메뉴 건너뛰기




Volumn 21, Issue 18, 2002, Pages 4763-4773

The structure of bacterial DnaA: Implications for general mechanisms underlying DNA replication initiation

Author keywords

Bacteria; DNA replication initiation; DnaA; Structure

Indexed keywords

BACTERIAL DNA; NUCLEOTIDE BINDING PROTEIN;

EID: 0037119995     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf496     Document Type: Article
Times cited : (200)

References (74)
  • 2
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton,G.J. (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng., 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 3
    • 0028949675 scopus 로고
    • Eukaryotic replicators and associated protein complexes
    • Bell,S.P. (1995) Eukaryotic replicators and associated protein complexes. Curr. Opin. Genet. Dev., 5, 162-167.
    • (1995) Curr. Opin. Genet. Dev. , vol.5 , pp. 162-167
    • Bell, S.P.1
  • 4
    • 0037087587 scopus 로고    scopus 로고
    • The origin recognition complex: From simple origins to complex functions
    • Bell,S.P. (2002) The origin recognition complex: from simple origins to complex functions. Genes Dev., 16, 659-672.
    • (2002) Genes Dev. , vol.16 , pp. 659-672
    • Bell, S.P.1
  • 5
    • 0026607331 scopus 로고
    • ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex
    • Bell,S.P. and Stillman,B. (1992) ATP-dependent recognition of eukaryotic origins of DNA replication by a multiprotein complex. Nature, 357, 128-134.
    • (1992) Nature , vol.357 , pp. 128-134
    • Bell, S.P.1    Stillman, B.2
  • 6
    • 0028832366 scopus 로고
    • The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing
    • Bell,S.P., Mitchell,J., Leber,J., Kobayashi,R. and Stillman,B. (1995) The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing. Cell, 83, 563-568.
    • (1995) Cell , vol.83 , pp. 563-568
    • Bell, S.P.1    Mitchell, J.2    Leber, J.3    Kobayashi, R.4    Stillman, B.5
  • 7
    • 0028092214 scopus 로고
    • Amino acid substitution during functionally constrained divergent evolution of protein sequences
    • Benner,S.A., Cohen,M.A. and Gonnet,G.H. (1994) Amino acid substitution during functionally constrained divergent evolution of protein sequences. Protein Eng., 7, 1323-1332.
    • (1994) Protein Eng. , vol.7 , pp. 1323-1332
    • Benner, S.A.1    Cohen, M.A.2    Gonnet, G.H.3
  • 8
    • 0034212268 scopus 로고    scopus 로고
    • Chromosome replication, nucleoid segregation and cell division in archaea
    • Bernander,R. (2000) Chromosome replication, nucleoid segregation and cell division in archaea. Trends Microbiol., 8, 278-283.
    • (2000) Trends Microbiol. , vol.8 , pp. 278-283
    • Bernander, R.1
  • 9
    • 0034016324 scopus 로고    scopus 로고
    • Analysis of the DNA-binding domain of Escherichia coli DnaA protein
    • Blaesing,F., Weigel,C., Welzeck,M. and Messer,W. (2000) Analysis of the DNA-binding domain of Escherichia coli DnaA protein. Mol. Microbiol., 36, 557-569.
    • (2000) Mol. Microbiol. , vol.36 , pp. 557-569
    • Blaesing, F.1    Weigel, C.2    Welzeck, M.3    Messer, W.4
  • 10
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev,A., Pfuetzner,R.A., Edwards,A.M. and Frappier,L. (1997) Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature, 385, 176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 12
    • 0023408580 scopus 로고
    • Cloning and characterization of dnaA(Cs), a mutation which leads to over-initiation of DNA replication in Escherichia coli K-12
    • Braun,R.E., O'Day,K. and Wright,A. (1987) Cloning and characterization of dnaA(Cs), a mutation which leads to over-initiation of DNA replication in Escherichia coli K-12. J. Bacteriol., 169, 3898-3903.
