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Volumn 15, Issue 4, 2007, Pages 156-164

Replisome mechanics: insights into a twin DNA polymerase machine

Author keywords

[No Author keywords available]

Indexed keywords

REPLISOME;

EID: 34047149973     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2007.02.007     Document Type: Review
Times cited : (73)

References (70)
  • 2
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: components and dynamics at the replication fork
    • Johnson A., and O'Donnell M. 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
  • 3
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences
    • McHenry C.S. 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
  • 4
    • 0034921855 scopus 로고    scopus 로고
    • Replisome-mediated DNA replication
    • Benkovic S.J., et al. Replisome-mediated DNA replication. Annu. Rev. Biochem. 70 (2001) 181-208
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 181-208
    • Benkovic, S.J.1
  • 5
    • 33749033347 scopus 로고    scopus 로고
    • The replication clamp-loading machine at work in the three domains of life
    • Indiani C., and O'Donnell M. The replication clamp-loading machine at work in the three domains of life. Nat. Rev. Mol. Cell Biol. 7 (2006) 751-761
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 751-761
    • Indiani, C.1    O'Donnell, M.2
  • 6
    • 0022977660 scopus 로고
    • The Escherichia coli DnaB replication protein is a DNA helicase
    • LeBowitz J.H., and McMacken R. The Escherichia coli DnaB replication 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
  • 7
    • 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. Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes. Mol. Cell 15 (2004) 453-465
    • (2004) Mol. Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 8
    • 0033790340 scopus 로고    scopus 로고
    • Regulation of chromosome replication
    • Kelly T.J., and Brown G.W. Regulation of chromosome replication. Annu. Rev. Biochem. 69 (2000) 829-880
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 829-880
    • Kelly, T.J.1    Brown, G.W.2
  • 9
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell S.P., and Dutta A. 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
  • 10
    • 0344198460 scopus 로고    scopus 로고
    • Perpetuating the double helix: molecular machines at eukaryotic DNA replication origins
    • Mendez J., and Stillman B. Perpetuating the double helix: molecular machines at eukaryotic DNA replication origins. Bioessays 25 (2003) 1158-1167
    • (2003) Bioessays , vol.25 , pp. 1158-1167
    • Mendez, J.1    Stillman, B.2
  • 12
    • 33747332833 scopus 로고    scopus 로고
    • The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision
    • Amado L., and Kuzminov A. The replication intermediates in Escherichia coli are not the product of DNA processing or uracil excision. J. Biol. Chem. 281 (2006) 22635-22646
    • (2006) J. Biol. Chem. , vol.281 , pp. 22635-22646
    • Amado, L.1    Kuzminov, A.2
  • 13
    • 33745932747 scopus 로고    scopus 로고
    • DNA replication: keep moving and don't mind the gap
    • Langston L.D., and O'Donnell M. DNA replication: keep moving and don't mind the gap. Mol. Cell 23 (2006) 155-160
    • (2006) Mol. Cell , vol.23 , pp. 155-160
    • Langston, L.D.1    O'Donnell, M.2
  • 14
    • 0034177963 scopus 로고    scopus 로고
    • PriA-directed replication fork restart in Escherichia coli
    • Marians K.J. PriA-directed replication fork restart in Escherichia coli. Trends Biochem. Sci. 25 (2000) 185-189
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 185-189
    • Marians, K.J.1
  • 15
    • 4444267632 scopus 로고    scopus 로고
    • Multiple pathways process stalled replication forks
    • Michel B., et al. Multiple pathways process stalled replication forks. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 12783-12788
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12783-12788
    • Michel, B.1
  • 16
