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Volumn 37, Issue 1, 2010, Pages 90-101

Primase Directs the Release of DnaC from DnaB

Author keywords

DNA

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ARGININE; DNA B; DNA C; DNA PRIMASE; MONOMER; POLYMER; SINGLE STRANDED DNA;

EID: 73649145533     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.12.031     Document Type: Article
Times cited : (65)

References (68)
  • 1
    • 0025876111 scopus 로고
    • Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli
    • Allen Jr. G.C., and Kornberg A. Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli. J. Biol. Chem. 266 (1991) 22096-22101
    • (1991) J. Biol. Chem. , vol.266 , pp. 22096-22101
    • Allen Jr., G.C.1    Kornberg, A.2
  • 2
    • 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. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318 (2007) 459-463
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 3
    • 34547886124 scopus 로고    scopus 로고
    • The crystal structure of the Thermus aquaticus DnaB helicase monomer
    • Bailey S., Eliason W.K., and Steitz T.A. The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res. 35 (2007) 4728-4736
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4728-4736
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 4
    • 0023654911 scopus 로고
    • Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro
    • Baker T.A., Funnell B.E., and Kornberg A. Helicase action of dnaB protein during replication from the Escherichia coli chromosomal origin in vitro. J. Biol. Chem. 262 (1987) 6877-6885
    • (1987) J. Biol. Chem. , vol.262 , pp. 6877-6885
    • Baker, T.A.1    Funnell, B.E.2    Kornberg, A.3
  • 6
    • 0034142263 scopus 로고    scopus 로고
    • DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates
    • Bhattacharyya S., and Griep M.A. DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates. Biochemistry 39 (2000) 745-752
    • (2000) Biochemistry , vol.39 , pp. 745-752
    • Bhattacharyya, S.1    Griep, M.A.2
  • 7
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • Bird L.E., Pan H., Soultanas P., and Wigley D.B. Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39 (2000) 171-182
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 8
    • 0023644941 scopus 로고
    • Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products
    • Biswas S.B., and Biswas E.E. Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products. J. Biol. Chem. 262 (1987) 7831-7838
    • (1987) J. Biol. Chem. , vol.262 , pp. 7831-7838
    • Biswas, S.B.1    Biswas, E.E.2
  • 9
    • 33749008780 scopus 로고    scopus 로고
    • Quantitative analysis of binding of single-stranded DNA by Escherichia coli DnaB helicase and the DnaB x DnaC complex
    • Biswas S.B., and Biswas-Fiss E.E. Quantitative analysis of binding of single-stranded DNA by Escherichia coli DnaB helicase and the DnaB x DnaC complex. Biochemistry 45 (2006) 11505-11513
    • (2006) Biochemistry , vol.45 , pp. 11505-11513
    • Biswas, S.B.1    Biswas-Fiss, E.E.2
  • 10
    • 2542535234 scopus 로고    scopus 로고
    • Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli
    • Biswas S.B., Flowers S., and Biswas-Fiss E.E. Quantitative analysis of nucleotide modulation of DNA binding by DnaC protein of Escherichia coli. Biochem. J. 379 (2004) 553-562
    • (2004) Biochem. J. , vol.379 , pp. 553-562
    • Biswas, S.B.1    Flowers, S.2    Biswas-Fiss, E.E.3
  • 11
    • 40549130342 scopus 로고    scopus 로고
    • CDC6: from DNA replication to cell cycle checkpoints and oncogenesis
    • Borlado L.R., and Méndez J. CDC6: from DNA replication to cell cycle checkpoints and oncogenesis. Carcinogenesis 29 (2008) 237-243
    • (2008) Carcinogenesis , vol.29 , pp. 237-243
    • Borlado, L.R.1    Méndez, J.2
  • 12
    • 0024284091 scopus 로고
    • Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
    • Bramhill D., and 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
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 13
    • 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. Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin. J. Biol. Chem. 276 (2001) 44919-44925
    • (2001) J. Biol. Chem. , vol.276 , pp. 44919-44925
    • Carr, K.M.1    Kaguni, J.M.2
  • 14
    • 0037131160 scopus 로고    scopus 로고
    • Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin
    • Carr K.M., and Kaguni J.M. Escherichia coli DnaA protein loads a single DnaB helicase at a DnaA box hairpin. J. Biol. Chem. 277 (2002) 39815-39822
    • (2002) J. Biol. Chem. , vol.277 , pp. 39815-39822
    • Carr, K.M.1    Kaguni, J.M.2
  • 15
    • 0034714241 scopus 로고    scopus 로고
    • Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork
    • Chang P., and Marians K.J. Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork. J. Biol. Chem. 275 (2000) 26187-26195
    • (2000) J. Biol. Chem. , vol.275 , pp. 26187-26195
    • Chang, P.1    Marians, K.J.2
  • 16
    • 38449105269 scopus 로고    scopus 로고
    • Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin
