메뉴 건너뛰기




Volumn 84, Issue 4, 1996, Pages 643-650

Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement

Author keywords

[No Author keywords available]

Indexed keywords

DNA B; DNA POLYMERASE; HELICASE;

EID: 0030070356     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81039-9     Document Type: Article
Times cited : (315)

References (35)
  • 1
    • 0024333260 scopus 로고
    • Characterization of the helicase and primase activities of the 63-kDa component of the bacteriophage T7 gene 4 protein
    • Bernstein, J., and Richardson, C.C. (1989). Characterization of the helicase and primase activities of the 63-kDa component of the bacteriophage T7 gene 4 protein. J. Biol. Chem. 264, 13066-13073.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13066-13073
    • Bernstein, J.1    Richardson, C.C.2
  • 2
    • 0016813835 scopus 로고
    • DnaG gene product, a rifampicin-resistant RNa polymerase, initiates the conversion of a single-stranded coliphage DNa to its duplex replicative form
    • Bouché, J.P., Zechel, K., and Kornberg, A. (1975). dnaG gene product, a rifampicin-resistant RNA polymerase, initiates the conversion of a single-stranded coliphage DNA to its duplex replicative form. J. Biol. Chem. 250, 5995-6001.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5995-6001
    • Bouché, J.P.1    Zechel, K.2    Kornberg, A.3
  • 3
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replication helicase DnaB protein
    • Bujalowski, W., Klonowska, M.M., and Jezewska, M.J. (1994). Oligomeric structure of Escherichia coli primary replication helicase DnaB protein. J. Biol. Chem. 269, 31350-31358.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 4
    • 0016769419 scopus 로고
    • The replication time of the Escherichia coli K12 chromosome as a function of cell doubling time
    • Chandler, M., Bird, R., and Caro, L. (1975). The replication time of the Escherichia coli K12 chromosome as a function of cell doubling time. J. Mol. Biol. 94, 127-131.
    • (1975) J. Mol. Biol. , vol.94 , pp. 127-131
    • Chandler, M.1    Bird, R.2    Caro, L.3
  • 5
    • 0028863156 scopus 로고
    • DnaX-complex of Escherichia coli DNA polymerase III holoenzyme: Central role of τ in initiation complex assembly and in determining the functional asymmetry of the holoenzyme
    • Dallmann, H.G., Thimmig, R.L., and McHenry, C.S. (1995). DnaX-complex of Escherichia coli DNA polymerase III holoenzyme: central role of τ in initiation complex assembly and in determining the functional asymmetry of the holoenzyme. J. Biol. Chem. 270, 29555-29562.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29555-29562
    • Dallmann, H.G.1    Thimmig, R.L.2    McHenry, C.S.3
  • 6
    • 0014687307 scopus 로고
    • Genetic control of mutation rates in bacteriophage T4
    • Drake, J., Allen, E., Forsberg, S., Preparata, R., and Greening, E.O. (1969). Genetic control of mutation rates in bacteriophage T4. Nature 221, 1128-1131.
    • (1969) Nature , vol.221 , pp. 1128-1131
    • Drake, J.1    Allen, E.2    Forsberg, S.3    Preparata, R.4    Greening, E.O.5
  • 7
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNa that suggest a general structure for hexameric helicases
    • Egelman, E.H., Yu, X., Wild, R., Hingorani, M.M., and Patel, S.S. (1995). Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl. Acad. Sci. USA 92, 3869-3873.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 8
    • 0027250342 scopus 로고
    • A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho
    • Geiselmann, J., Wang, Y., Seifried, S.E., and von Hippel, P.H. (1993). A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho. Proc. Natl. Acad. Sci. USA 90, 7754-7758.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7754-7758
    • Geiselmann, J.1    Wang, Y.2    Seifried, S.E.3    Von Hippel, P.H.4
  • 9
    • 0022999955 scopus 로고
    • Chemical characterization and purification of the β subunit of the DNA polymerase III holoenzyme from an overproducing strain
    • Johanson, K.O., Haynes, I.E., and McHenry, C.S. (1986). Chemical characterization and purification of the β subunit of the DNA polymerase III holoenzyme from an overproducing strain. J. Biol. Chem. 261, 11460-11465.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11460-11465
    • Johanson, K.O.1    Haynes, I.E.2    McHenry, C.S.3
  • 10
    • 0030043101 scopus 로고    scopus 로고
    • τ protects β in the leading-strand polymerase complex at the replication fork
    • Kim, S., Dallmann, H.G., McHenry, C.S., and Marians, K.J. (1996). τ protects β in the leading-strand polymerase complex at the replication fork. J. Biol. Chem. 271, 4315-4318.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4315-4318
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 11
    • 0021112633 scopus 로고
    • Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III
    • LaDuca, R.J., Fay, P.J., Chuang, C., McHenry, C.S., and Bambara, R.A. (1983). Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III. Biochemistry 22, 5177-5188.