    • (1987) J. Bacteriol. , vol.169 , pp. 3898-3903
    • Braun, R.E.1    O'Day, K.2    Wright, A.3
  • 13
    • 0029901503 scopus 로고    scopus 로고
    • The A184V missense mutation of the dnaA5 and dnaA46 alleles confers a defect in ATP binding and thermolability in initiation of Escherichia coli DNA replication
    • Carr,K.M. and Kaguni,J.M. (1996) The A184V missense mutation of the dnaA5 and dnaA46 alleles confers a defect in ATP binding and thermolability in initiation of Escherichia coli DNA replication. Mol. Microbiol., 20, 1307-1318.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1307-1318
    • Carr, K.M.1    Kaguni, J.M.2
  • 14
    • 0035977018 scopus 로고    scopus 로고
    • Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin
    • Carr,K.M. and Kaguni,J.M. (2001) Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin. J. Biol. Chem., 276, 44919-44925.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44919-44925
    • Carr, K.M.1    Kaguni, J.M.2
  • 16
    • 0002583957 scopus 로고
    • 'DM': An automated procedure for phase improvement by density modification
    • Cowtan,K. (1994) 'DM': an automated procedure for phase improvement by density modification. Joint CCP4 ESF-EACBM Newslett. Protein Crystallogr., 31, 34-38.
    • (1994) Joint CCP4 ESF-EACBM Newslett. Protein Crystallogr. , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 17
    • 0035111557 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein-phospholipid interactions: In vitro and in vivo
    • Crooke,E. (2001) Escherichia coli DnaA protein-phospholipid interactions: in vitro and in vivo. Biochimie, 83, 19-23.
    • (2001) Biochimie , vol.83 , pp. 19-23
    • Crooke, E.1
  • 18
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavyatom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle,E. and Bricogne,G. (1997) Maximum-likelihood heavyatom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 19
    • 0031587829 scopus 로고    scopus 로고
    • Archaea and the origin(s) of DNA replication initiation
    • Edgell,D.R. and Doolittle,W.F. (1997) Archaea and the origin(s) of DNA replication initiation. Cell, 87, 995-998.
    • (1997) Cell , vol.87 , pp. 995-998
    • Edgell, D.R.1    Doolittle, W.F.2
  • 20
    • 0033213720 scopus 로고    scopus 로고
    • Replisome assembly at oriC, the replication origin of E.coli, reveals an explanation for initiation sites outside an origin
    • Fang,L., Davey,M.J. and O'Donnell,M. (1999) Replisome assembly at oriC, the replication origin of E.coli, reveals an explanation for initiation sites outside an origin. Mol. Cell, 4, 541-553.
    • (1999) Mol. Cell , vol.4 , pp. 541-553
    • Fang, L.1    Davey, M.J.2    O'Donnell, M.3
  • 21
    • 0023664708 scopus 로고
    • In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome
    • Funnell,B.E., Baker,T.A. and Kornberg,A. (1987) In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. J. Biol. Chem., 262, 10327-10334.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10327-10334
    • Funnell, B.E.1    Baker, T.A.2    Kornberg, A.3
  • 22
    • 0032570678 scopus 로고    scopus 로고
    • Membrane-mediated release of nucleotide from an initiator of chromosomal replication, Escherichia coli DnaA, occurs with insertion of a distinct region of the protein into the lipid bilayer
    • Garner,J., Durrer,P., Kitchen,J., Brunner,J. and Crooke,E. (1998) Membrane-mediated release of nucleotide from an initiator of chromosomal replication, Escherichia coli DnaA, occurs with insertion of a distinct region of the protein into the lipid bilayer. J. Biol. Chem., 273, 5167-5173.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5167-5173
    • Garner, J.1    Durrer, P.2    Kitchen, J.3    Brunner, J.4    Crooke, E.5
  • 23
    • 0028932026 scopus 로고
    • Mutations in Escherichia coli dnaA which suppress a dnaX(Ts) polymerization mutation and are dominant when located in the chromosomal allele and recessive on plasmids
    • Gines-Candelaria,E., Blinkova,A. and Walker,J.R. (1995) Mutations in Escherichia coli dnaA which suppress a dnaX(Ts) polymerization mutation and are dominant when located in the chromosomal allele and recessive on plasmids. J. Bacteriol., 177, 705-715.