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller R.C., and Marians K.J. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7 (2006) 932-943
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 17
    • 0019223518 scopus 로고
    • Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system
    • Sinha N.K., et al. Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system. J. Biol. Chem. 255 (1980) 4290-4293
    • (1980) J. Biol. Chem. , vol.255 , pp. 4290-4293
    • Sinha, N.K.1
  • 18
    • 0028093437 scopus 로고
    • An explanation for lagging strand replication: polymerase hopping among DNA sliding clamps
    • Stukenberg P.T., et al. An explanation for lagging strand replication: polymerase hopping among DNA sliding clamps. Cell 78 (1994) 877-887
    • (1994) Cell , vol.78 , pp. 877-887
    • Stukenberg, P.T.1
  • 19
    • 0034602402 scopus 로고    scopus 로고
    • Two distinct triggers for cycling of the lagging strand polymerase at the replication fork
    • Li X., and Marians K.J. Two distinct triggers for cycling of the lagging strand polymerase at the replication fork. J. Biol. Chem. 275 (2000) 34757-34765
    • (2000) J. Biol. Chem. , vol.275 , pp. 34757-34765
    • Li, X.1    Marians, K.J.2
  • 20
    • 0036535908 scopus 로고    scopus 로고
    • Clamp loaders and sliding clamps
    • Jeruzalmi D., et al. Clamp loaders and sliding clamps. Curr. Opin. Struct. Biol. 12 (2002) 217-224
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 217-224
    • Jeruzalmi, D.1
  • 21
    • 0027217643 scopus 로고
    • Compilation, alignment, and phylogenetic relationships of DNA polymerases
    • Braithwaite D.K., and Ito J. Compilation, alignment, and phylogenetic relationships of DNA polymerases. Nucleic Acids Res. 21 (1993) 787-802
    • (1993) Nucleic Acids Res. , vol.21 , pp. 787-802
    • Braithwaite, D.K.1    Ito, J.2
  • 22
    • 33748146483 scopus 로고    scopus 로고
    • Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III
    • Lamers M.H., et al. Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III. Cell 126 (2006) 881-892
    • (2006) Cell , vol.126 , pp. 881-892
    • Lamers, M.H.1
  • 23
    • 33748146034 scopus 로고    scopus 로고
    • The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
    • Bailey S., et al. The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell 126 (2006) 893-904
    • (2006) Cell , vol.126 , pp. 893-904
    • Bailey, S.1
  • 24
    • 0025809742 scopus 로고
    • Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme
    • Stukenberg P.T., et al. Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 266 (1991) 11328-11334
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1
  • 25
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S., et al. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79 (1994) 1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1
  • 26
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis J.M., et al. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 87 (1996) 297-306
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1
  • 27
    • 0026717535 scopus 로고
    • Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp
    • Kong X.P., et al. Three-dimensional structure of the β subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69 (1992) 425-437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1
  • 28
    • 0031038379 scopus 로고    scopus 로고
    • Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen
    • Mossi R., et al. Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. J. Biol. Chem. 272 (1997) 1769-1776
    • (1997) J. Biol. Chem. , vol.272 , pp. 1769-1776
    • Mossi, R.1
  • 29
    • 0033777562 scopus 로고    scopus 로고
    • The puzzle of PCNA's many partners
    • Warbrick E. The puzzle of PCNA's many partners. Bioessays 22 (2000) 997-1006
    • (2000) Bioessays , vol.22 , pp. 997-1006
    • Warbrick, E.1
  • 30
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman G.D., et al. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 429 (2004) 724-730
