메뉴 건너뛰기




Volumn 11, Issue 4, 2003, Pages 1009-1020

A two-protein strategy for the functional loading of a cellular replicative DNA helicase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DNA B; HELICASE; HELICASE DNAC; HELICASE DNAI; INITIATION FACTOR; UNCLASSIFIED DRUG;

EID: 0038637844     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00130-8     Document Type: Article
Times cited : (113)

References (36)
  • 1
    • 0034600838 scopus 로고    scopus 로고
    • A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein
    • Ahnert P., Picha K.M., Patel S.S. A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein. EMBO J. 19:2000;3418-3427.
    • (2000) EMBO J. , vol.19 , pp. 3418-3427
    • Ahnert, P.1    Picha, K.M.2    Patel, S.S.3
  • 2
    • 0025876111 scopus 로고
    • Fine balance in the regulation of DnaB helicase by DnaC protein in replication in Escherichia coli
    • Allen G.C., 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, G.C.1    Kornberg, A.2
  • 3
    • 0032489041 scopus 로고    scopus 로고
    • Polymerases and the replisome: Machines within machines
    • Baker T.A., Bell S.P. Polymerases and the replisome. machines within machines Cell. 92:1998;295-305.
    • (1998) Cell , vol.92 , pp. 295-305
    • Baker, T.A.1    Bell, S.P.2
  • 4
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell S.P., Dutta A. DNA replication in eukaryotic cells. Annu. Rev. Biochem. 71:2002;333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 5
    • 0029003909 scopus 로고
    • The Bacillus subtilis dnaI gene is part of the dnaB operon
    • Bruand C., Ehrlich S.D. The Bacillus subtilis dnaI gene is part of the dnaB operon. Microbiology. 141:1995;1199-1200.
    • (1995) Microbiology , vol.141 , pp. 1199-1200
    • Bruand, C.1    Ehrlich, S.D.2
  • 6
    • 0029003406 scopus 로고
    • Primosome assembly site in Bacillus subtilis
    • Bruand C., Ehrlich S.D., Janniere L. Primosome assembly site in Bacillus subtilis. EMBO J. 14:1995;2642-2650.
    • (1995) EMBO J. , vol.14 , pp. 2642-2650
    • Bruand, C.1    Ehrlich, S.D.2    Janniere, L.3
  • 7
    • 0035725265 scopus 로고    scopus 로고
    • DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome
    • Bruand C., Farache M., McGovern S., Ehrlich S.D., Polard P. DnaB, DnaD and DnaI proteins are components of the Bacillus subtilis replication restart primosome. Mol. Microbiol. 42:2001;245-255.
    • (2001) Mol. Microbiol. , vol.42 , pp. 245-255
    • Bruand, C.1    Farache, M.2    McGovern, S.3    Ehrlich, S.D.4    Polard, P.5
  • 9
    • 0026770783 scopus 로고
    • The simian virus 40 T antigen double hexamer assembles around the DNA at the replication origin J
    • Dean F.B., Borowiec J.A., Eki T., Hurwitz J. The simian virus 40 T antigen double hexamer assembles around the DNA at the replication origin J. Biol. Chem. 267:1992;14129-14137.
    • (1992) Biol. Chem. , vol.267 , pp. 14129-14137
    • Dean, F.B.1    Borowiec, J.A.2    Eki, T.3    Hurwitz, J.4
  • 10
    • 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., 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
  • 11
    • 0034033766 scopus 로고    scopus 로고
    • Subcellular localization of Dna-initiation proteins of Bacillus subtilis: Evidence that chromosome replication begins at either edge of the nucleoids
    • Imai Y., Ogasawara N., Ishigo-Oka D., Kadoya R., Daito T., Moriya S. Subcellular localization of Dna-initiation proteins of Bacillus subtilis. evidence that chromosome replication begins at either edge of the nucleoids Mol. Microbiol. 36:2000;1037-1048.
    • (2000) Mol. Microbiol. , vol.36 , pp. 1037-1048
    • Imai, Y.1    Ogasawara, N.2    Ishigo-Oka, D.3    Kadoya, R.4    Daito, T.5    Moriya, S.6
  • 12
    • 0035108406 scopus 로고    scopus 로고
    • DnaD protein of Bacillus subtilis interacts with DnaA, the initiator protein of replication
    • Ishigo-Oka D., Ogasawara N., Moriya S. DnaD protein of Bacillus subtilis interacts with DnaA, the initiator protein of replication. J. Bacteriol. 183:2001;2148-2150.
    • (2001) J. Bacteriol. , vol.183 , pp. 2148-2150
    • Ishigo-Oka, D.1    Ogasawara, N.2    Moriya, S.3
  • 14
    • 0033548710 scopus 로고    scopus 로고
    • DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence
    • Kaplan D.L., Steitz T.A. DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence. J. Biol. Chem. 274:1999;6889-6897.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6889-6897
    • Kaplan, D.L.1    Steitz, T.A.2
  • 15
    • 0014724607 scopus 로고
    • Isolation and genetic analysis of temperature sensitive mutants of B. subtilis defective in DNA synthesis
    • Karamata D., Gross J.D. Isolation and genetic analysis of temperature sensitive mutants of B. subtilis defective in DNA synthesis. Mol. Gen. Genet. 108:1970;277-287.
    • (1970) Mol. Gen. Genet. , vol.108 , pp. 277-287
    • Karamata, D.1    Gross, J.D.2
  • 16
    • 0026532095 scopus 로고
    • DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA
    • Koonin, E.V. (1992). DnaC protein contains a modified ATP-binding motif and belongs to a novel family of ATPases including also DnaA. Nucleic Acids Res. 20, 1997.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1997
    • Koonin, E.V.1
  • 17