    • (1995) J. Bacteriol. , vol.177 , pp. 705-715
    • Gines-Candelaria, E.1    Blinkova, A.2    Walker, J.R.3
  • 24
    • 0033975575 scopus 로고    scopus 로고
    • IHF redistributes bound initiator protein, DnaA, on supercoiled oriC of Escherichia coli
    • Grimwade,J.E., Ryan,V.T. and Leonard,A.C. (2000) IHF redistributes bound initiator protein, DnaA, on supercoiled oriC of Escherichia coli. Mol. Microbiol., 35, 835-844.
    • (2000) Mol. Microbiol. , vol.35 , pp. 835-844
    • Grimwade, J.E.1    Ryan, V.T.2    Leonard, A.C.3
  • 25
    • 0026749793 scopus 로고
    • Cloning and nucleotide sequence determination of twelve mutant dnaA genes of Escherichia coli
    • Hansen,F.G., Koefoed,S. and Atlung,T. (1992) Cloning and nucleotide sequence determination of twelve mutant dnaA genes of Escherichia coli. Mol. Gen. Genet., 234, 14-21.
    • (1992) Mol. Gen. Genet. , vol.234 , pp. 14-21
    • Hansen, F.G.1    Koefoed, S.2    Atlung, T.3
  • 26
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm,L.L. and Sander,C. (1996) Mapping the protein universe. Science, 273, 595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.L.1    Sander, C.2
  • 27
    • 0026463867 scopus 로고
    • Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF
    • Hwang,D.S. and Kornberg,A. (1992) Opening of the replication origin of Escherichia coli by DnaA protein with protein HU or IHF. J. Biol. Chem., 267, 23083-23086.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23083-23086
    • Hwang, D.S.1    Kornberg, A.2
  • 28
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader γ (γ) complex of E.coli DNA polymerase III
    • Jeruzalmi,D., O'Donnell,M. and Kuriyan,J. (2001) Crystal structure of the processivity clamp loader γ (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
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones,T.A., Zou,J.Y., Cowan,S.W. and Kjeldgaard,M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A, 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 30
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust,R.B. and Waugh,D.S. (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci., 8, 1668-1674.
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 31
    • 0033543650 scopus 로고    scopus 로고
    • Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH
    • Karata,K., Inagawa,T., Wilkinson,A.J., Tatsuta,T. and Ogura,T. (1999) Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH. J. Biol. Chem., 274, 26225-26232.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26225-26232
    • Karata, K.1    Inagawa, T.2    Wilkinson, A.J.3    Tatsuta, T.4    Ogura, T.5
  • 32
    • 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
  • 33
    • 0034327485 scopus 로고    scopus 로고
    • The replication origin of archaea is finally revealed
    • Kelman,Z. (2000) The replication origin of archaea is finally revealed. Trends Biochem. Sci., 25, 521-523.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 521-523
    • Kelman, Z.1
  • 34
    • 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
  • 36
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna,T.S., Kong,X.P., Gary,S., Burgers,P.M. and Kuriyan,J. (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell, 79, 1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 37
    • 0033485526 scopus 로고    scopus 로고
    • Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli
    • Kurokawa,K., Nishida,S., Emoto,A., Sekimizu,K. and Katayama,T. (1999) Replication cycle-coordinated change of the adenine nucleotide-bound forms of DnaA protein in Escherichia coli. EMBO J., 18, 6642-6652.