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1
  • 31
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III
    • Jeruzalmi D., et al. Crystal structure of the processivity clamp loader gamma (γ) complex of E. coli DNA polymerase III. Cell 106 (2001) 429-441
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1
  • 32
    • 0027314532 scopus 로고
    • DNA polymerase III accessory proteins. IV. Characterization of chi and psi
    • Xiao H., et al. DNA polymerase III accessory proteins. IV. Characterization of chi and psi. J. Biol. Chem. 268 (1993) 11779-11784
    • (1993) J. Biol. Chem. , vol.268 , pp. 11779-11784
    • Xiao, H.1
  • 33
    • 0032522760 scopus 로고    scopus 로고
    • Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
    • Kelman Z., et al. Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly. EMBO J. 17 (1998) 2436-2449
    • (1998) EMBO J. , vol.17 , pp. 2436-2449
    • Kelman, Z.1
  • 34
    • 0032483511 scopus 로고    scopus 로고
    • The chi psi 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. The chi psi 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
  • 35
    • 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., et al. Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96 (1999) 153-163
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1
  • 36
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., et al. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9 (1999) 27-43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1
  • 37
    • 0034602163 scopus 로고    scopus 로고
    • The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli
    • Leu F.P., et al. The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli. J. Biol. Chem. 275 (2000) 34609-34618
    • (2000) J. Biol. Chem. , vol.275 , pp. 34609-34618
    • Leu, F.P.1
  • 38
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • Turner J., et al. The internal workings of a DNA polymerase clamp-loading machine. EMBO J. 18 (1999) 771-783
    • (1999) EMBO J. , vol.18 , pp. 771-783
    • Turner, J.1
  • 39
    • 0029019805 scopus 로고
    • Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp
    • Naktinis V., et al. Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. II. Intermediate complex between the clamp loader and its clamp. J. Biol. Chem. 270 (1995) 13358-13365
    • (1995) J. Biol. Chem. , vol.270 , pp. 13358-13365
    • Naktinis, V.1
  • 40
    • 0032544708 scopus 로고    scopus 로고
    • ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme
    • Hingorani M.M., and O'Donnell M. ATP binding to the Escherichia coli clamp loader powers opening of the ring-shaped clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 273 (1998) 24550-24563
    • (1998) J. Biol. Chem. , vol.273 , pp. 24550-24563
    • Hingorani, M.M.1    O'Donnell, M.2
  • 41
    • 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., et al. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III. Cell 106 (2001) 417-428
    • (2001) Cell , vol.106 , pp. 417-428
    • Jeruzalmi, D.1
  • 42
    • 0037515607 scopus 로고    scopus 로고
    • Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine
    • Johnson A., and O'Donnell M. Ordered ATP hydrolysis in the gamma complex clamp loader AAA+ machine. J. Biol. Chem. 278 (2003) 14406-14413
    • (2003) J. Biol. Chem. , vol.278 , pp. 14406-14413
    • Johnson, A.1    O'Donnell, M.2
  • 43
    • 1042266661 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the beta and DNA binding activities of the gamma complex
    • Snyder A.K., et al. Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp: II. Uncoupling the beta and DNA binding activities of the gamma complex. J. Biol. Chem. 279 (2004) 4386-4393
    • (2004) J. Biol. Chem. , vol.279 , pp. 4386-4393
    • Snyder, A.K.1
  • 44
    • 0025303309 scopus 로고
    • The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting
    • Flower A.M., and McHenry C.S. The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 3713-3717
