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0032969563
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AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
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Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9:1999;27-43.
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Neuwald, A.F.1
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0001607723
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Distantly related sequences in the alpha- And beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
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A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
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Koonin E.V. A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication. Nucleic Acids Res. 21:1993;2541-2547.
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Components and dynamics of DNA replication complexes in S. cerevisiae: Redistribution of MCM proteins and Cdc45p during S phase
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Aparicio O.M., Weinstein D.M., Bell S.P. Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase. Cell. 91:1997;59-69.
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Aparicio, O.M.1
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Bell, S.P.3
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Loading of an Mcm protein onto DNA replication origins is regulated by Cdc6p and CDKs
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Tanaka T., Knapp D., Nasmyth K. Loading of an Mcm protein onto DNA replication origins is regulated by Cdc6p and CDKs. Cell. 90:1997;649-660.
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Tanaka, T.1
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9
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0033499708
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Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity
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This paper characterizes the intrinsic helicase of the mouse MCM4-MCM6-MCM7 complex. The authors demonstrate that mutations in the MCM ATP-binding motif result in a loss of DNA helicase activity.
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You Z., Komamura Y., Ishimi Y. Biochemical analysis of the intrinsic Mcm4-Mcm6-mcm7 DNA helicase activity. Mol Cell Biol. 19:1999;8003-8015. This paper characterizes the intrinsic helicase of the mouse MCM4-MCM6-MCM7 complex. The authors demonstrate that mutations in the MCM ATP-binding motif result in a loss of DNA helicase activity.
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Mol Cell Biol
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You, Z.1
Komamura, Y.2
Ishimi, Y.3
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10
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0033593053
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The single minichromosome maintenance protein of methanobacterium thermoautotrophicum Delta H contains DNAhelicase activity
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See annotation [11••].
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Kelman Z., Lee J.K., Hurwitz J. The single minichromosome maintenance protein of methanobacterium thermoautotrophicum Delta H contains DNAhelicase activity. Proc Natl Acad Sci USA. 96:1999;14783-14788. See annotation [11••].
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Proc Natl Acad Sci USA
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Kelman, Z.1
Lee, J.K.2
Hurwitz, J.3
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11
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0034652354
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A double-hexamer archael minichromosome mainrenance protein is an ATP-dependent helicase
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These papers [10••,11••] describe biochemical studies of an MCM-related protein derived from the thermophilic archaeon Methanobacterium thermoautotrophicum. Unlike eukaryotic cells, the archaeon have only a single MCM-related protein that form double hexamers in solution as seen by gel filtration and electron microscopy studies. More impotantly, this assembly is shown to act as a robust 3′ to 5′ DNA helicase with significant processivity. The similarity of this archaeon MCM protein to the eukaryotic MCM proteins strongly suggests the eukaryotic proteins will also as a DNAhelicase.
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Chong J.P., Hayashi M.K., Simon M.N., Xu R.M., Stillamn B. A double-hexamer archael minichromosome mainrenance protein is an ATP-dependent helicase. Proc Natl Acad Sci USA. 97:2000;1530-1535. These papers [10••,11••] describe biochemical studies of an MCM-related protein derived from the thermophilic archaeon Methanobacterium thermoautotrophicum. Unlike eukaryotic cells, the archaeon have only a single MCM-related protein that form double hexamers in solution as seen by gel filtration and electron microscopy studies. More impotantly, this assembly is shown to act as a robust 3′ to 5′ DNA helicase with significant processivity. The similarity of this archaeon MCM protein to the eukaryotic MCM proteins strongly suggests the eukaryotic proteins will also as a DNAhelicase.
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(2000)
Proc Natl Acad Sci USA
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, pp. 1530-1535
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Chong, J.P.1
Hayashi, M.K.2
Simon, M.N.3
Xu, R.M.4
Stillamn, B.5
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12
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0033529791
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Regulation of Cdc45p association with replication origins controls the timing of DNA polymerase loading and origin activation
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See annotation [13••].
