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Volumn 57, Issue 1, 2005, Pages 5-12

Protein-protein interactions in the eubacterial replisome

Author keywords

Bacillus subtilis; Bacteriophage; DNA replication; Elongation; Escherichia coli; Initiation; Termination

Indexed keywords

DNA DIRECTED DNA POLYMERASE GAMMA; DNA PRIMASE; HELICASE; HOLOENZYME; PRIMER RNA; REPLISOME; RNA DIRECTED RNA POLYMERASE;

EID: 18344385508     PISSN: 15216543     EISSN: None     Source Type: Journal    
DOI: 10.1080/15216540500058956     Document Type: Review
Times cited : (71)

References (72)
  • 2
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: Implications for general mechanisms underlying DNA replication initiation
    • Erzberger, J. P., Pirruccello, M. M., and Berger, J. M. (2002) The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 21, 4763-4773.
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 3
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • Messer, W. (2002) The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol. Rev. 26, 355-374.
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 355-374
    • Messer, W.1
  • 6
    • 0033229814 scopus 로고    scopus 로고
    • ATP- and ADP-DnaA protein, a molecular switch in gene regulation
    • Speck, C., Weigel, C., and Messer, W. (1999) ATP- and ADP-DnaA protein, a molecular switch in gene regulation. EMBO J. 18, 6169-6176.
    • (1999) EMBO J. , vol.18 , pp. 6169-6176
    • Speck, C.1    Weigel, C.2    Messer, W.3
  • 7
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • Marszalek, J. and Kaguni, J. M. (1994) DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. J. Biol. Chem. 269, 4883-4890.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4883-4890
    • Marszalek, J.1    Kaguni, J.M.2
  • 8
    • 0037222240 scopus 로고    scopus 로고
    • Strategies for helicase recruitment and loading in bacteria
    • Konieczny, I. (2003) Strategies for helicase recruitment and loading in bacteria. EMBO Rep. 4, 37-41.
    • (2003) EMBO Rep. , vol.4 , pp. 37-41
    • Konieczny, I.1
  • 9
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz, H., Weigel, C., and Messer, W. (2000) The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol. Microbiol. 37, 1270-1279.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 10
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel, S. S. and Picha, K. M. (2000) Structure and function of hexameric helicases. Annu. Rev. Biochem. 69, 651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 11
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II. Integration of helicases into cellular processes
    • Delagoutte, E. and von Hippel, P. H. (2003) Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II. Integration of helicases into cellular processes. Quart. Rev. Biophys. 36, 1-69.
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 12
    • 0035868712 scopus 로고    scopus 로고
    • The DnaB-DnaC complex: A structure based on dimers assembled around an occluded channel
    • Bárcena, M., Ruiz, T., Donate, L. E., Brown, S. E., Dixon, N. E., Radermacher, M., and Carazo, J. M. (2001) The DnaB-DnaC complex: a structure based on dimers assembled around an occluded channel. EMBO J. 20, 1462-1468.
    • (2001) EMBO J. , vol.20 , pp. 1462-1468
    • Bárcena, M.1    Ruiz, T.2    Donate, L.E.3    Brown, S.E.4    Dixon, N.E.5    Radermacher, M.6    Carazo, J.M.7
  • 13
    • 0028905501 scopus 로고
    • The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate
    • Dong, F., Gogol, E. P., and von Hippel, P. H. (1995) The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J. Biol. Chem. 270, 7462-7473.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7462-7473
    • Dong, F.1    Gogol, E.P.2    Von Hippel, P.H.3
  • 14
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • Bujalowski, W., Klonowska, M. M., and Jezewska, M. J. (1994) Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 269, 31350-31358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 15
    • 0037616144 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex
    • Galletto, R., Jezewska, M. J., and Bujalowski, W. (2003) Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex. J. Mol. Biol. 329, 441-465.
    • (2003) J. Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 17
    • 0029832926 scopus 로고    scopus 로고
    • The extreme C terminus of primase is required for interaction with DnaB at the replication fork
    • Tougu, K. and Marians, K. J. (1996) The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J. Biol. Chem. 271, 21391-21397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 19
    • 0347993077 scopus 로고    scopus 로고
    • Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis
    • Mitkova, A. V., Khopde, S. M., and Biswas, S. B. (2003) Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J. Biol. Chem. 278, 52253-52261.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 20
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • Bird, L. E., Pan, H., Soultanas, P., and Wigley, D. B. (2000) Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39, 171-182.
