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Volumn 44, Issue 1, 2016, Pages 210-220

DnaC traps DnaB as an open ring and remodels the domain that binds primase

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; DNAB HELICASE; DNAC PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA PRIMASE; PEPTIDE; PROTEIN BINDING;

EID: 84959560869     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv961     Document Type: Article
Times cited : (29)

References (67)
  • 2
    • 0026709650 scopus 로고
    • Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. V. Primase action regulates the cycle of Okazaki fragment synthesis
    • Wu,C.A., Zechner,E.L., Reems,J.A., McHenry,C.S. and Marians,K.J. (1992) Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. V. Primase action regulates the cycle of Okazaki fragment synthesis. J. Biol. Chem., 267, 4074-4083.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4074-4083
    • Wu, C.A.1    Zechner, E.L.2    Reems, J.A.3    McHenry, C.S.4    Marians, K.J.5
  • 3
    • 0029788209 scopus 로고    scopus 로고
    • The interaction between helicase and primase sets the replication fork clock
    • Tougu,K. and Marians,K.J. (1996) The interaction between helicase and primase sets the replication fork clock. J. Biol. Chem., 271, 21398-21405.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21398-21405
    • Tougu, K.1    Marians, K.J.2
  • 4
    • 33749119130 scopus 로고    scopus 로고
    • Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions
    • Corn,J.E. and Berger,J.M. (2006) Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions. Nucleic Acids Res., 34, 4082-4088.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4082-4088
    • Corn, J.E.1    Berger, J.M.2
  • 5
    • 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
  • 6
    • 73649145533 scopus 로고    scopus 로고
    • Primase directs the release of DnaC from DnaB
    • Makowska-Grzyska,M. and Kaguni,J.M. (2010) Primase directs the release of DnaC from DnaB. Mol. Cell, 37, 90-101.
    • (2010) Mol. Cell , vol.37 , pp. 90-101
    • Makowska-Grzyska, M.1    Kaguni, J.M.2
  • 8
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey,S., Eliason,W.K. and Steitz,T.A. (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science, 318, 459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 10
    • 63349092249 scopus 로고    scopus 로고
    • The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA
    • Lo,Y.H., Tsai,K.L., Sun,Y.J., Chen,W.T., Huang,C.Y. and Hsiao,C.D. (2009) The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res., 37, 804-814.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 804-814
    • Lo, Y.H.1    Tsai, K.L.2    Sun, Y.J.3    Chen, W.T.4    Huang, C.Y.5    Hsiao, C.D.6
  • 12
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn,O., Wing,R.A., Eliason,W.K., Wang,J. and Steitz,T.A. (2012) The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell, 151, 267-277.
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 13
    • 84890724459 scopus 로고    scopus 로고
    • Loading strategies of ring-shaped nucleic acid translocases and helicases
    • O'Shea,V.L. and Berger,J.M. (2014) Loading strategies of ring-shaped nucleic acid translocases and helicases. Curr. Opin. Struct. Biol., 25, 16-24.
    • (2014) Curr. Opin. Struct. Biol. , vol.25 , pp. 16-24
    • O'Shea, V.L.1    Berger, J.M.2
  • 14
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies
    • Jezewska,M.J., Rajendran,S., Bujalowska,D. and Bujalowski,W. (1998) Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies. J. Biol. Chem., 273, 10515-10529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 15
    • 0019400815 scopus 로고
    • Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA
    • Arai,K. and Kornberg,A. (1981) Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA. J. Biol. Chem., 256, 5253-5259.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5253-5259
    • Arai, K.1    Kornberg, A.2
  • 16
    • 0022829375 scopus 로고
    • The dnaB protein of Escherichia coli: Mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein
    • Biswas,E.E., Biswas,S.B. and Bishop,J.E. (1986) The dnaB protein of Escherichia coli: mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein. Biochemistry, 25, 7368-7374.
    • (1986) Biochemistry , vol.25 , pp. 7368-7374
    • Biswas, E.E.1    Biswas, S.B.2    Bishop, J.E.3
  • 17
    • 0034634365 scopus 로고    scopus 로고
    • Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: Quantitative analysis using the rapid quench-flow method
    • Rajendran,S., Jezewska,M.J. and Bujalowski,W. (2000) Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: quantitative analysis using the rapid quench-flow method. J. Mol. Biol., 303, 773-795.