    • (1999) EMBO J. , vol.18 , pp. 6642-6652
    • Kurokawa, K.1    Nishida, S.2    Emoto, A.3    Sekimizu, K.4    Katayama, T.5
  • 38
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin,V.S. and Wilson,K.S. (1993) Automated refinement of protein models. Acta Crystallogr. D, 49, 129-147.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 39
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski,R.A., MacArthur,M.W., Moss,D.S. and Thornton,J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr., 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 0034063607 scopus 로고    scopus 로고
    • ATPase switches controlling DNA replication initiation
    • Lee,D.G. and Bell,S.P. (2000) ATPase switches controlling DNA replication initiation. Curr. Opin. Cell Biol., 12, 280-285.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 280-285
    • Lee, D.G.1    Bell, S.P.2
  • 41
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen,C.U., Steinmann,D., Whiteheart,S.W. and Weis,W.I. (1998) Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell, 94, 525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 42
    • 0033634866 scopus 로고    scopus 로고
    • Structure and function of Cdc6/Cdc18: Implications for origin recognition and checkpoint control
    • Liu,J., Smith,C.L, DeRyckere,D., DeAngelis,K., Martin,G.S. and Berger,J.M. (2000) Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control. Mol. Cell, 6, 637-648.
    • (2000) Mol. Cell , vol.6 , pp. 637-648
    • Liu, J.1    Smith, C.L.2    DeRyckere, D.3    DeAngelis, K.4    Martin, G.S.5    Berger, J.M.6
  • 43
    • 0034635464 scopus 로고    scopus 로고
    • Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids
    • Makise,M., Mima,S., Tsuchiya,T. and Mizushima,T. (2000) Identification of amino acids involved in the functional interaction between DnaA protein and acidic phospholipids. J. Biol. Chem., 275, 4513-4518.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4513-4518
    • Makise, M.1    Mima, S.2    Tsuchiya, T.3    Mizushima, T.4
  • 44
    • 0035949506 scopus 로고    scopus 로고
    • In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance proteins with the replication origin
    • Matsunaga,F., Forterre,P., Ishino,Y. and Myllykallio,H. (2001) In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance proteins with the replication origin. Proc. Natl Acad. Sci. USA, 98, 11152-11157.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11152-11157
    • Matsunaga, F.1    Forterre, P.2    Ishino, Y.3    Myllykallio, H.4
  • 45
    • 0032736348 scopus 로고    scopus 로고
    • Functional domains of DnaA proteins
    • Messer,W. et al. (1999) Functional domains of DnaA proteins. Biochimie, 81, 819-825.
    • (1999) Biochimie , vol.81 , pp. 819-825
    • Messer, W.1
  • 46
    • 0035118496 scopus 로고    scopus 로고
    • Bacterial replication initiator DnaA. Rules for DnaA binding and roles of DnaA in origin unwinding and helicase loading
    • Messer,W. et al. (2001) Bacterial replication initiator DnaA. Rules for DnaA binding and roles of DnaA in origin unwinding and helicase loading. Biochimie, 83, 5-12.
    • (2001) Biochimie , vol.83 , pp. 5-12
    • Messer, W.1
  • 47
    • 0030983404 scopus 로고    scopus 로고
    • Negative control of DNA replication by hydrolysis of ATP bound to DnaA protein, the initiator of chromosomal DNA replication in Escherichia coli
    • Mizushima,T., Nishida,S., Kurokawa,K., Katayama,T., Miki,T. and Sekimizu,K. (1997) 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, 3724-3730.