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Aparicio O.M., Sout A.M., Bell S.P. Regulation of Cdc45p association with replication origins controls the timing of DNA polymerase loading and origin activation. Proc Natl Acad Sci USA. 96:1999;9130-9135. See annotation [13••].
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Proc Natl Acad Sci USA
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Aparicio, O.M.1
Sout, A.M.2
Bell, S.P.3
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13
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0032562610
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Formation of a preinitiation complex by S-phase cyclin CDK-dependent loading of Cdc45p onto chromatin
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??] demonstrates that the timing of Cdc45p assembly is regulated according to the time of initiation. It also shows that Cdc45p can be detected at certain origins prior to entry into S phase.
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??] demonstrates that the timing of Cdc45p assembly is regulated according to the time of initiation. It also shows that Cdc45p can be detected at certain origins prior to entry into S phase.
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(1998)
Science
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Zou, L.1
Stillman, B.2
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14
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0033583219
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The essential role of Saccharomyces cerevisiae CDC6 nucleotide-binding site in cell growth, DNA synthesis, and Orc1 association
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Wang B., Feng L., Hu Y., Huang S.H., Reynolds C.P., Wu L., Jong A.Y. The essential role of Saccharomyces cerevisiae CDC6 nucleotide-binding site in cell growth, DNA synthesis, and Orc1 association. J Biol Chem. 274:1999;8291-8298.
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Wang, B.1
Feng, L.2
Hu, Y.3
Huang, S.H.4
Reynolds, C.P.5
Wu, L.6
Jong, A.Y.7
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15
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0033582262
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The Cdc6p nucleotide-binding motif is required for loading mcm proteins onto chromatin
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See annotation [16••].
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Weinreich M., Liang C., Stillman B. The Cdc6p nucleotide-binding motif is required for loading mcm proteins onto chromatin. Proc Natl Acad Sci USA. 96:1999;441-446. See annotation [16••].
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Proc Natl Acad Sci USA
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, pp. 441-446
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Weinreich, M.1
Liang, C.2
Stillman, B.3
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16
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0032110626
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Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders
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These two manuscripts [15••,16••] describe the analysis of a series of Cdc6 (ScCdc6) mutants in S. cerevisiae. Both papers show that mutations in the Cdc6p ATP-binding motifs result in defects in replication complex assembly. In addition, Perkins and Diffley [16••] describes a CDC6 allele that is lethal when overexpressed.
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Perkins G., Diffley J.F. Nucleotide-dependent prereplicative complex assembly by Cdc6p, a homolog of eukaryotic and prokaryotic clamp-loaders. Mol Cell. 2:1998;23-32. These two manuscripts [15••,16••] describe the analysis of a series of Cdc6 (ScCdc6) mutants in S. cerevisiae. Both papers show that mutations in the Cdc6p ATP-binding motifs result in defects in replication complex assembly. In addition, Perkins and Diffley [16••] describes a CDC6 allele that is lethal when overexpressed.
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(1998)
Mol Cell
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, pp. 23-32
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Perkins, G.1
Diffley, J.F.2
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17
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0032807099
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The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells
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This manuscript describes a biochemical analysis of the human Cdc6p (HsCdc6p). The authors demonstrate that HsCdc6p is an active ATPase and that mutations in the A- and P-loop have different effects on ATP binding and ATP hydrolysis. Microinjection of mutant, but not wild-type HsCdc6p, results in inhibition of DNA replication.
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Herbig U., Marlar C.A., Fanning E. The Cdc6 nucleotide-binding site regulates its activity in DNA replication in human cells. Mol Biol Cell. 10:1999;2631-2645. This manuscript describes a biochemical analysis of the human Cdc6p (HsCdc6p). The authors demonstrate that HsCdc6p is an active ATPase and that mutations in the A- and P-loop have different effects on ATP binding and ATP hydrolysis. Microinjection of mutant, but not wild-type HsCdc6p, results in inhibition of DNA replication.