    • (2000) J. Mol. Biol. , vol.303 , pp. 773-795
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 18
    • 80053575452 scopus 로고    scopus 로고
    • Dynamic coupling between the motors of DNA replication: Hexameric helicase, DNA polymerase, and primase
    • Patel,S.S., Pandey,M. and Nandakumar,D. (2011) Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase. Curr. Opin. Chem. Biol., 15, 595-605.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 595-605
    • Patel, S.S.1    Pandey, M.2    Nandakumar, D.3
  • 19
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya,M.R., Guo,S., Tabor,S., Richardson,C.C. and Ellenberger,T. (1999) Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell, 99, 167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 20
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton,M.R., Sawaya,M.R., Ellenberger,T. and Wigley,D.B. (2000) Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell, 101, 589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 21
  • 22
    • 34547886124 scopus 로고    scopus 로고
    • The crystal structure of the Thermus aquaticus DnaB helicase monomer
    • Bailey,S., Eliason,W.K. and Steitz,T.A. (2007) The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res., 35, 4728-4736.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4728-4736
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 23
    • 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
  • 24
    • 0024520416 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions
    • Wahle,E., Lasken,R.S. and Kornberg,A. (1989) The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions. J. Biol. Chem., 264, 2469-2475.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 25
    • 0024562458 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
    • Wahle,E., Lasken,R.S. and Kornberg,A. (1989) The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties. J. Biol. Chem., 264, 2463-2468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2463-2468
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 26
    • 0034711089 scopus 로고    scopus 로고
    • Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein
    • Galletto,R., Rajendran,S. and Bujalowski,W. (2000) Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein. Biochemistry, 39, 12959-12969.
    • (2000) Biochemistry , vol.39 , pp. 12959-12969
    • Galletto, R.1    Rajendran, S.2    Bujalowski, W.3
  • 28
    • 55649098814 scopus 로고    scopus 로고
    • Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators
    • Mott,M.L., Erzberger,J.P., Coons,M.M. and Berger,J.M. (2008) Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators. Cell, 135, 623-634.
    • (2008) Cell , vol.135 , pp. 623-634
    • Mott, M.L.1    Erzberger, J.P.2    Coons, M.M.3    Berger, J.M.4
  • 29
    • 2542535234 scopus 로고    scopus 로고
    • Quantitative analysis of nucleotide modulation of DNA binding by the DnaC protein of Escherichia coli
    • Biswas,S.B., Flowers,S. and Biswas-Fiss,E.E. (2004) Quantitative analysis of nucleotide modulation of DNA binding by the DnaC protein of Escherichia coli. Biochem. J., 379, 553-562.
    • (2004) Biochem. J. , vol.379 , pp. 553-562
    • Biswas, S.B.1    Flowers, S.2    Biswas-Fiss, E.E.3
  • 30
    • 0038637844 scopus 로고    scopus 로고
    • A two-protein strategy for the functional loading of a cellular replicative DNA helicase
    • Velten,M., McGovern,S., Marsin,S., Ehrlich,S.D., Noirot,P. and Polard,P. (2003) A two-protein strategy for the functional loading of a cellular replicative DNA helicase. Mol. Cell, 11, 1009-1020.
    • (2003) Mol. Cell , vol.11 , pp. 1009-1020
    • Velten, M.1    McGovern, S.2    Marsin, S.3    Ehrlich, S.D.4    Noirot, P.5    Polard, P.6
  • 31
    • 84884627894 scopus 로고    scopus 로고
    • Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly
    • Liu,B., Eliason,W.K. and Steitz,T.A. (2013) Structure of a helicase-helicase loader complex reveals insights into the mechanism of bacterial primosome assembly. Nat. Commun., 4, doi:10.1038/ncomms3495.
    • (2013) Nat. Commun. , vol.4
    • Liu, B.1    Eliason, W.K.2    Steitz, T.A.3
  • 32
    • 84876286140 scopus 로고    scopus 로고
    • The bacterial DnaC helicase loader is a DnaB ring breaker
    • Arias-Palomo,E., O'Shea,V.L., Hood,I.V. and Berger,J.M. (2013) The bacterial DnaC helicase loader is a DnaB ring breaker. Cell, 153, 438-448.