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 21
    • 2942679433 scopus 로고    scopus 로고
    • DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings
    • Thirlway, J., Turner, I. J., Gibson, C. T., Gardiner, L., Brady, K., Allen, S., Roberts, C. J., and Soultanas, P. (2004) DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings. Nucleic Acids Res. 31, 2977 - 2986.
    • (2004) Nucleic Acids Res. , vol.31 , pp. 2977-2986
    • Thirlway, J.1    Turner, I.J.2    Gibson, C.T.3    Gardiner, L.4    Brady, K.5    Allen, S.6    Roberts, C.J.7    Soultanas, P.8
  • 23
    • 0345276497 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional primase-helicase of bacteriophage T7
    • Toth, E. A., Li, Y., Sawaya, M. R., Cheng, Y., and Ellenberger, T. (2003) The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol. Cell 12, 1113-1123.
    • (2003) Mol. Cell , vol.12 , pp. 1113-1123
    • Toth, E.A.1    Li, Y.2    Sawaya, M.R.3    Cheng, Y.4    Ellenberger, T.5
  • 24
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: Studies of subunit arrangement and functional consequences
    • McHenry, C. S. (2003) Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences. Mol. Microbiol. 49, 1157-1165.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1157-1165
    • McHenry, C.S.1
  • 25
    • 0033619538 scopus 로고    scopus 로고
    • Two functional domains of the ε subunit of DNA polymerase III
    • Perrino, F. W., Harvey, S., and McNeill, S. M. (1999) Two functional domains of the ε subunit of DNA polymerase III. Biochemistry 38, 16001-16009.
    • (1999) Biochemistry , vol.38 , pp. 16001-16009
    • Perrino, F.W.1    Harvey, S.2    McNeill, S.M.3
  • 26
    • 0036229246 scopus 로고    scopus 로고
    • Structural basis for proofreading during replication of the Escherichia coli chromosome
    • Hamdan, S., Carr, P. D., Brown, S. E., Ollis, D. L., and Dixon, N. E. (2002) Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure 10, 535-546.
    • (2002) Structure , vol.10 , pp. 535-546
    • Hamdan, S.1    Carr, P.D.2    Brown, S.E.3    Ollis, D.L.4    Dixon, N.E.5
  • 28
    • 0034056323 scopus 로고    scopus 로고
    • NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli
    • Keniry, M. A., Berthon, H. A., Yang, J. Y., Miles, C. S., and Dixon, N. E. (2000) NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli. Protein Sci. 9, 721-733.
    • (2000) Protein Sci. , vol.9 , pp. 721-733
    • Keniry, M.A.1    Berthon, H.A.2    Yang, J.Y.3    Miles, C.S.4    Dixon, N.E.5
  • 32
    • 0025355475 scopus 로고
    • Translational frameshifting generates the γ subunit of DNA polymerase III holoenzyme
    • Tsuchihashi, Z. and Kornberg, A. (1990) Translational frameshifting generates the γ subunit of DNA polymerase III holoenzyme. Proc. Natl. Acad. Sci. USA 87, 2516-2520.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2516-2520
    • Tsuchihashi, Z.1    Kornberg, A.2
  • 33
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • Jeruzalmi, D., O'Donnell, M., and Kuriyan, J. (2001) Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III. Cell 106, 429-441.
