메뉴 건너뛰기




Volumn 39, Issue 2, 2011, Pages 606-610

Helicases that underpin replication of protein-bound DNA in Escherichia coli

Author keywords

Chromosome; Genome; Recombination; Rep; Repair; UvrD

Indexed keywords

DNA; DNA POLYMERASE; DNAB HELICASE; DOUBLE STRANDED DNA; HELICASE; RNA POLYMERASE; SINGLE STRANDED DNA;

EID: 79953194151     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390606     Document Type: Review
Times cited : (18)

References (48)
  • 1
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M.R., Dillingham, M.S. and Wigley, D.B. (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76, 23-50
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 2
    • 0035868712 scopus 로고    scopus 로고
    • The DnaB.DnaC complex: A structure based on dimers assembled around an occluded channel
    • DOI 10.1093/emboj/20.6.1462
    • Barcena, M., Ruiz, T., Donate, L.E., Brown, S.E., Dixon, N.E., Radermacher, M. and Carazo, J.M. (2001) The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel. EMBO J. 20, 1462-1468 (Pubitemid 32233985)
    • (2001) EMBO Journal , vol.20 , Issue.6 , pp. 1462-1468
    • Barcena, M.1    Ruiz, T.2    Donate, L.E.3    Brown, S.E.4    Dixon, N.E.5    Radermacher, M.6    Carazo, J.M.7
  • 3
    • 71449107031 scopus 로고    scopus 로고
    • The Mcm complex: Unwinding the mechanism of a replicative helicase
    • Bochman, M.L. and Schwacha, A. (2009) The Mcm complex: unwinding the mechanism of a replicative helicase. Microbiol. Mol. Biol. Rev. 73, 652-683
    • (2009) Microbiol. Mol. Biol. Rev. , vol.73 , pp. 652-683
    • Bochman, M.L.1    Schwacha, A.2
  • 4
    • 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
  • 5
    • 0034636979 scopus 로고    scopus 로고
    • The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase
    • Kaplan, D.L. (2000) The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase. J. Mol. Biol. 301, 285-299
    • (2000) J. Mol. Biol. , vol.301 , pp. 285-299
    • Kaplan, D.L.1
  • 6
    • 74049108938 scopus 로고    scopus 로고
    • DNA structure specificity conferred on a replicative helicase by its loader
    • Gupta, M.K., Atkinson, J. and McGlynn, P. (2010) DNA structure specificity conferred on a replicative helicase by its loader. J. Biol. Chem. 285, 979-987
    • (2010) J. Biol. Chem. , vol.285 , pp. 979-987
    • Gupta, M.K.1    Atkinson, J.2    McGlynn, P.3
  • 7
    • 67649862225 scopus 로고    scopus 로고
    • Replication fork reversal and the maintenance of genome stability
    • Atkinson, J. and McGlynn, P. (2009) Replication fork reversal and the maintenance of genome stability. Nucleic Acids Res. 37, 3475-3492
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3475-3492
    • Atkinson, J.1    McGlynn, P.2
  • 8
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl, T. and Wood, R.D. (1999) Quality control by DNA repair. Science 286, 1897-1905 (Pubitemid 129515891)
    • (1999) Science , vol.286 , Issue.5446 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 9
    • 33947432388 scopus 로고    scopus 로고
    • Replication fork stalling at natural impediments
    • Mirkin, E.V. and Mirkin, S.M. (2007) Replication fork stalling at natural impediments. Microbiol. Mol. Biol. Rev. 71, 13-35
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 13-35
    • Mirkin, E.V.1    Mirkin, S.M.2
  • 10
    • 0024276903 scopus 로고
    • When polymerases collide: Replication and the transcriptional organization of the E. coli chromosome
    • Brewer, B.J. (1988) When polymerases collide: replication and the transcriptional organization of the E. coli chromosome. Cell 53, 679-686
    • (1988) Cell , vol.53 , pp. 679-686
    • Brewer, B.J.1
  • 11