    • (2013) Cell , vol.153 , pp. 438-448
    • Arias-Palomo, E.1    O'Shea, V.L.2    Hood, I.V.3    Berger, J.M.4
  • 33
    • 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
  • 34
    • 0023732715 scopus 로고
    • Interaction of dnaA46 protein with a stimulatory protein in replication from the Escherichia coli chromosomal origin
    • Hwang,D.S. and Kaguni,J.M. (1988) Interaction of dnaA46 protein with a stimulatory protein in replication from the Escherichia coli chromosomal origin. J. Biol. Chem., 263, 10633-10640.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10633-10640
    • Hwang, D.S.1    Kaguni, J.M.2
  • 35
    • 0019490027 scopus 로고
    • Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication
    • Arai,K. and Kornberg,A. (1981) Mechanism of dnaB protein action. III. Allosteric role of ATP in the alteration of DNA structure by dnaB protein in priming replication. J. Biol. Chem., 256, 5260-5266.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5260-5266
    • Arai, K.1    Kornberg, A.2
  • 36
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: Optimization of digestion conditions
    • Wang,L., Pan,H. and Smith,D.L. (2002) Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol. Cell Proteomics, 1, 132-138.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 37
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis,D.D., Engen,J.R. and Kass,I.J. (2006) Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom., 17, 1700-1703.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3
  • 38
    • 33749326831 scopus 로고    scopus 로고
    • Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis
    • Weis,D.D., Wales,T.E., Engen,J.R., Hotchko,M. and Ten Eyck,L.F. (2006) Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom., 17, 1498-1509.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1498-1509
    • Weis, D.D.1    Wales, T.E.2    Engen, J.R.3    Hotchko, M.4    Ten Eyck, L.F.5
  • 39
    • 84868575176 scopus 로고    scopus 로고
    • Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment
    • Walters,B.T., Ricciuti,A., Mayne,L. and Englander,S.W. (2012) Minimizing back exchange in the hydrogen exchange-mass spectrometry experiment. J. Am. Soc. Mass Spectrom., 23, 2132-2139.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 2132-2139
    • Walters, B.T.1    Ricciuti, A.2    Mayne, L.3    Englander, S.W.4
  • 40
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales,T.E. and Engen,J.R. (2006) Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev., 25, 158-170.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 41
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: Implications for structure rearrangements in the helicase hexamer
    • Weigelt,J., Brown,S.E., Miles,C.S., Dixon,N.E. and Otting,G. (1999) NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure, 7, 681-690.
    • (1999) Structure , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 43
    • 0033152872 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the DnaB hexameric helicase
    • Fass,D., Bogden,C.E. and Berger,J.M. (1999) Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure, 7, 691-698.
    • (1999) Structure , vol.7 , pp. 691-698
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 44
    • 0028068822 scopus 로고
    • Structure and function of Escherichia coli DnaB protein: Role of the N- terminal domain in helicase activity
    • Biswas,S.B., Chen,P.H. and Biswas,E.E. (1994) Structure and function of Escherichia coli DnaB protein: role of the N- terminal domain in helicase activity. Biochemistry, 33, 11307-11314.
    • (1994) Biochemistry , vol.33 , pp. 11307-11314
    • Biswas, S.B.1    Chen, P.H.2    Biswas, E.E.3
  • 45
    • 0029772574 scopus 로고    scopus 로고
    • Defect in general priming conferred by linker region mutants of Escherichia coli dnaB
    • Stordal,L. and Maurer,R. (1996) Defect in general priming conferred by linker region mutants of Escherichia coli dnaB. J. Bacteriol., 178, 4620-4627.
    • (1996) J. Bacteriol. , vol.178 , pp. 4620-4627
    • Stordal, L.1    Maurer, R.2
  • 46
    • 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., 32, 2977-2986.
    • (2004) Nucleic Acids Res. , vol.32 , 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
  • 47
    • 20444463552 scopus 로고    scopus 로고
    • Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states
    • Lisal,J., Lam,T.T., Kainov,D.E., Emmett,M.R., Marshall,A.G. and Tuma,R. (2005) Functional visualization of viral molecular motor by hydrogen-deuterium exchange reveals transient states. Nat. Struct. Mol. Biol., 12, 460-466.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 460-466
    • Lisal, J.1    Lam, T.T.2    Kainov, D.E.3    Emmett, M.R.4    Marshall, A.G.5    Tuma, R.6
  • 48
    • 4644257077 scopus 로고    scopus 로고
    • Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors
    • Galletto,R., Maillard,R., Jezewska,M.J. and Bujalowski,W. (2004) Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors. Biochemistry, 43, 10988-11001.