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 34
    • 0035830939 scopus 로고    scopus 로고
    • τ binds and organizes Escherichia coli replication proteins through distinct domains. Partial proteolysis of terminally tagged τ to determine candidate domains and to assign domain V as the α binding domain
    • Gao, D. and McHenry, C. S. (2001) τ binds and organizes Escherichia coli replication proteins through distinct domains. Partial proteolysis of terminally tagged τ to determine candidate domains and to assign domain V as the α binding domain. J. Biol. Chem. 276, 4433-4440.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 36
    • 0035830834 scopus 로고    scopus 로고
    • τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of τ, binds the replication fork helicase, DnaB
    • Gao, D. and McHenry, C. S. (2001) τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of τ, binds the replication fork helicase, DnaB. J. Biol. Chem. 276, 4441-4446.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4441-4446
    • Gao, D.1    McHenry, C.S.2
  • 37
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong, X. -P., Onrust, R., O'Donnell, M., and Kuriyan, J. (1992) Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp. Cell 69, 425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 38
    • 0035943399 scopus 로고    scopus 로고
    • Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III
    • Jeruzalmi, D., Yurieva, O., Zhao, Y., Young, M., Stewart, J., Hingorani, M., O'Donnell, M., and Kuriyan, J. (2001) Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106, 417-428.
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1    Yurieva, O.2    Zhao, Y.3    Young, M.4    Stewart, J.5    Hingorani, M.6    O'Donnell, M.7    Kuriyan, J.8
  • 39
    • 0035856473 scopus 로고    scopus 로고
    • Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC
    • O'Donnell, M., Jeruzalmi, D., and Kuriyan, J. (2001) Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC. Curr. Biol. 11, R935-R946.
    • (2001) Curr. Biol. , vol.11
    • O'Donnell, M.1    Jeruzalmi, D.2    Kuriyan, J.3
  • 40
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III β sliding clamp on DNA. Bona fide primer/templates preferentially trigger the y complex to hydrolyze ATP and load the clamp
    • Ason, B., Handayani, R., Williams, C. R., Bertram, J. G., Hingorani, M. M., O'Donnell, M., Goodman, M. F., and Bloom, L. B. (2003) Mechanism of loading the Escherichia coli DNA polymerase III β sliding clamp on DNA. Bona fide primer/templates preferentially trigger the y complex to hydrolyze ATP and load the clamp. J. Biol. Chem. 278, 10033-10040.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10033-10040
    • Ason, B.1    Handayani, R.2    Williams, C.R.3    Bertram, J.G.4    Hingorani, M.M.5    O'Donnell, M.6    Goodman, M.F.7    Bloom, L.B.8
  • 41
    • 0000210315 scopus 로고    scopus 로고
    • Identification of the β-binding domain of the α subunit of Escherichia coli polymerase III holoenzyme
    • Kim, D. R. and McHenry, C. S. (1996) Identification of the β-binding domain of the α subunit of Escherichia coli polymerase III holoenzyme. J. Biol. Chem. 271, 20699-20704.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20699-20704
    • Kim, D.R.1    McHenry, C.S.2
  • 42
    • 0030070111 scopus 로고    scopus 로고
    • A molecular switch in a replication machine defined by an internal competition for protein rings
    • Naktinis, V., Turner, J., and O'Donnell, M. (1996) A molecular switch in a replication machine defined by an internal competition for protein rings. Cell 84, 137-145.
    • (1996) Cell , vol.84 , pp. 137-145
    • Naktinis, V.1    Turner, J.2    O'Donnell, M.3
  • 43
    • 0035949599 scopus 로고    scopus 로고
    • A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems
    • Dalrymple, B. P., Kongsuwan, K., Wijffels, G., Dixon, N. E., and Jennings, P. A. (2001) A universal protein-protein interaction motif in the eubacterial DNA replication and repair systems. Proc. Natl. Acad. Sci. USA 98, 11627-11632.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11627-11632
    • Dalrymple, B.P.1    Kongsuwan, K.2    Wijffels, G.3    Dixon, N.E.4    Jennings, P.A.5
  • 45
    • 0032504050 scopus 로고    scopus 로고
    • The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase
    • Katayama, T., Kubota, T., Kurokawa, K., Crooke, E., and Sekimizu, K. (1998) The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase. Cell 94, 61-71.
    • (1998) Cell , vol.94 , pp. 61-71
    • Katayama, T.1    Kubota, T.2    Kurokawa, K.3    Crooke, E.4    Sekimizu, K.5
  • 46
    • 0035422651 scopus 로고    scopus 로고
    • Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli
    • Kato, J. and Katayama, T. (2001) Hda, a novel DnaA-related protein, regulates the replication cycle in Escherichia coli. EMBO J. 20, 4253-4262.