    • 24044476230 scopus 로고    scopus 로고
    • Transcription arrest at DNA damage sites
    • Tornaletti, S. (2005) Transcription arrest at DNA damage sites. Mutat. Res. 577, 131-145
    • (2005) Mutat. Res. , vol.577 , pp. 131-145
    • Tornaletti, S.1
  • 12
    • 0034737294 scopus 로고    scopus 로고
    • Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression
    • McGlynn, P. and Lloyd, R.G. (2000) Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression. Cell 101, 35-45
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.G.2
  • 13
    • 33644619706 scopus 로고    scopus 로고
    • Prokaryotic nucleotide excision repair: The UvrABC system
    • Truglio, J.J., Croteau, D.L., Van Houten, B. and Kisker, C. (2006) Prokaryotic nucleotide excision repair: the UvrABC system. Chem. Rev. 106, 233-252
    • (2006) Chem. Rev. , vol.106 , pp. 233-252
    • Truglio, J.J.1    Croteau, D.L.2    Van Houten, B.3    Kisker, C.4
  • 14
    • 0014432520 scopus 로고
    • Discontinuities in the DNA synthesized in an excision-defective strain of Escherichia coli following ultraviolet irradiation
    • Rupp, W.D. and Howard-Flanders, P. (1968) Discontinuities in the DNA synthesized in an excision-defective strain of Escherichia coli following ultraviolet irradiation. J. Mol. Biol. 31, 291-304
    • (1968) J. Mol. Biol. , vol.31 , pp. 291-304
    • Rupp, W.D.1    Howard-Flanders, P.2
  • 15
    • 34548507222 scopus 로고    scopus 로고
    • Replisome fate upon encountering a leading strand block and clearance from DNA by recombination proteins
    • McInerney, P. and O'Donnell, M. (2007) Replisome fate upon encountering a leading strand block and clearance from DNA by recombination proteins. J. Biol. Chem. 282, 25903-25916
    • (2007) J. Biol. Chem. , vol.282 , pp. 25903-25916
    • McInerney, P.1    O'Donnell, M.2
  • 16
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller, R.C. and Marians, K.J. (2006) Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7, 932-943
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 17
    • 0030852247 scopus 로고    scopus 로고
    • The DNA replication protein PriA and the recombination protein RecG bind D-loops
    • McGlynn, P., Al-Deib, A.A., Liu, J., Marians, K.J. and Lloyd, R.G. (1997) The DNA replication protein PriA and the recombination protein RecG bind D-loops. J. Mol. Biol. 270, 212-221
    • (1997) J. Mol. Biol. , vol.270 , pp. 212-221
    • McGlynn, P.1    Al-Deib, A.A.2    Liu, J.3    Marians, K.J.4    Lloyd, R.G.5
  • 18
    • 0033616683 scopus 로고    scopus 로고
    • Replication fork assembly at recombination intermediates is required for bacterial growth
    • Liu, J., Xu, L., Sandler, S.J. and Marians, K.J. (1999) Replication fork assembly at recombination intermediates is required for bacterial growth. Proc. Natl. Acad. Sci. U.S.A. 96, 3552-3555
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 3552-3555
    • Liu, J.1    Xu, L.2    Sandler, S.J.3    Marians, K.J.4
  • 19
    • 0034123356 scopus 로고    scopus 로고
    • Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12
    • Sandler, S.J. (2000) Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12. Genetics 155, 487-497
    • (2000) Genetics , vol.155 , pp. 487-497
    • Sandler, S.J.1
  • 20
    • 14644415982 scopus 로고    scopus 로고
    • The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart
    • DOI 10.1016/j.molcel.2005.01.019
    • Heller, R.C. and Marians, K.J. (2005) The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart. Mol. Cell 17, 733-743 (Pubitemid 40320922)
    • (2005) Molecular Cell , vol.17 , Issue.5 , pp. 733-743
    • Heller, R.C.1    Marians, K.J.2
  • 21
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • DOI 10.1093/nar/gkh980