    • (2004) Biochemistry , vol.43 , pp. 10988-11001
    • Galletto, R.1    Maillard, R.2    Jezewska, M.J.3    Bujalowski, W.4
  • 49
    • 0020355756 scopus 로고
    • The Escherichia coli dnaC gene product. II. Purification, physical properties, and role in replication
    • Kobori,J.A. and Kornberg,A. (1982) The Escherichia coli dnaC gene product. II. Purification, physical properties, and role in replication. J. Biol. Chem., 257, 13763-13769.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13763-13769
    • Kobori, J.A.1    Kornberg, A.2
  • 50
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones,D.T. (1999) Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol., 292, 195-202.
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 51
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali,A. and Blundell,T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol., 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 52
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser,A., Do,R.K. and Sali,A. (2000) Modeling of loops in protein structures. Protein Sci., 9, 1753-1773.
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 53
    • 70350022740 scopus 로고    scopus 로고
    • Molecular interplay between the replicative helicase DnaC and its loader protein DnaI from Geobacillus kaustophilus
    • Tsai,K.L., Lo,Y.H., Sun,Y.J. and Hsiao,C.D. (2009) Molecular interplay between the replicative helicase DnaC and its loader protein DnaI from Geobacillus kaustophilus. J. Mol. Biol., 393, 1056-1069.
    • (2009) J. Mol. Biol. , vol.393 , pp. 1056-1069
    • Tsai, K.L.1    Lo, Y.H.2    Sun, Y.J.3    Hsiao, C.D.4
  • 54
    • 33746860263 scopus 로고    scopus 로고
    • Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling
    • Erzberger,J.P., Mott,M.L. and Berger,J.M. (2006) Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling. Nat. Struct. Mol. Biol., 13, 676-683.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 676-683
    • Erzberger, J.P.1    Mott, M.L.2    Berger, J.M.3
  • 55
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura,T. and Wilkinson,A.J. (2001) AAA+ superfamily ATPases: common structure-diverse function. Genes Cells, 6, 575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 56
    • 1642377971 scopus 로고    scopus 로고
    • Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases
    • Ogura,T., Whiteheart,S.W. and Wilkinson,A.J. (2004) Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases. J. Struct. Biol., 146, 106-112.
    • (2004) J. Struct. Biol. , vol.146 , pp. 106-112
    • Ogura, T.1    Whiteheart, S.W.2    Wilkinson, A.J.3
  • 57
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther,B., Onrust,R., Sali,A., O'Donnell,M. and Kuriyan,J. (1997) Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell, 91, 335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 58
    • 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., Aravind,L., Spouge,J.L. and Koonin,E.V. (1999) AAA+: A class of chaperone-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
  • 59
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer,L.M., Leipe,D.D., Koonin,E.V. and Aravind,L. (2004) Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol., 146, 11-31.
    • (2004) J. Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 60
    • 80054029342 scopus 로고    scopus 로고
    • DNA stretching by bacterial initiators promotes replication origin opening
    • Duderstadt,K.E., Chuang,K. and Berger,J.M. (2011) DNA stretching by bacterial initiators promotes replication origin opening. Nature, 478, 209-213.
    • (2011) Nature , vol.478 , pp. 209-213
    • Duderstadt, K.E.1    Chuang, K.2    Berger, J.M.3
  • 62
    • 4944231970 scopus 로고    scopus 로고
    • On the solution structure of the T4 sliding clamp (gp45)
    • Millar,D., Trakselis,M.A. and Benkovic,S.J. (2004) On the solution structure of the T4 sliding clamp (gp45). Biochemistry, 43, 12723-12727.
    • (2004) Biochemistry , vol.43 , pp. 12723-12727
    • Millar, D.1    Trakselis, M.A.2    Benkovic, S.J.3
  • 63
    • 79959799630 scopus 로고    scopus 로고
    • Escherichia coli processivity clamp beta from DNA polymerase III is dynamic in solution
    • Fang,J., Engen,J.R. and Beuning,P.J. (2011) Escherichia coli processivity clamp beta from DNA polymerase III is dynamic in solution. Biochemistry, 50, 5958-5968.
    • (2011) Biochemistry , vol.50 , pp. 5958-5968
    • Fang, J.1    Engen, J.R.2    Beuning, P.J.3
  • 64
    • 33745586075 scopus 로고    scopus 로고
    • An alternative clamp loading pathway via the T4 clamp loader gp44/62-DNA complex
    • Zhuang,Z., Berdis,A.J. and Benkovic,S.J. (2006) An alternative clamp loading pathway via the T4 clamp loader gp44/62-DNA complex. Biochemistry, 45, 7976-7989.
    • (2006) Biochemistry , vol.45 , pp. 7976-7989
    • Zhuang, Z.1    Berdis, A.J.2    Benkovic, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.