    • (2001) EMBO J. , vol.20 , pp. 4253-4262
    • Kato, J.1    Katayama, T.2
  • 47
    • 2442504231 scopus 로고    scopus 로고
    • Interaction of the sliding clamp β-subunit and Hda, a DnaA-related protein
    • Kurz, M., Dalrymple, B., Wijffels, G., and Kongsuwan, K. (2004) Interaction of the sliding clamp β-subunit and Hda, a DnaA-related protein. J. Bacteriol. 186, 3508-3515.
    • (2004) J. Bacteriol. , vol.186 , pp. 3508-3515
    • Kurz, M.1    Dalrymple, B.2    Wijffels, G.3    Kongsuwan, K.4
  • 48
    • 0034628915 scopus 로고    scopus 로고
    • Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage
    • Moarefi, I., Jeruzalmi, D., Turner, J., O'Donnell, M., and Kuriyan, J. (2000) Crystal structure of the DNA polymerase processivity factor of T4 bacteriophage. J. Mol. Biol. 296, 1215-1223.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1215-1223
    • Moarefi, I.1    Jeruzalmi, D.2    Turner, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 49
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature 391, 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 50
    • 0031009811 scopus 로고    scopus 로고
    • Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-Å resolution
    • Raghunathan, S., Ricard, C. S., Lohman, T. M., and Waksman, G. (1997) Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-Å resolution. Proc. Natl. Acad. Sci. USA 94, 6652-6657.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6652-6657
    • Raghunathan, S.1    Ricard, C.S.2    Lohman, T.M.3    Waksman, G.4
  • 51
    • 0033887437 scopus 로고    scopus 로고
    • Structure of the DNA binding domain of E. coli SSB bound to ssDNA
    • Raghunathan, S., Kozlov, A. G., Lohman, T. M., and Waksman, G. (2000) Structure of the DNA binding domain of E. coli SSB bound to ssDNA. Nat. Struct. Biol. 7, 648-652.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 648-652
    • Raghunathan, S.1    Kozlov, A.G.2    Lohman, T.M.3    Waksman, G.4
  • 52
    • 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
    • Glover, B. P. and McHenry, C. S. (1998) 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, 23476-23484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23476-23484
    • Glover, B.P.1    McHenry, C.S.2
  • 53
    • 1642521025 scopus 로고    scopus 로고
    • Crystal structure of the chi:psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex
    • Gulbis, J. M., Kazmirski, S. L., Finkelstein, J., Kelman, Z., O'Donnell, M., and Kuriyan, J. (2004) Crystal structure of the chi:psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex. Eur. J. Biochem. 271, 439-449.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 439-449
    • Gulbis, J.M.1    Kazmirski, S.L.2    Finkelstein, J.3    Kelman, Z.4    O'Donnell, M.5    Kuriyan, J.6
  • 54
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA-A three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov, A., Kelman, Z., and O'Donnell, M. (1999) Trading places on DNA-A three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96, 153-163.
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 55
    • 0026794488 scopus 로고
    • Arrest of bacterial DNA replication
    • Hill, T. M. (1992) Arrest of bacterial DNA replication. Annu. Rev. Microbiol. 46, 603-633.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 603-633
    • Hill, T.M.1
  • 56
    • 0000384235 scopus 로고    scopus 로고
    • Features of the chromosomal terminus
    • Neidhardt, F. C., ed. American Society for Microbiology, Washington, D.C.
    • Hill, T.M. (1996) Features of the chromosomal terminus. In Escherichia coli and Salmonella: Cellular and Molecular Biology (Neidhardt, F. C., ed.). Vol. 2, pp. 1602-1614, American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , vol.2 , pp. 1602-1614
    • Hill, T.M.1
  • 57
    • 0029908981 scopus 로고    scopus 로고
    • Structure of a replication-terminator protein complexed with DNA
    • Kamada, K., Horiuchi, T., Ohsumi, K., Shimamoto, N., and Morikawa, K. (1996) Structure of a replication-terminator protein complexed with DNA. Nature 383, 598-603.