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3713-3717
    • Flower, A.M.1    McHenry, C.S.2
  • 45
    • 0025355475 scopus 로고
    • Translational frameshifting generates the gamma subunit of DNA polymerase III holoenzyme
    • Tsuchihashi Z., and Kornberg A. Translational frameshifting generates the gamma subunit of DNA polymerase III holoenzyme. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 2516-2520
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 2516-2520
    • Tsuchihashi, Z.1    Kornberg, A.2
  • 46
    • 0035830847 scopus 로고    scopus 로고
    • Tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain III, shared by gamma and tau, binds delta delta ′ and chi psi
    • Gao D., and McHenry C.S. Tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain III, shared by gamma and tau, binds delta delta ′ and chi psi. J. Biol. Chem. 276 (2001) 4447-4453
    • (2001) J. Biol. Chem. , vol.276 , pp. 4447-4453
    • Gao, D.1    McHenry, C.S.2
  • 47
    • 0035830939 scopus 로고    scopus 로고
    • tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain
    • Gao D., and McHenry C.S. tau binds and organizes Escherichia coli replication through distinct domains. Partial proteolysis of terminally tagged tau to determine candidate domains and to assign domain V as the alpha binding domain. J. Biol. Chem. 276 (2001) 4433-4440
    • (2001) J. Biol. Chem. , vol.276 , pp. 4433-4440
    • Gao, D.1    McHenry, C.S.2
  • 48
    • 0034423473 scopus 로고    scopus 로고
    • A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta′ with DnaX(4) forms DnaX(3)deltadelta′
    • Pritchard A.E., et al. A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta′ with DnaX(4) forms DnaX(3)deltadelta′. EMBO J. 19 (2000) 6536-6545
    • (2000) EMBO J. , vol.19 , pp. 6536-6545
    • Pritchard, A.E.1
  • 49
    • 0029058292 scopus 로고
    • Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader
    • Onrust R., et al. Assembly of a chromosomal replication machine: two DNA polymerases, a clamp loader, and sliding clamps in one holoenzyme particle. I. Organization of the clamp loader. J. Biol. Chem. 270 (1995) 13348-13357
    • (1995) J. Biol. Chem. , vol.270 , pp. 13348-13357
    • Onrust, R.1
  • 50
    • 0034603089 scopus 로고    scopus 로고
    • The DnaX-binding subunits delta′ and psi are bound to gamma and not tau in the DNA polymerase III holoenzyme
    • Glover B.P., and McHenry C.S. The DnaX-binding subunits delta′ and psi are bound to gamma and not tau in the DNA polymerase III holoenzyme. J. Biol. Chem. 275 (2000) 3017-3020
    • (2000) J. Biol. Chem. , vol.275 , pp. 3017-3020
    • Glover, B.P.1    McHenry, C.S.2
  • 51
    • 0035967930 scopus 로고    scopus 로고
    • The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases
    • Glover B.P., and McHenry C.S. The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases. Cell 105 (2001) 925-934
    • (2001) Cell , vol.105 , pp. 925-934
    • Glover, B.P.1    McHenry, C.S.2
  • 52
    • 0029150469 scopus 로고
    • Characterization of the five replication factor C genes of Saccharomyces cerevisiae
    • Cullmann G., et al. Characterization of the five replication factor C genes of Saccharomyces cerevisiae. Mol. Cell. Biol. 15 (1995) 4661-4671
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4661-4671
    • Cullmann, G.1
  • 53
    • 25444469141 scopus 로고    scopus 로고
    • Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen
    • Kazmirski S.L., et al. Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13801-13806
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13801-13806
    • Kazmirski, S.L.1
  • 54
    • 25444480278 scopus 로고    scopus 로고
    • Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis
    • Miyata T., et al. Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 13795-13800
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13795-13800
    • Miyata, T.1
  • 55
    • 34047179554 scopus 로고    scopus 로고
    • Yao, N.Y. et al. (2006) Mechanism of PCNA clamp opening by RFC. J. Biol. Chem.