    • Cadman, C.J. and McGlynn, P. (2004) PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 32, 6378-6387 (Pubitemid 40202096)
    • (2004) Nucleic Acids Research , vol.32 , Issue.21 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 22
    • 0028810659 scopus 로고
    • Insertion of inverted Ter sites into the terminus region of the Escherichia coli chromosome delays completion of DNA replication and disrupts the cell cycle
    • Sharma, B. and Hill, T.M. (1995) Insertion of inverted Ter sites into the terminus region of the Escherichia coli chromosome delays completion of DNA replication and disrupts the cell cycle. Mol. Microbiol. 18, 45-61
    • (1995) Mol. Microbiol. , vol.18 , pp. 45-61
    • Sharma, B.1    Hill, T.M.2
  • 23
    • 33751003256 scopus 로고    scopus 로고
    • Replication fork blockage by transcription factor-DNA complexes in Escherichia coli
    • DOI 10.1093/nar/gkl682
    • Payne, B.T., van Knippenberg, I.C., Bell, H., Filipe, S.R., Sherratt, D.J. and McGlynn, P. (2006) Replication fork blockage by transcription factor-DNA complexes in Escherichia coli. Nucleic Acids Res. 34, 5194-5202 (Pubitemid 44742484)
    • (2006) Nucleic Acids Research , vol.34 , Issue.18 , pp. 5194-5202
    • Payne, B.T.I.1    Van Knippenberg, I.C.2    Bell, H.3    Filipe, S.R.4    Sherratt, D.J.5    McGlynn, P.6
  • 24
    • 0037099681 scopus 로고    scopus 로고
    • Replication fork collapse at replication terminator sequences
    • DOI 10.1093/emboj/cdf369
    • Bidnenko, V., Ehrlich, S.D. and Michel, B. (2002) Replication fork collapse at replication terminator sequences. EMBO J. 21, 3898-3907 (Pubitemid 34787062)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3898-3907
    • Bidnenko, V.1    Ehrlich, S.D.2    Michel, B.3
  • 25
    • 0031892179 scopus 로고    scopus 로고
    • Role of the core DNA polymerase III subunits at the replication fork. α is the only subunit required for processive replication
    • Marians, K.J., Hiasa, H., Kim, D.R. and McHenry, C.S. (1998) Role of the core DNA polymerase III subunits at the replication fork. α is the only subunit required for processive replication. J. Biol. Chem. 273, 2452-2457
    • (1998) J. Biol. Chem. , vol.273 , pp. 2452-2457
    • Marians, K.J.1    Hiasa, H.2    Kim, D.R.3    McHenry, C.S.4
  • 26
    • 47049124441 scopus 로고    scopus 로고
    • Replication forks blocked by protein-DNA complexes have limited stability in vitro
    • McGlynn, P. and Guy, C.P. (2008) Replication forks blocked by protein-DNA complexes have limited stability in vitro. J. Mol. Biol. 381, 249-255
    • (2008) J. Mol. Biol. , vol.381 , pp. 249-255
    • McGlynn, P.1    Guy, C.P.2
  • 27
    • 75749150810 scopus 로고    scopus 로고
    • Direct restart of a replication fork stalled by a head-on RNA polymerase
    • Pomerantz, R.T. and O'Donnell, M. (2010) Direct restart of a replication fork stalled by a head-on RNA polymerase. Science 327, 590-592
    • (2010) Science , vol.327 , pp. 590-592
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 28
    • 0027515187 scopus 로고
    • A gene with specific and global effects on recombination of sequences from tandemly repeated genes in Saccharomyces cerevisiae
    • Keil, R.L. and McWilliams, A.D. (1993) A gene with specific and global effects on recombination of sequences from tandemly repeated genes in Saccharomyces cerevisiae. Genetics 135, 711-718 (Pubitemid 23324815)
    • (1993) Genetics , vol.135 , Issue.3 , pp. 711-718
    • Keil, R.L.1    McWilliams, A.D.2
  • 29
    • 0348047594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Helicase Rrm3p Facilitates Replication Past Nonhistone Protein-DNA Complexes