    • Chodavarapu S., Felczak M.M., Yaniv J.R., and Kaguni J.M. Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin. Mol. Microbiol. 67 (2008) 781-792
    • (2008) Mol. Microbiol. , vol.67 , pp. 781-792
    • Chodavarapu, S.1    Felczak, M.M.2    Yaniv, J.R.3    Kaguni, J.M.4
  • 17
    • 38849106170 scopus 로고    scopus 로고
    • Identification of a DNA primase template tracking site redefines the geometry of primer synthesis
    • Corn J.E., Pelton J.G., and Berger J.M. Identification of a DNA primase template tracking site redefines the geometry of primer synthesis. Nat. Struct. Mol. Biol. 15 (2008) 163-169
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 163-169
    • Corn, J.E.1    Pelton, J.G.2    Berger, J.M.3
  • 19
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger J.P., and Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 93-114
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 20
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
    • Erzberger J.P., Pirruccello M.M., and Berger J.M. The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation. EMBO J. 21 (2002) 4763-4773
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 21
    • 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. Replisome assembly at oriC, the replication origin of E. coli, reveals an explanation for initiation sites outside an origin. Mol. Cell 4 (1999) 541-553
    • (1999) Mol. Cell , vol.4 , pp. 541-553
    • Fang, L.1    Davey, M.J.2    O'Donnell, M.3
  • 22
    • 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. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7 (1999) 691-698
    • (1999) Structure , vol.7 , pp. 691-698
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 23
    • 10944257577 scopus 로고    scopus 로고
    • The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin
    • Felczak M.M., and Kaguni J.M. The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin. J. Biol. Chem. 279 (2004) 51156-51162
    • (2004) J. Biol. Chem. , vol.279 , pp. 51156-51162
    • Felczak, M.M.1    Kaguni, J.M.2
  • 24
    • 21644437635 scopus 로고    scopus 로고
    • An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin
    • Felczak M.M., Simmons L.A., and Kaguni J.M. An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin. J. Biol. Chem. 280 (2005) 24627-24633
    • (2005) J. Biol. Chem. , vol.280 , pp. 24627-24633
    • Felczak, M.M.1    Simmons, L.A.2    Kaguni, J.M.3
  • 25
    • 61849173573 scopus 로고    scopus 로고
    • Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation
    • Francis L.I., Randell J.C., Takara T.J., Uchima L., and Bell S.P. Incorporation into the prereplicative complex activates the Mcm2-7 helicase for Cdc7-Dbf4 phosphorylation. Genes Dev. 23 (2009) 643-654
    • (2009) Genes Dev. , vol.23 , pp. 643-654
    • Francis, L.I.1    Randell, J.C.2    Takara, T.J.3    Uchima, L.4    Bell, S.P.5
  • 26
    • 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. In vitro assembly of a prepriming complex at the origin of the Escherichia coli chromosome. J. Biol. Chem. 262 (1987) 10327-10334
    • (1987) J. Biol. Chem. , vol.262 , pp. 10327-10334
    • Funnell, B.E.1    Baker, T.A.2    Kornberg, A.3
  • 27
    • 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. 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 (2003) 441-465
    • (2003) J. Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 29
    • 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. 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 (1998) 10515-10529
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 30
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: recognition and structure
    • Jezewska M.J., Rajendran S., and Bujalowski W. Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: recognition and structure. Biochemistry 37 (1998) 3116-3136
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 31
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein
    • Jezewska M.J., Rajendran S., and Bujalowski W. Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein. J. Biol. Chem. 273 (1998) 9058-9069
    • (1998) J. Biol. Chem. , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 32
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: controlling the initiation of bacterial DNA replication and more
    • Kaguni J.M. DnaA: controlling the initiation of bacterial DNA replication and more. Annu. Rev. Microbiol. 60 (2006) 351-375
    • (2006) Annu. Rev. Microbiol. , vol.60 , pp. 351-375
    • Kaguni, J.M.1
  • 33
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement
    • Kim S., Dallmann H.G., McHenry C.S., and Marians K.J. 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    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 34
    • 0021859620 scopus 로고
    • Evidence that discontinuous DNA replication in Escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine
    • Kitani T., Yoda K., Ogawa T., and Okazaki T. Evidence that discontinuous DNA replication in Escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine. J. Mol. Biol. 184 (1985) 45-52
