Marion, J. Fero, and N.R. Salama DNA damage triggers genetic exchange in Helicobacter pylori PLoS Pathog. 6 7 2010 e1001026
    • (2010) PLoS Pathog. , vol.6 , Issue.7 , pp. 1001026
    • Marion, S.D.1    Fero, J.2    Salama, N.R.3
  • 136
    • 75849129293 scopus 로고    scopus 로고
    • The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria
    • USA
    • Natrajan, G., Noirot-Gros, M.F., Zawilak-Pawlik, A., Kapp, U. and Terradot, L. (2009). The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria. Proc. Natl. Acad. Sci. USA 106, 21115-21120.
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 21115-21120
    • Natrajan, G.1    Noirot-Gros, M.F.2    Zawilak-Pawlik, A.3    Kapp, U.4    Terradot, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.