    • DOI 10.1016/S1097-2765(03)00456-8
    • Ivessa, A.S., Lenzmeier, B.A., Bessler, J.B., Goudsouzian, L.K., Schnakenberg, S.L. and Zakian, V.A. (2003) The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes. Mol. Cell 12, 1525-1536 (Pubitemid 38037020)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1525-1536
    • Ivessa, A.S.1    Lenzmeier, B.A.2    Bessler, J.B.3    Goudsouzian, L.K.4    Schnakenberg, S.L.5    Zakian, V.A.6
  • 30
    • 67449113551 scopus 로고    scopus 로고
    • Highly transcribed RNA polymerase II genes are impediments to replication fork progression in Saccharomyces cerevisiae
    • Azvolinsky, A., Giresi, P.G., Lieb, J.D. and Zakian, V.A. (2009) Highly transcribed RNA polymerase II genes are impediments to replication fork progression in Saccharomyces cerevisiae. Mol. Cell 34, 722-734
    • (2009) Mol. Cell , vol.34 , pp. 722-734
    • Azvolinsky, A.1    Giresi, P.G.2    Lieb, J.D.3    Zakian, V.A.4
  • 31
    • 0016710698 scopus 로고
    • The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains
    • Lane, H.E. and Denhardt, D.T. (1975) The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains. J. Mol. Biol. 97, 99-112
    • (1975) J. Mol. Biol. , vol.97 , pp. 99-112
    • Lane, H.E.1    Denhardt, D.T.2
  • 32
    • 0023405041 scopus 로고
    • The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels
    • Colasanti, J. and Denhardt, D.T. (1987) The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels. Mol. Gen. Genet. 209, 382-390
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 382-390
    • Colasanti, J.1    Denhardt, D.T.2
  • 33
    • 0014713029 scopus 로고
    • Characterization of REP- Mutants and their interaction with P2 phage
    • Calendar, R., Lindqvist, B., Sironi, G. and Clark, A.J. (1970) Characterization of REP- mutants and their interaction with P2 phage. Virology 40, 72-83
    • (1970) Virology , vol.40 , pp. 72-83
    • Calendar, R.1    Lindqvist, B.2    Sironi, G.3    Clark, A.J.4
  • 34
    • 0028786478 scopus 로고
    • Lethality of rep recB and rep recC double mutants of Escherichia coli
    • Uzest, M., Ehrlich, S.D. and Michel, B. (1995) Lethality of rep recB and rep recC double mutants of Escherichia coli. Mol. Microbiol. 17, 1177-1188
    • (1995) Mol. Microbiol. , vol.17 , pp. 1177-1188
    • Uzest, M.1    Ehrlich, S.D.2    Michel, B.3
  • 35
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • DOI 10.1093/emboj/16.2.430
    • Michel, B., Ehrlich, S.D. and Uzest, M. (1997) DNA double-strand breaks caused by replication arrest. EMBO J. 16, 430-438 (Pubitemid 27049398)
    • (1997) EMBO Journal , vol.16 , Issue.2 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 36
    • 26644472197 scopus 로고    scopus 로고
    • Unwinding of the nascent lagging strand by Rep and PriA enables the direct restart of stalled replication forks
    • Heller, R.C. and Marians, K.J. (2005) Unwinding of the nascent lagging strand by Rep and PriA enables the direct restart of stalled replication forks. J. Biol. Chem. 280, 34143-34151
    • (2005) J. Biol. Chem. , vol.280 , pp. 34143-34151
    • Heller, R.C.1    Marians, K.J.2
  • 39
    • 75649142564 scopus 로고    scopus 로고
    • The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo
    • Boubakri, H., de Septenville, A.L., Viguera, E. and Michel, B. (2010) The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo. EMBO J. 29, 145-157
    • (2010) EMBO J. , vol.29 , pp. 145-157
    • Boubakri, H.1    De Septenville, A.L.2    Viguera, E.3    Michel, B.4
  • 40
    • 34249941504 scopus 로고    scopus 로고
    • Avoiding and resolving conflicts between DNA replication and transcription