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(1999)
Mol Biol Cell
, vol.10
, pp. 2631-2645
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Herbig, U.1
Marlar, C.A.2
Fanning, E.3
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0031002795
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Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex
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Klemm R.D., Austin R.J., Bell S.P. Coordinate binding of ATP and origin DNA regulates the ATPase activity of the origin recognition complex. Cell. 88:1997;493-502.
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Klemm, R.D.1
Austin, R.J.2
Bell, S.P.3
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20
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Negative control of DNA replication by hydrolysis of ATP bound to DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli
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Mizushima T., Nishida S., Kurokawa K., Katayama T., Miki T., Sekimizu K. Negative control of DNA replication by hydrolysis of ATP bound to DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli. EMBO J. 16:1997;3724-3730.
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Mizushima, T.1
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Miki, T.5
Sekimizu, K.6
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21
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0032516840
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Site-directed mutational analysis for the ATP binding of DnaA protein. Functions of two conserved amino acids (Lys-178 and Asp-235) located in the ATP-binding domain of DnaA protein in vitro and in vivo
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Mizushima T., Takaki T., Kubota T., Tsuchiya T., Miki T., Katayama T., Sekimizu K. Site-directed mutational analysis for the ATP binding of DnaA protein. Functions of two conserved amino acids (Lys-178 and Asp-235) located in the ATP-binding domain of DnaA protein in vitro and in vivo. J Biol Chem. 273:1998;20847-20851.
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Mizushima, T.1
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Tsuchiya, T.4
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Katayama, T.6
Sekimizu, K.7
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0023658349
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ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
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Sekimizu K., Bramhill D., Kornberg A. ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell. 50:1987;259-265.
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Duplex opening by DnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
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Bramhill D., Kornberg A. Duplex opening by DnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell. 52:1988;743-755.
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24
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0032504050
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The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase
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See annotation [25••].
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Katayama T., Kubota T., Kurokawa K., Crooke E., Sekimizu K. The initiator function of DnaA protein is negatively regulated by the sliding clamp of the E. coli chromosomal replicase. Cell. 94:1998;61-71. See annotation [25••].
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Katayama, T.1
Kubota, T.2
Kurokawa, K.3
Crooke, E.4
Sekimizu, K.5
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25
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0033485526
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Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli
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These two papers [24••,25••] investigate the control of the dnaA ATPase by replication proteins and cell cycle position. The authors provide both in vitro and in vivo evidence that the nucleotide-bound state of dnaA is critical for regulating DNA replication in E. coli.
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Kurokawa K., Nishida S., Emoto A., Sekimizu K., Katayama T. Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli. EMBO J. 18:1999;6642-6652. These two papers [24••,25••] investigate the control of the dnaA ATPase by replication proteins and cell cycle position. The authors provide both in vitro and in vivo evidence that the nucleotide-bound state of dnaA is critical for regulating DNA replication in E. coli.
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EMBO J
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Kurokawa, K.1
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Katayama, T.5
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26
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Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products
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The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
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28
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0031019643
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Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA
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Learn B.A., Um S.J., Huang L., McMacken R. Cryptic single-stranded-DNA binding activities of the phage lambda P and Escherichia coli DnaC replication initiation proteins facilitate the transfer of E. coli DnaB helicase onto DNA. Proc Natl Acad Sci USA. 94:1997;1154-1159.
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The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions
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The internal workings of a DNA polymerase clamp-loading machine
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This manuscript describes a detailed analysis of the role of ATP and DNA in the control of sliding clamp assembly by the E. coli γ-complex. Interestingly, the authors find that ATP hydolysis is not required to open the sliding clamp but rather to allow the release of the sliding clamp from the γ-complex.
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Turner J., Hingorani M.M., Kelman Z., O'Donnell M. The internal workings of a DNA polymerase clamp-loading machine. EMBO J. 18:1999;771-783. This manuscript describes a detailed analysis of the role of ATP and DNA in the control of sliding clamp assembly by the E. coli γ-complex. Interestingly, the authors find that ATP hydolysis is not required to open the sliding clamp but rather to allow the release of the sliding clamp from the γ-complex.
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