    • (1983) Biochemistry , vol.22 , pp. 5177-5188
    • LaDuca, R.J.1    Fay, P.J.2    Chuang, C.3    McHenry, C.S.4    Bambara, R.A.5
  • 12
    • 0022977660 scopus 로고
    • The Escherichia coli DnaB replication protein is a DNa helicase
    • Lebowitz, J.H., and McMacken, R. (1986). The Escherichia coli DnaB replication protein is a DNA helicase. J. Biol. Chem. 261, 4738-4748.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 13
    • 0023897674 scopus 로고
    • DNA polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites
    • Maki, H., Maki, S., and Kornberg, A. (1988). DNA polymerase III holoenzyme of Escherichia coli. IV. The holoenzyme is an asymmetric dimer with twin active sites. J. Biol. Chem. 263, 6570-6578.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6570-6578
    • Maki, H.1    Maki, S.2    Kornberg, A.3
  • 14
    • 0023952130 scopus 로고
    • DNA polymerase III holoenzyme of Escherichia coli. III. Distinctive processive polymerases reconstituted from purified subunits
    • Maki, S., and Kornberg, A. (1988). DNA polymerase III holoenzyme of Escherichia coli. III. Distinctive processive polymerases reconstituted from purified subunits. J. Biol. Chem. 263, 6561-6569.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6561-6569
    • Maki, S.1    Kornberg, A.2
  • 15
    • 0026777126 scopus 로고
    • Prokaryotic DNA replication
    • Marians, K.J. (1992). Prokaryotic DNA replication. Annu. Rev. Biochem. 61, 673-719.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 673-719
    • Marians, K.J.1
  • 16
    • 0028868621 scopus 로고
    • The φX174-type primosomal proteins: Purification and assay
    • Marians, K.J. (1995). The φX174-type primosomal proteins: purification and assay. Meth. Enzymol. 262, 507-521.
    • (1995) Meth. Enzymol. , vol.262 , pp. 507-521
    • Marians, K.J.1
  • 17
    • 0024550638 scopus 로고
    • ATP-dependent assembly of a double hexamer of SV40 Tantigen at the viral original of DNa replication
    • Mastrangelo, I.A., Hough, P.V.C., Wall, J.S., Dobson, M., Dean, F.B., and Hurwitz, J. (1989). ATP-dependent assembly of a double hexamer of SV40 Tantigen at the viral original of DNA replication. Nature 338, 658-662.
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.C.2    Wall, J.S.3    Dobson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 18
    • 0020478712 scopus 로고
    • Purification and characterization of DNa polymerase III′: Identification of τ as a subunit of the DNa polymerase III holoenzyme
    • McHenry, C.S. (1982). Purification and characterization of DNA polymerase III′: identification of τ as a subunit of the DNA polymerase III holoenzyme. J. Biol. Chem. 257, 2657-2663.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2657-2663
    • McHenry, C.S.1
  • 19
    • 0018786252 scopus 로고
    • DNA polymerase III of Escherichia coli: Purification and identification of subunits
    • McHenry, C.S., and Crow, W. (1979). DNA polymerase III of Escherichia coli: purification and identification of subunits. J. Biol. Chem. 254, 1748-1753.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1748-1753
    • McHenry, C.S.1    Crow, W.2
  • 20
    • 0017898890 scopus 로고
    • A multienzyme system for priming the replication of φX174 viral DNA
    • McMacken, R., and Kornberg, A. (1978). A multienzyme system for priming the replication of φX174 viral DNA. J. Biol. Chem. 253, 3313-3319.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3313-3319
    • McMacken, R.1    Kornberg, A.2
  • 21
    • 0022353304 scopus 로고
    • Replication of pBR322 DNA in vitro with purified proteins: Requirement for topoisomerase I in the maintenance of template specificity
    • Minden, J.S., and Marians, K.J. (1985). Replication of pBR322 DNA in vitro with purified proteins: requirement for topoisomerase I in the maintenance of template specificity. J. Biol. Chem. 260, 9316-9325.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9316-9325
    • Minden, J.S.1    Marians, K.J.2
  • 22
    • 0023646050 scopus 로고
    • The Escherichia coli preprimosome and DnaB helicase can form replication forks that move at the same rate
    • Mok, M., and Marians, K.J. (1987). The Escherichia coli preprimosome and DnaB helicase can form replication forks that move at the same rate. J. Biol. Chem. 262, 16644-16654.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16644-16654
    • Mok, M.1    Marians, K.J.2
  • 23
    • 0023646086 scopus 로고
    • Accessory proteins bind a primed template and mediate rapid recycling of DNa polymerase III holoenzyme from Escherichia coli
    • O'Donnell, M.E. (1987). Accessory proteins bind a primed template and mediate rapid recycling of DNA polymerase III holoenzyme from Escherichia coli. J. Biol. Chem. 262, 16558-16565.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16558-16565
    • O'Donnell, M.E.1
  • 24
    • 0028839775 scopus 로고
    • DnaX-complex of Escherichia coli DNa polymerase III holoenzyme: The χ-ψ complex functions by increasing the affinity of τ and γ for δ-δ′ to a physiologically relevant range