    • DOI 10.1016/j.dnarep.2007.02.017, PII S1568786407000687, Replication Fork Repair Processes
    • Rudolph, C.J., Dhillon, P., Moore, T. and Lloyd, R.G. (2007) Avoiding and resolving conflicts between DNA replication and transcription. DNA Repair 6, 981-993 (Pubitemid 46880478)
    • (2007) DNA Repair , vol.6 , Issue.7 , pp. 981-993
    • Rudolph, C.J.1    Dhillon, P.2    Moore, T.3    Lloyd, R.G.4
  • 41
    • 77954371207 scopus 로고    scopus 로고
    • RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases
    • Baharoglu, Z., Lestini, R., Duigou, S. and Michel, B. (2010) RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases. Mol. Microbiol. 77, 324-336
    • (2010) Mol. Microbiol. , vol.77 , pp. 324-336
    • Baharoglu, Z.1    Lestini, R.2    Duigou, S.3    Michel, B.4
  • 42
    • 0041344536 scopus 로고    scopus 로고
    • Characterization of the DNA damage-inducible helicase DinG from Escherichia coli
    • Voloshin, O.N., Vanevski, F., Khil, P.P. and Camerini-Otero, R.D. (2003) Characterization of the DNA damage-inducible helicase DinG from Escherichia coli. J. Biol. Chem. 278, 28284-28293
    • (2003) J. Biol. Chem. , vol.278 , pp. 28284-28293
    • Voloshin, O.N.1    Vanevski, F.2    Khil, P.P.3    Camerini-Otero, R.D.4
  • 43
    • 0022580659 scopus 로고
    • RNase H-defective mutants of Escherichia coli
    • Kogoma, T. (1986) RNase H-defective mutants of Escherichia coli. J. Bacteriol. 166, 361-363
    • (1986) J. Bacteriol. , vol.166 , pp. 361-363
    • Kogoma, T.1
  • 44
    • 33751237066 scopus 로고    scopus 로고
    • The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes
    • DOI 10.1101/gad.1478906
    • Azvolinsky, A., Dunaway, S., Torres, J.Z., Bessler, J.B. and Zakian, V.A. (2006) The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes. Genes Dev. 20, 3104-3116 (Pubitemid 44790626)
    • (2006) Genes and Development , vol.20 , Issue.22 , pp. 3104-3116
    • Azvolinsky, A.1    Dunaway, S.2    Torres, J.Z.3    Bessler, J.B.4    Zakian, V.A.5
  • 45
    • 0037160099 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RRM3, a 5′ to 3′ DNA helicase, physically interacts with proliferating cell nuclear antigen
    • Schmidt, K.H., Derry, K.L. and Kolodner, R.D. (2002) Saccharomyces cerevisiae RRM3, a 5′ to 3′ DNA helicase, physically interacts with proliferating cell nuclear antigen. J. Biol. Chem. 277, 45331-45337
    • (2002) J. Biol. Chem. , vol.277 , pp. 45331-45337
    • Schmidt, K.H.1    Derry, K.L.2    Kolodner, R.D.3
  • 46
    • 0036606186 scopus 로고    scopus 로고
    • Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA
    • DOI 10.1101/gad.982902
    • Ivessa, A.S., Zhou, J.Q., Schulz, V.P., Monson, E.K. and Zakian, V.A. (2002) Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA. Genes Dev. 16, 1383-1396 (Pubitemid 34615091)
    • (2002) Genes and Development , vol.16 , Issue.11 , pp. 1383-1396
    • Ivessa, A.S.1    Zhou, J.-Q.2    Schulz, V.P.3    Monson, E.K.4    Zakian, V.A.5
  • 47
    • 67649766870 scopus 로고    scopus 로고
    • Transcription factories: Gene expression in unions? Nat
    • Sutherland, H. and Bickmore, W.A. (2009) Transcription factories: gene expression in unions? Nat. Rev. Genet. 10, 457-466
    • (2009) Rev. Genet. , vol.10 , pp. 457-466
    • Sutherland, H.1    Bickmore, W.A.2
  • 48
    • 70450153952 scopus 로고    scopus 로고
    • Increased rate of human mutations where DNA and RNA polymerases collide
    • Jorgensen, F.G. and Schierup, M.H. (2009) Increased rate of human mutations where DNA and RNA polymerases collide. Trends Genet. 25, 523-527
    • (2009) Trends Genet. , vol.25 , pp. 523-527
    • Jorgensen, F.G.1    Schierup, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.