    • (1997) EMBO J. , vol.16 , pp. 3724-3730
    • Mizushima, T.1    Nishida, S.2    Kurokawa, K.3    Katayama, T.4    Miki, T.5    Sekimizu, K.6
  • 48
    • 0032516840 scopus 로고    scopus 로고
    • 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
    • Mizushima,T., Takaki,T., Kubota,T., Tsuchiya,T., Miki,T., Katayama,T. and Sekimizu,K. (1998) 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, 20847-20851.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20847-20851
    • Mizushima, T.1    Takaki, T.2    Kubota, T.3    Tsuchiya, T.4    Miki, T.5    Katayama, T.6    Sekimizu, K.7
  • 50
    • 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
  • 51
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls,A., Sharp,K.A. and Honig,B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 52
    • 0037177830 scopus 로고    scopus 로고
    • A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication: Evidence from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo
    • Nishida,S., Fujimitsu,K., Sekimizu,K., Ohmura,T., Ueda,T. and Katayama,T. (2002) A nucleotide switch in the Escherichia coli DnaA protein initiates chromosomal replication: evidence from a mutant DnaA protein defective in regulatory ATP hydrolysis in vitro and in vivo. J. Biol. Chem., 277, 14986-14995.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14986-14995
    • Nishida, S.1    Fujimitsu, K.2    Sekimizu, K.3    Ohmura, T.4    Ueda, T.5    Katayama, T.6
  • 53
    • 0029948001 scopus 로고    scopus 로고
    • SSAP: Sequential structure alignment program for protein structure comparison
    • Orengo,C.A. and Taylor,W.R. (1996) SSAP: sequential structure alignment program for protein structure comparison. Methods Enzymol., 266, 617-635.
    • (1996) Methods Enzymol. , vol.266 , pp. 617-635
    • Orengo, C.A.1    Taylor, W.R.2
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski,Z. and Minor,W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 276, 472-494.
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 0034840471 scopus 로고    scopus 로고
    • Atomic structure of the clamp loader small subunit from Pyrococcus furiosus
    • Oyama,T., Ishino,Y., Cann,I.K., Ishino,S. and Morikawa,K. (2001) Atomic structure of the clamp loader small subunit from Pyrococcus furiosus. Mol. Cell, 8, 455-463.
    • (2001) Mol. Cell , vol.8 , pp. 455-463
    • Oyama, T.1    Ishino, Y.2    Cann, I.K.3    Ishino, S.4    Morikawa, K.5
  • 58
    • 0029088758 scopus 로고
    • Interaction of the initiator protein DnaA of Escherichia coli with its DNA target
    • Schaper,S. and Messer,W. (1995) Interaction of the initiator protein DnaA of Escherichia coli with its DNA target. J. Biol. Chem., 270, 17622-17626.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17622-17626
    • Schaper, S.1    Messer, W.2
  • 59
    • 0030894736 scopus 로고    scopus 로고
    • Prediction of the structure of the replication initiator protein DnaA
    • Schaper,S. and Messer,W. (1997) Prediction of the structure of the replication initiator protein DnaA. Proteins, 28, 1-9.
    • (1997) Proteins , vol.28 , pp. 1-9
    • Schaper, S.1    Messer, W.2
  • 60
    • 0023904203 scopus 로고
    • Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli
    • Sekimizu,K. and Kornberg,A. (1988) Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli. J. Biol. Chem., 263, 7131-7135.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7131-7135
    • Sekimizu, K.1    Kornberg, A.2
  • 61
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Shamoo,Y., Friedman,A.M., Parsons,M.R., Konigsberg,W.H. and Steitz,T.A. (1995) Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA. Nature, 376, 362-366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 62
    • 0023955263 scopus 로고
    • Coordination of chromosome replication initiation in Escherichia coli: Effects of different dnaA alleles
    • Skarstad,K., von Meyenburg,K., Hansen,F.G. and Boye,E. (1988) Coordination of chromosome replication initiation in Escherichia coli: effects of different dnaA alleles. J. Bacteriol., 170, 852-858.
    • (1988) J. Bacteriol. , vol.170 , pp. 852-858
    • Skarstad, K.1    Von Meyenburg, K.2    Hansen, F.G.3    Boye, E.4
  • 63
    • 0035869023 scopus 로고    scopus 로고
    • Mechanism of origin unwinding: Sequential binding of DnaA to double- and single-stranded DNA
    • Speck,C. and Messer,W. (2001) Mechanism of origin unwinding: sequential binding of DnaA to double- and single-stranded DNA. EMBO J., 20, 1469-1476.