    • Olson, M.W., Dallmann, H.G., and McHenry, C.S. (1995). DnaX-complex of Escherichia coli DNA polymerase III holoenzyme: the χ-ψ complex functions by increasing the affinity of τ and γ for δ-δ′ to a physiologically relevant range. J. Biol. Chem. 270, 29570-29577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29570-29577
    • Olson, M.W.1    Dallmann, H.G.2    McHenry, C.S.3
  • 25
    • 0028899314 scopus 로고
    • Escherichia coli DNA polymerase III holoenzyme subunits α, β, and γ directly contact the prime-template
    • Reems, J.A., Wood, S., and McHenry, C.S. (1995). Escherichia coli DNA polymerase III holoenzyme subunits α, β, and γ directly contact the prime-template. J. Biol. Chem. 270, 5606-5613.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5606-5613
    • Reems, J.A.1    Wood, S.2    McHenry, C.S.3
  • 26
    • 0025988893 scopus 로고
    • Constitution of the twin polymerase of DNA polymerase III holoenzyme
    • Studwell-Vaughan, P.S., and O'Donnell, M. (1991). Constitution of the twin polymerase of DNA polymerase III holoenzyme. J. Biol. Chem. 266, 19833-19841.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19833-19841
    • Studwell-Vaughan, P.S.1    O'Donnell, M.2
  • 27
    • 0025809742 scopus 로고
    • Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme
    • Stukenberg, P.T., Studwell-Vaughan, P.S., and O'Donnell, M. (1991). Mechanism of the sliding β-clamp of DNA polymerase III holoenzyme. J. Biol. Chem. 266, 11328-11334.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    O'Donnell, M.3
  • 28
    • 0028049949 scopus 로고
    • Identification of a domain of Escherichia coli primase required for functional interaction with DnaB helicase at the replication fork
    • Tougu, K., Peng, H., and Marians, K.J. (1994). Identification of a domain of Escherichia coli primase required for functional interaction with DnaB helicase at the replication fork. J. Biol. Chem. 269, 4675-4682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 29
    • 0020364657 scopus 로고
    • Bacteriophage T4 gene 41 protein, required for the synthesis of RNa primers, is also a DNa helicase
    • Venkatesan, M., Silver, L.L., and Nossal, N.G. (1982). Bacteriophage T4 gene 41 protein, required for the synthesis of RNA primers, is also a DNA helicase. J. Biol. Chem. 257, 12426-12434.
    • (1982) J. Biol. Chem. , vol.257 , pp. 12426-12434
    • Venkatesan, M.1    Silver, L.L.2    Nossal, N.G.3
  • 30
    • 0017091688 scopus 로고
    • Mechanism of DNA elongation catalyzed by Escherichia coli DNA polymerase III, dnaZprotein, and DNA elongation factors I and III
    • Wickner, S. (1976). Mechanism of DNA elongation catalyzed by Escherichia coli DNA polymerase III, dnaZprotein, and DNA elongation factors I and III. Proc. Natl. Acad. Sci. USA 73, 3511-3515.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3511-3515
    • Wickner, S.1
  • 31
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong, I., and Lohman, T.M. (1992). Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256, 350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 32
    • 0026706674 scopus 로고
    • Coordinated leading- And lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple factors actto modulate Okazaki fragment size
    • Wu, C.A., Zechner, E.L., and Marians, K.J. (1992a). Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. I. Multiple factors actto modulate Okazaki fragment size. J. Biol. Chem. 267, 4030-4044.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4030-4044
    • Wu, C.A.1    Zechner, E.L.2    Marians, K.J.3
  • 33
    • 0026706676 scopus 로고
    • Coordinated leading- And lagging-strand synthesis at the Escherichia coli DNA replication fork. IV. Reconstitution of an asymmetric, dimeric DNA polymerase III holoenzyme
    • Wu, C.A., Zechner, E.L., Hughes, A.J., Jr., Franden, M.A., McHenry, C.S., and Marians, K.J. (1992b). Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. IV. Reconstitution of an asymmetric, dimeric DNA polymerase III holoenzyme. J. Biol. Chem. 267, 4064-4073.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4064-4073
    • Wu, C.A.1    Zechner, E.L.2    Hughes A.J., Jr.3    Franden, M.A.4    McHenry, C.S.5    Marians, K.J.6
  • 34
    • 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. (1992c). 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
  • 35
    • 0026660979 scopus 로고
    • Coordinated leading- And lagging-strand synthesis at the Escherichia coli DNa replication fork. III. a polymerase-primase interaction governs primer size
    • Zechner, E.L., Wu, C.A., and Marians, K.J. (1992). Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. III. A polymerase-primase interaction governs primer size. J. Biol. Chem. 267, 4054-4063.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4054-4063
    • Zechner, E.L.1    Wu, C.A.2    Marians, K.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.