    • (1996) Nature , vol.383 , pp. 598-603
    • Kamada, K.1    Horiuchi, T.2    Ohsumi, K.3    Shimamoto, N.4    Morikawa, K.5
  • 58
    • 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., Brown, S. E., Kralicek, A. V., Miles, C. S., Love, C. A., and Dixon, N. E. (2000) 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) Biochemistry , vol.39 , pp. 11989-11999
    • Neylon, C.1    Brown, S.E.2    Kralicek, A.V.3    Miles, C.S.4    Love, C.A.5    Dixon, N.E.6
  • 59
    • 0030740823 scopus 로고    scopus 로고
    • Replication fork arrest and termination of chromosome replication in Bacillus subtilis
    • Wake, R. G. (1997) Replication fork arrest and termination of chromosome replication in Bacillus subtilis. FEMS Microbiol. Lett. 153, 247-254.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 247-254
    • Wake, R.G.1
  • 60
    • 0033032373 scopus 로고    scopus 로고
    • Termination of DNA replication of bacterial and plasmid chromosomes
    • Bussiere, D. E. and Bastia, D. (1999) Termination of DNA replication of bacterial and plasmid chromosomes. Mol. Microbiol. 31, 1611-1618.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1611-1618
    • Bussiere, D.E.1    Bastia, D.2
  • 62
    • 0035859954 scopus 로고    scopus 로고
    • Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction
    • Mulugu, S., Potnis, A., Shamsuzzaman, Taylor, J., Alexander, K., and Bastia, D. (2001) Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction. Proc. Natl. Acad. Sci. USA 98, 9569-9574.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9569-9574
    • Mulugu, S.1    Potnis, A.2    Shamsuzzaman3    Taylor, J.4    Alexander, K.5    Bastia, D.6
  • 63
    • 0023484986 scopus 로고
    • Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase
    • Lee, M. S. and Marians, K. J. (1987) Escherichia coli replication factor Y, a component of the primosome, can act as a DNA helicase. Proc. Natl. Acad. Sci. USA 84, 8345-8349.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8345-8349
    • Lee, M.S.1    Marians, K.J.2
  • 64
    • 0023876623 scopus 로고
    • The primosomal protein n of Escherichia coli is a DNA helicase
    • Lasken, R. S. and Kornberg, A. (1988) The primosomal protein n of Escherichia coli is a DNA helicase. J. Biol. Chem. 263, 5512-5518.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5512-5518
    • Lasken, R.S.1    Kornberg, A.2
  • 65
    • 0027305619 scopus 로고
    • Strand switching of a replicative DNA helicase promoted by the E. coli primosome
    • Allen, G. C., Jr., Dixon, N. E., and Kornberg, A. (1993) Strand switching of a replicative DNA helicase promoted by the E. coli primosome. Cell 74, 713-722.
    • (1993) Cell , vol.74 , pp. 713-722
    • Allen Jr., G.C.1    Dixon, N.E.2    Kornberg, A.3
  • 66
    • 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
  • 68
    • 0032553470 scopus 로고    scopus 로고
    • Localization of bacterial DNA polymerase: Evidence for a factory model of replication
    • Lemon, K. P. and Grossman, A. D. (1998) Localization of bacterial DNA polymerase: Evidence for a factory model of replication. Science 282, 1516-1519.
    • (1998) Science , vol.282 , pp. 1516-1519
    • Lemon, K.P.1    Grossman, A.D.2
  • 69
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes
    • Kaplan, D. L. and O'Donnell, M. (2004) Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes. Mol. Cell 15, 453-465.
    • (2004) Mol. Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 70
    • 0034509678 scopus 로고    scopus 로고
    • Movement of replicating DNA through a stationary replisome
    • Lemon, K. P. and Grossman, A. D. (2000) Movement of replicating DNA through a stationary replisome. Mol. Cell 6, 1321-1330.
    • (2000) Mol. Cell , vol.6 , pp. 1321-1330
    • Lemon, K.P.1    Grossman, A.D.2
  • 71
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chape rone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999) AAA+: A class of chape rone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43.
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 72
    • 0035920173 scopus 로고    scopus 로고
    • Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase
    • Ludlam, A. V., McNatt, M. W., Carr, K. M., and Kaguni, J. M. (2001) Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase. J. Biol. Chem. 276, 27345-27353.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27345-27353
    • Ludlam, A.V.1    McNatt, M.W.2    Carr, K.M.3    Kaguni, J.M.4


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