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Volumn 9, Issue 3, 2010, Pages 210-223

Is RecG a general guardian of the bacterial genome?

Author keywords

Holliday junctions; Pathological replication; Replication fork collision; Stable DNA replication

Indexed keywords

HELICASE; PRIA HELICASE; RECG HELICASE; UNCLASSIFIED DRUG;

EID: 76749090152     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2009.12.014     Document Type: Review
Times cited : (75)

References (138)
  • 1
    • 0030582737 scopus 로고    scopus 로고
    • The RecG branch migration protein of Escherichia coli dissociates R-loops
    • Vincent S.D., Mahdi A.A., and Lloyd R.G. The RecG branch migration protein of Escherichia coli dissociates R-loops. J. Mol. Biol. 264 (1996) 713-721
    • (1996) J. Mol. Biol. , vol.264 , pp. 713-721
    • Vincent, S.D.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 2
    • 0031028107 scopus 로고    scopus 로고
    • ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase
    • Fukuoh A., Iwasaki H., Ishioka K., and Shinagawa H. ATP-dependent resolution of R-loops at the ColE1 replication origin by Escherichia coli RecG protein, a Holliday junction-specific helicase. EMBO J. 16 (1997) 203-209
    • (1997) EMBO J. , vol.16 , pp. 203-209
    • Fukuoh, A.1    Iwasaki, H.2    Ishioka, K.3    Shinagawa, H.4
  • 3
    • 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. The DNA replication protein PriA and the recombination protein RecG bind D-loops. J. Mol. Biol. 270 (1997) 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
  • 4
    • 0032584598 scopus 로고    scopus 로고
    • Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli
    • Whitby M.C., and Lloyd R.G. Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. J. Biol. Chem. 273 (1998) 19729-19739
    • (1998) J. Biol. Chem. , vol.273 , pp. 19729-19739
    • Whitby, M.C.1    Lloyd, R.G.2
  • 5
    • 55449115425 scopus 로고    scopus 로고
    • Comparative and evolutionary analysis of the bacterial homologous recombination systems
    • Rocha E.P., Cornet E., and Michel B. Comparative and evolutionary analysis of the bacterial homologous recombination systems. PLoS Genet. 1 (2005) e15
    • (2005) PLoS Genet. , vol.1
    • Rocha, E.P.1    Cornet, E.2    Michel, B.3
  • 6
    • 0032873606 scopus 로고    scopus 로고
    • Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA
    • Sharples G.J., Ingleston S.M., and Lloyd R.G. Holliday junction processing in bacteria: insights from the evolutionary conservation of RuvABC, RecG, and RusA. J. Bacteriol. 181 (1999) 5543-5550
    • (1999) J. Bacteriol. , vol.181 , pp. 5543-5550
    • Sharples, G.J.1    Ingleston, S.M.2    Lloyd, R.G.3
  • 7
    • 0026009412 scopus 로고
    • Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG
    • Lloyd R.G. Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG. J. Bacteriol. 173 (1991) 5414-5418
    • (1991) J. Bacteriol. , vol.173 , pp. 5414-5418
    • Lloyd, R.G.1
  • 8
    • 0025924538 scopus 로고
    • Genetic analysis of the recG locus of Escherichia coli K-12 and of its role in recombination and DNA repair
    • Lloyd R.G., and Buckman C. Genetic analysis of the recG locus of Escherichia coli K-12 and of its role in recombination and DNA repair. J. Bacteriol. 173 (1991) 1004-1011
    • (1991) J. Bacteriol. , vol.173 , pp. 1004-1011
    • Lloyd, R.G.1    Buckman, C.2
  • 9
    • 0035902474 scopus 로고    scopus 로고
    • Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant
    • McCool J.D., and Sandler S.J. Effects of mutations involving cell division, recombination, and chromosome dimer resolution on a priA2::kan mutant. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 8203-8210
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8203-8210
    • McCool, J.D.1    Sandler, S.J.2
  • 10
    • 0036184234 scopus 로고    scopus 로고
    • Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities
    • Gregg A.V., McGlynn P., Jaktaji R.P., and Lloyd R.G. Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities. Mol. Cell 9 (2002) 241-251
    • (2002) Mol. Cell , vol.9 , pp. 241-251
    • Gregg, A.V.1    McGlynn, P.2    Jaktaji, R.P.3    Lloyd, R.G.4
  • 11
    • 0030737725 scopus 로고    scopus 로고
    • Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription
    • Kogoma T. Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription. Microbiol. Mol. Biol. Rev. 61 (1997) 212-238
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 212-238
    • Kogoma, T.1
  • 12
    • 0029026201 scopus 로고
    • Escherichia coli RecG and RecA proteins in R-loop formation
    • Hong X., Cadell G.W., and Kogoma T. Escherichia coli RecG and RecA proteins in R-loop formation. EMBO J. 14 (1995) 2385-2392
    • (1995) EMBO J. , vol.14 , pp. 2385-2392
    • Hong, X.1    Cadell, G.W.2    Kogoma, T.3
  • 13
    • 67651205866 scopus 로고    scopus 로고
    • Pathological replication in cells lacking RecG DNA translocase
    • Rudolph C.J., Upton A.L., Harris L., and Lloyd R.G. Pathological replication in cells lacking RecG DNA translocase. Mol. Microbiol. 73 (2009) 352-366
    • (2009) Mol. Microbiol. , vol.73 , pp. 352-366
    • Rudolph, C.J.1    Upton, A.L.2    Harris, L.3    Lloyd, R.G.4
  • 15
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • McGlynn P., and Lloyd R.G. Recombinational repair and restart of damaged replication forks. Nat. Rev. Mol. Cell Biol. 3 (2002) 859-870
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 16
    • 0036683338 scopus 로고    scopus 로고
    • Genome stability and the processing of damaged replication forks by RecG
    • McGlynn P., and Lloyd R.G. Genome stability and the processing of damaged replication forks by RecG. Trends Genet. 18 (2002) 413-419
    • (2002) Trends Genet. , vol.18 , pp. 413-419
    • McGlynn, P.1    Lloyd, R.G.2
  • 17
    • 67649862225 scopus 로고    scopus 로고
    • Replication fork reversal and the maintenance of genome stability
    • Atkinson J., and McGlynn P. Replication fork reversal and the maintenance of genome stability. Nucleic Acids Res. 37 (2009) 3475-3492
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3475-3492
    • Atkinson, J.1    McGlynn, P.2
  • 18
    • 27144433837 scopus 로고    scopus 로고
    • Interplay between DNA replication and recombination in prokaryotes
    • Kreuzer K.N. Interplay between DNA replication and recombination in prokaryotes. Annu. Rev. Microbiol. 59 (2005) 43-67
    • (2005) Annu. Rev. Microbiol. , vol.59 , pp. 43-67
    • Kreuzer, K.N.1
  • 19
    • 0035679232 scopus 로고    scopus 로고
    • Recombinational DNA repair of damaged replication forks in Escherichia coli: questions
    • Cox M.M. Recombinational DNA repair of damaged replication forks in Escherichia coli: questions. Annu. Rev. Genet. 35 (2001) 53-82
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 53-82
    • Cox, M.M.1
  • 20
    • 33750102798 scopus 로고    scopus 로고
    • Facing stalled replication forks: the intricacies of doing the right thing
    • Lankenau D.-H. (Ed), Springer, Berlin, Heidelberg
    • Rudolph C., Schürer K.A., and Kramer W. Facing stalled replication forks: the intricacies of doing the right thing. In: Lankenau D.-H. (Ed). Genome Integrity: Facets and Perspectives (2006), Springer, Berlin, Heidelberg 105-152
    • (2006) Genome Integrity: Facets and Perspectives , pp. 105-152
    • Rudolph, C.1    Schürer, K.A.2    Kramer, W.3
  • 21
    • 70449560624 scopus 로고    scopus 로고
    • Replication fork collisions cause pathological chromosomal amplification in cells lacking RecG DNA translocase
    • Rudolph C.J., Upton A.L., and Lloyd R.G. Replication fork collisions cause pathological chromosomal amplification in cells lacking RecG DNA translocase. Mol. Microbiol. 74 (2009) 940-955
    • (2009) Mol. Microbiol. , vol.74 , pp. 940-955