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz J.H., McMacken R. The Escherichia coli dnaB replication protein is a DNA helicase. J. Biol. Chem. 261:1986;4738-4748.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 18
    • 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., 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
  • 19
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe D.D., Aravind L., Grishin N.V., Koonin E.V. The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res. 10:2000;5-16.
    • (2000) Genome Res. , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 21
    • 0034177963 scopus 로고    scopus 로고
    • PriA-directed replication fork restart in Escherichia coli
    • Marians K.J. PriA-directed replication fork restart in Escherichia coli. Trends Biochem. Sci. 25:2000;185-189.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 185-189
    • Marians, K.J.1
  • 23
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • Marszalek J., 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
  • 24
    • 0032958074 scopus 로고    scopus 로고
    • Regulation of initiation of Bacillus subtilis chromosome replication
    • Moriya S., Imai Y., Hassan A.K., Ogasawara N. Regulation of initiation of Bacillus subtilis chromosome replication. Plasmid. 41:1999;17-29.
    • (1999) Plasmid , vol.41 , pp. 17-29
    • Moriya, S.1    Imai, Y.2    Hassan, A.K.3    Ogasawara, N.4
  • 25
    • 0029666277 scopus 로고    scopus 로고
    • The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes
    • Ng J.Y., Marians K.J. The ordered assembly of the phiX174-type primosome. I. Isolation and identification of intermediate protein-DNA complexes. J. Biol. Chem. 271:1996;15642-15648.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15642-15648
    • Ng, J.Y.1    Marians, K.J.2
  • 27
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel S.S., Picha K.M. Structure and function of hexameric helicases. Annu. Rev. Biochem. 69:2000;651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 28
    • 0036529480 scopus 로고    scopus 로고
    • Restart of DNA replication in Gram-positive bacteria: Functional characterisation of the Bacillus subtilis PriA initiator
    • Polard P., Marsin S., McGovern S., Velten M., Wigley D.B., Ehrlich S.D., Bruand C. Restart of DNA replication in Gram-positive bacteria. functional characterisation of the Bacillus subtilis PriA initiator Nucleic Acids Res. 30:2002;1593-1605.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1593-1605
    • Polard, P.1    Marsin, S.2    McGovern, S.3    Velten, M.4    Wigley, D.B.5    Ehrlich, S.D.6    Bruand, C.7
  • 29
    • 0028918316 scopus 로고
    • The Bacillus subtilis dnaC gene encodes a protein homologous to the DnaB helicase of Escherichia coli
    • Sakamoto Y., Nakai S., Moriya S., Yoshikawa H., Ogasawara N. The Bacillus subtilis dnaC gene encodes a protein homologous to the DnaB helicase of Escherichia coli. Microbiology. 141:1995;641-644.
    • (1995) Microbiology , vol.141 , pp. 641-644
    • Sakamoto, Y.1    Nakai, S.2    Moriya, S.3    Yoshikawa, H.4    Ogasawara, N.5
  • 30
    • 0029960337 scopus 로고    scopus 로고
    • Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC
    • Sandler S.J., Samra H.S., Clark A.J. Differential suppression of priA2::kan phenotypes in Escherichia coli K-12 by mutations in priA, lexA, and dnaC. Genetics. 143:1996;5-13.
    • (1996) Genetics , vol.143 , pp. 5-13
    • Sandler, S.J.1    Samra, H.S.2    Clark, A.J.3
  • 31
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin M.C., Stamford N.P., Dammerova N., Dixon N.E., Carazo J.M. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J. Struct. Biol. 114:1995;167-176.
    • (1995) J. Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 32
    • 0024562458 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties
    • a
    • Wahle E., Lasken R.S., Kornberg A. The dnaB-dnaC replication protein complex of Escherichia coli. I. Formation and properties. J. Biol. Chem. 264:1989;2463-2468. a.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2463-2468
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 33
    • 0024520416 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions
    • b
    • Wahle E., Lasken R.S., 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. b.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 34
    • 0034677944 scopus 로고    scopus 로고
    • Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function
    • Xu L., Marians K.J. Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function. J. Biol. Chem. 275:2000;8196-8205.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8196-8205
    • Xu, L.1    Marians, K.J.2
  • 35
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary states
    • Yu X., Jezewska M.J., Bujalowski W., 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
  • 36
    • 0030595331 scopus 로고    scopus 로고
    • Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication
    • Yuzhakov A., Turner J., O'Donnell M. Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication. Cell. 86:1996;877-886.
    • (1996) Cell , vol.86 , pp. 877-886
    • Yuzhakov, A.1    Turner, J.2    O'Donnell, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.