    • (1985) J. Mol. Biol. , vol.184 , pp. 45-52
    • Kitani, T.1    Yoda, K.2    Ogawa, T.3    Okazaki, T.4
  • 35
    • 0020405207 scopus 로고
    • The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex
    • Kobori J.A., and Kornberg A. The Escherichia coli dnaC gene product. III. Properties of the dnaB-dnaC protein complex. J. Biol. Chem. 257 (1982) 13770-13775
    • (1982) J. Biol. Chem. , vol.257 , pp. 13770-13775
    • Kobori, J.A.1    Kornberg, A.2
  • 36
    • 0027480463 scopus 로고
    • A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif
    • Koonin E.V. A superfamily of ATPases with diverse functions containing either classical or deviant ATP-binding motif. J. Mol. Biol. 229 (1993) 1165-1174
    • (1993) J. Mol. Biol. , vol.229 , pp. 1165-1174
    • Koonin, E.V.1
  • 37
    • 34249710254 scopus 로고    scopus 로고
    • A key role for the GINS complex at DNA replication forks
    • Labib K., and Gambus A. A key role for the GINS complex at DNA replication forks. Trends Cell Biol. 17 (2007) 271-278
    • (2007) Trends Cell Biol. , vol.17 , pp. 271-278
    • Labib, K.1    Gambus, A.2
  • 38
    • 0031019643 scopus 로고    scopus 로고
    • 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
    • Learn B.A., Um S.J., Huang L., and 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
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1154-1159
    • Learn, B.A.1    Um, S.J.2    Huang, L.3    McMacken, R.4
  • 39
    • 66149123740 scopus 로고    scopus 로고
    • Initiating chromosome replication in E. coli: it makes sense to recycle
    • Leonard A.C., and Grimwade J.E. Initiating chromosome replication in E. coli: it makes sense to recycle. Genes Dev. 23 (2009) 1145-1150
    • (2009) Genes Dev. , vol.23 , pp. 1145-1150
    • Leonard, A.C.1    Grimwade, J.E.2
  • 40
    • 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. The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res. 37 (2009) 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
  • 41
    • 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. Essential amino acids of Escherichia coli DnaC protein in an N-terminal domain interact with DnaB helicase. J. Biol. Chem. 276 (2001) 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
  • 42
    • 0025276460 scopus 로고
    • Host virus interactions in the initiation of bacteriophage lambda DNA replication. Recruitment of Escherichia coli DnaB helicase by lambda P replication protein
    • Mallory J.B., Alfano C., and McMacken R. Host virus interactions in the initiation of bacteriophage lambda DNA replication. Recruitment of Escherichia coli DnaB helicase by lambda P replication protein. J. Biol. Chem. 265 (1990) 13297-13307
    • (1990) J. Biol. Chem. , vol.265 , pp. 13297-13307
    • Mallory, J.B.1    Alfano, C.2    McMacken, R.3
  • 43
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • Marszalek J., and Kaguni J.M. DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. J. Biol. Chem. 269 (1994) 4883-4890
    • (1994) J. Biol. Chem. , vol.269 , pp. 4883-4890
    • Marszalek, J.1    Kaguni, J.M.2
  • 44
    • 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
  • 46
    • 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. Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators. Cell 135 (2008) 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
  • 47
    • 0021759104 scopus 로고
    • Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome
    • Nakayama N., Arai N., Kaziro Y., and Arai K. Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome. J. Biol. Chem. 259 (1984) 88-96
    • (1984) J. Biol. Chem. , vol.259 , pp. 88-96
    • Nakayama, N.1    Arai, N.2    Kaziro, Y.3    Arai, K.4
  • 48
    • 0023645239 scopus 로고
    • Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein
    • Nakayama N., Bond M.W., Miyajima A., Kobori J., and Arai K. Structure of Escherichia coli dnaC. Identification of a cysteine residue possibly involved in association with dnaB protein. J. Biol. Chem. 262 (1987) 10475-10480
    • (1987) J. Biol. Chem. , vol.262 , pp. 10475-10480
    • Nakayama, N.1    Bond, M.W.2    Miyajima, A.3    Kobori, J.4    Arai, K.5
  • 49
    • 38949213341 scopus 로고    scopus 로고
    • Once in a lifetime: strategies for preventing re-replication in prokaryotic and eukaryotic cells
    • Nielsen O., and Løbner-Olesen A. Once in a lifetime: strategies for preventing re-replication in prokaryotic and eukaryotic cells. EMBO Rep. 9 (2008) 151-156
    • (2008) EMBO Rep. , vol.9 , pp. 151-156
    • Nielsen, O.1    Løbner-Olesen, A.2
  • 52
    • 34047149973 scopus 로고    scopus 로고
    • Replisome mechanics: insights into a twin DNA polymerase machine
    • Pomerantz R.T., and O'Donnell M. Replisome mechanics: insights into a twin DNA polymerase machine. Trends Microbiol. 15 (2007) 156-164
    • (2007) Trends Microbiol. , vol.15 , pp. 156-164
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 53
    • 29544435484 scopus 로고    scopus 로고
    • Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase
    • Randell J.C., Bowers J.L., Rodríguez H.K., and Bell S.P. Sequential ATP hydrolysis by Cdc6 and ORC directs loading of the Mcm2-7 helicase. Mol. Cell 21 (2006) 29-39
    • (2006) Mol. Cell , vol.21 , pp. 29-39
    • Randell, J.C.1    Bowers, J.L.2    Rodríguez, H.K.3    Bell, S.P.4
  • 54
    • 23644448872 scopus 로고    scopus 로고
    • Origins of DNA replication in the three domains of life
    • Robinson N.P., and Bell S.D. Origins of DNA replication in the three domains of life. FEBS J. 272 (2005) 3757-3766
    • (2005) FEBS J. , vol.272 , pp. 3757-3766
    • Robinson, N.P.1    Bell, S.D.2
  • 55
    • 0032522423 scopus 로고    scopus 로고
    • Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC
    • San Martin C., Radermacher M., Wolpensinger B., Engel A., Miles C.S., Dixon N.E., and Carazo J.M. Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC. Structure 6 (1998) 501-509
    • (1998) Structure , vol.6 , pp. 501-509
    • San Martin, C.1    Radermacher, M.2    Wolpensinger, B.3    Engel, A.4    Miles, C.S.5    Dixon, N.E.6    Carazo, J.M.7
  • 56
    • 0023658349 scopus 로고
    • ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome
    • Sekimizu K., Bramhill D., and Kornberg A. ATP activates dnaA protein in initiating replication of plasmids bearing the origin of the E. coli chromosome. Cell 50 (1987) 259-265
    • (1987) Cell , vol.50 , pp. 259-265
    • Sekimizu, K.1    Bramhill, D.2    Kornberg, A.3
  • 57
    • 33749075373 scopus 로고    scopus 로고
    • Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression
    • Sheu Y.J., and Stillman B. Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression. Mol. Cell 24 (2006) 101-113
    • (2006) Mol. Cell , vol.24 , pp. 101-113
    • Sheu, Y.J.1    Stillman, B.2
  • 59
    • 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. Escherichia coli DnaA protein. The N-terminal domain and loading of DnaB helicase at the E. coli chromosomal origin. J. Biol. Chem. 273 (1998) 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
  • 60
    • 0029832926 scopus 로고    scopus 로고
    • The extreme C terminus of primase is required for interaction with DnaB at the replication fork
    • Tougu K., and Marians K.J. The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J. Biol. Chem. 271 (1996) 21391-21397
    • (1996) J. Biol. Chem. , vol.271 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 61
    • 0029788209 scopus 로고    scopus 로고
    • The interaction between helicase and primase sets the replication fork clock
    • Tougu K., and Marians K.J. The interaction between helicase and primase sets the replication fork clock. J. Biol. Chem. 271 (1996) 21398-21405
    • (1996) J. Biol. Chem. , vol.271 , pp. 21398-21405
    • Tougu, K.1    Marians, K.J.2
  • 62
    • 0024562458 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
    • Wahle E., Lasken R.S., and Kornberg A. The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties. J. Biol. Chem. 264 (1989) 2463-2468
    • (1989) J. Biol. Chem. , vol.264 , pp. 2463-2468
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 63
    • 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. The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions. J. Biol. Chem. 264 (1989) 2469-2475
    • (1989) J. Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 64
    • 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. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7 (1999) 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
  • 65
    • 0032528270 scopus 로고    scopus 로고
    • Effects of purified SeqA protein on oriC-dependent DNA replication in vitro
    • Wold S., Boye E., Slater S., Kleckner N., and Skarstad K. Effects of purified SeqA protein on oriC-dependent DNA replication in vitro. EMBO J. 17 (1998) 4158-4165
    • (1998) EMBO J. , vol.17 , pp. 4158-4165
    • Wold, S.1    Boye, E.2    Slater, S.3    Kleckner, N.4    Skarstad, K.5
  • 66
    • 0026706674 scopus 로고
    • Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size
    • Wu C.A., Zechner E.L., and Marians K.J. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple effectors act to modulate Okazaki fragment size. J. Biol. Chem. 267 (1992) 4030-4044
    • (1992) J. Biol. Chem. , vol.267 , pp. 4030-4044
    • Wu, C.A.1    Zechner, E.L.2    Marians, K.J.3
  • 67
    • 0025782760 scopus 로고
    • Specificity of recognition sequence for Escherichia coli primase
    • Yoda K., and Okazaki T. Specificity of recognition sequence for Escherichia coli primase. Mol. Gen. Genet. 227 (1991) 1-8
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 1-8
    • Yoda, K.1    Okazaki, T.2
  • 68
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different Quaternary states
    • Yu X., Jezewska M.J., Bujalowski W., and Egelman E.H. The hexameric E. coli DnaB helicase can exist in different Quaternary states. J. Mol. Biol. 259 (1996) 7-14
    • (1996) J. Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.