    • (2001) EMBO J. , vol.20 , pp. 1469-1476
    • Speck, C.1    Messer, W.2
  • 64
    • 0030854615 scopus 로고    scopus 로고
    • From footprint to toeprint: A close-up of the DnaA box, the binding site for the bacterial initiator protein DnaA
    • Speck,C., Weigel,C. and Messer,W. (1997) From footprint to toeprint: a close-up of the DnaA box, the binding site for the bacterial initiator protein DnaA. Nucleic Acids Res., 25, 3242-3247.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3242-3247
    • Speck, C.1    Weigel, C.2    Messer, W.3
  • 65
    • 0028859388 scopus 로고
    • Novel alleles of the Escherichia coli dnaA gene are defective in replication of pSC101 but not of oriC
    • Sutton,M.D. and Kaguni,J.M. (1995) Novel alleles of the Escherichia coli dnaA gene are defective in replication of pSC101 but not of oriC. J. Bacteriol., 177, 6657-6665.
    • (1995) J. Bacteriol. , vol.177 , pp. 6657-6665
    • Sutton, M.D.1    Kaguni, J.M.2
  • 66
    • 0031565989 scopus 로고    scopus 로고
    • The Escherichia coli dnaA gene: Four functional domains
    • Sutton,M.D. and Kaguni,J.M. (1997a) The Escherichia coli dnaA gene: four functional domains. J. Mol. Biol., 274, 546-561.
    • (1997) J. Mol. Biol. , vol.274 , pp. 546-561
    • Sutton, M.D.1    Kaguni, J.M.2
  • 67
    • 0030823757 scopus 로고    scopus 로고
    • Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity
    • Sutton,M.D. and Kaguni,J.M. (1997b) Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity. J. Biol. Chem., 272, 23017-23024.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23017-23024
    • Sutton, M.D.1    Kaguni, J.M.2
  • 68
    • 0032545466 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E.coli chromosomal origin
    • Sutton,M.D., Carr,K.M., Vicente,M. and Kaguni,J.M. (1998) Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E.coli chromosomal origin. J. Biol. Chem., 273, 34255-34262.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34255-34262
    • Sutton, M.D.1    Carr, K.M.2    Vicente, M.3    Kaguni, J.M.4
  • 69
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger,T. and Berendzen,J. (1999) Automated structure solution for MIR and MAD. Acta Crystallogr. D, 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.1    Berendzen, J.2
  • 70
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL-X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson,J.D., Gibson,T.J., Plewniak,F., Jeanmougin,F. and Higgins,D.G. (1997) The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 72
    • 0031715606 scopus 로고    scopus 로고
    • Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
    • Yu,R.C., Hanson,P.I., Jahn,R. and Brunger,A.T. (1998) Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP. Nat. Struct. Biol., 5, 803-811.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 803-811
    • Yu, R.C.1    Hanson, P.I.2    Jahn, R.3    Brunger, A.T.4
  • 73
    • 0034502514 scopus 로고    scopus 로고
    • Structure of the AAA ATPase p97
    • Zhang,X. et al. (2000) Structure of the AAA ATPase p97. Mol. Cell, 6, 1473-1484.
    • (2000) Mol. Cell , vol.6 , pp. 1473-1484
    • Zhang, X.1
  • 74
    • 0035282783 scopus 로고    scopus 로고
    • Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells
    • Zheng,W., Li,Z., Skarstad,K. and Crooke,E. (2001) Mutations in DnaA protein suppress the growth arrest of acidic phospholipid-deficient Escherichia coli cells. EMBO J., 20, 1164-1172.
    • (2001) EMBO J. , vol.20 , pp. 1164-1172
    • Zheng, W.1    Li, Z.2    Skarstad, K.3    Crooke, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.