  • 56
    • 15544366916 scopus 로고    scopus 로고
    • Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex
    • Goedken E.R., et al. Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complex. Nat. Struct. Mol. Biol. 12 (2005) 183-190
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 183-190
    • Goedken, E.R.1
  • 57
    • 0035860719 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen
    • Gomes X.V., and Burgers P.M. ATP utilization by yeast replication factor C. I. ATP-mediated interaction with DNA and with proliferating cell nuclear antigen. J. Biol. Chem. 276 (2001) 34768-34775
    • (2001) J. Biol. Chem. , vol.276 , pp. 34768-34775
    • Gomes, X.V.1    Burgers, P.M.2
  • 58
    • 0035860694 scopus 로고    scopus 로고
    • ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA
    • Gomes X.V., et al. ATP utilization by yeast replication factor C. II. Multiple stepwise ATP binding events are required to load proliferating cell nuclear antigen onto primed DNA. J. Biol. Chem. 276 (2001) 34776-34783
    • (2001) J. Biol. Chem. , vol.276 , pp. 34776-34783
    • Gomes, X.V.1
  • 59
    • 0034723355 scopus 로고    scopus 로고
    • A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the gamma complex clamp loader
    • Ason B., et al. A model for Escherichia coli DNA polymerase III holoenzyme assembly at primer/template ends. DNA triggers a change in binding specificity of the gamma complex clamp loader. J. Biol. Chem. 275 (2000) 3006-3015
    • (2000) J. Biol. Chem. , vol.275 , pp. 3006-3015
    • Ason, B.1
  • 60
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp
    • Ason B., et al. Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp. J. Biol. Chem. 278 (2003) 10033-10040
    • (2003) J. Biol. Chem. , vol.278 , pp. 10033-10040
    • Ason, B.1
  • 61
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement
    • Kim S., et al. Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 84 (1996) 643-650
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1
  • 62
    • 1542405310 scopus 로고    scopus 로고
    • Eukaryotic MCM proteins: beyond replication initiation
    • Forsburg S.L. Eukaryotic MCM proteins: beyond replication initiation. Microbiol. Mol. Biol. Rev. 68 (2004) 109-131
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 109-131
    • Forsburg, S.L.1
  • 63
    • 0035253410 scopus 로고    scopus 로고
    • Is the MCM2-7 complex the eukaryotic DNA replication fork helicase?
    • Labib K., and Diffley J.F. Is the MCM2-7 complex the eukaryotic DNA replication fork helicase?. Curr. Opin. Genet. Dev. 11 (2001) 64-70
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 64-70
    • Labib, K.1    Diffley, J.F.2
  • 64
    • 0035793113 scopus 로고    scopus 로고
    • Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6 and 7 complex requires forked DNA structures
    • Lee J.K., and Hurwitz J. Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6 and 7 complex requires forked DNA structures. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 54-59
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 54-59
    • Lee, J.K.1    Hurwitz, J.2
  • 65
    • 0030859463 scopus 로고    scopus 로고
    • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex
    • Ishimi Y. A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. J. Biol. Chem. 272 (1997) 24508-24513
    • (1997) J. Biol. Chem. , vol.272 , pp. 24508-24513
    • Ishimi, Y.1
  • 66
    • 0347157844 scopus 로고    scopus 로고
    • Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex
    • Kaplan D.L., et al. Mcm4,6,7 uses a "pump in ring" mechanism to unwind DNA by steric exclusion and actively translocate along a duplex. J. Biol. Chem. 278 (2003) 49171-49182
    • (2003) J. Biol. Chem. , vol.278 , pp. 49171-49182
    • Kaplan, D.L.1
  • 67
    • 0034595448 scopus 로고    scopus 로고
    • Uninterrupted MCM2-7 function required for DNA replication fork progression
    • Labib K., et al. Uninterrupted MCM2-7 function required for DNA replication fork progression. Science 288 (2000) 1643-1647
    • (2000) Science , vol.288 , pp. 1643-1647
    • Labib, K.1
  • 68
    • 0035930346 scopus 로고    scopus 로고
    • Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication
    • Schwacha A., and Bell S.P. Interactions between two catalytically distinct MCM subgroups are essential for coordinated ATP hydrolysis and DNA replication. Mol. Cell 8 (2001) 1093-1104
    • (2001) Mol. Cell , vol.8 , pp. 1093-1104
    • Schwacha, A.1    Bell, S.P.2
  • 69
    • 0030070111 scopus 로고    scopus 로고
    • A molecular switch in a replication machine defined by an internal competition for protein rings
    • Naktinis V., et al. A molecular switch in a replication machine defined by an internal competition for protein rings. Cell 84 (1996) 137-145
    • (1996) Cell , vol.84 , pp. 137-145
    • Naktinis, V.1
  • 70
    • 0023646086 scopus 로고
    • Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli
    • O'Donnell M.E. Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli. J. Biol. Chem. 262 (1987) 16558-16565
    • (1987) J. Biol. Chem. , vol.262 , pp. 16558-16565
    • O'Donnell, M.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.