    • Rudolph, C.J.1    Upton, A.L.2    Lloyd, R.G.3
  • 22
    • 56749098227 scopus 로고    scopus 로고
    • The replication fork trap and termination of chromosome replication
    • Duggin I.G., Wake R.G., Bell S.D., and Hill T.M. The replication fork trap and termination of chromosome replication. Mol. Microbiol. 70 (2008) 1323-1333
    • (2008) Mol. Microbiol. , vol.70 , pp. 1323-1333
    • Duggin, I.G.1    Wake, R.G.2    Bell, S.D.3    Hill, T.M.4
  • 23
    • 33947432388 scopus 로고    scopus 로고
    • Replication fork stalling at natural impediments
    • Mirkin E.V., and Mirkin S.M. Replication fork stalling at natural impediments. Microbiol. Mol. Biol. Rev. 71 (2007) 13-35
    • (2007) Microbiol. Mol. Biol. Rev. , vol.71 , pp. 13-35
    • Mirkin, E.V.1    Mirkin, S.M.2
  • 24
    • 4544221279 scopus 로고    scopus 로고
    • Regulation of early events in chromosome replication
    • Diffley J. Regulation of early events in chromosome replication. Curr. Biol. 14 (2004) R778-R786
    • (2004) Curr. Biol. , vol.14
    • Diffley, J.1
  • 26
    • 52549115459 scopus 로고    scopus 로고
    • Replication licensing and cancer-a fatal entanglement?
    • Blow J.J., and Gillespie P.J. Replication licensing and cancer-a fatal entanglement?. Nat. Rev. Cancer 8 (2008) 799-806
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 799-806
    • Blow, J.J.1    Gillespie, P.J.2
  • 27
    • 33750472654 scopus 로고    scopus 로고
    • Deregulated replication licensing causes DNA fragmentation consistent with head-to-tail fork collision
    • Davidson I.F., Li A., and Blow J.J. Deregulated replication licensing causes DNA fragmentation consistent with head-to-tail fork collision. Mol. Cell 24 (2006) 433-443
    • (2006) Mol. Cell , vol.24 , pp. 433-443
    • Davidson, I.F.1    Li, A.2    Blow, J.J.3
  • 28
    • 0034574441 scopus 로고    scopus 로고
    • Limiting DNA replication to once and only once
    • Boye E., Lobner-Olesen A., and Skarstad K. Limiting DNA replication to once and only once. EMBO Rep. 1 (2000) 479-483
    • (2000) EMBO Rep. , vol.1 , pp. 479-483
    • Boye, E.1    Lobner-Olesen, A.2    Skarstad, K.3
  • 29
    • 38949213341 scopus 로고    scopus 로고
    • Once in a lifetime: strategies for preventing re-replication in prokaryotic and eukaryotic cells
    • Nielsen O., and Lobner-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    Lobner-Olesen, A.2
  • 30
    • 0942290452 scopus 로고    scopus 로고
    • Hyperinitiation of DNA replication in Escherichia coli leads to replication fork collapse and inviability
    • Simmons L.A., Breier A.M., Cozzarelli N.R., and Kaguni J.M. Hyperinitiation of DNA replication in Escherichia coli leads to replication fork collapse and inviability. Mol. Microbiol. 51 (2004) 349-358
    • (2004) Mol. Microbiol. , vol.51 , pp. 349-358
    • Simmons, L.A.1    Breier, A.M.2    Cozzarelli, N.R.3    Kaguni, J.M.4
  • 31
    • 42049099692 scopus 로고    scopus 로고
    • The great divide: coordinating cell cycle events during bacterial growth and division
    • Haeusser D.P., and Levin P.A. The great divide: coordinating cell cycle events during bacterial growth and division. Curr. Opin. Microbiol. 11 (2008) 94-99
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 94-99
    • Haeusser, D.P.1    Levin, P.A.2
  • 32
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • Messer W. The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol. Rev. 26 (2002) 355-374
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 355-374
    • Messer, W.1
  • 33
    • 33745260902 scopus 로고    scopus 로고
    • A molecular mousetrap determines polarity of termination of DNA replication in E. coli
    • Mulcair M.D., Schaeffer P.M., Oakley A.J., Cross H.F., Neylon C., Hill T.M., and Dixon N.E. A molecular mousetrap determines polarity of termination of DNA replication in E. coli. Cell 125 (2006) 1309-1319
    • (2006) Cell , vol.125 , pp. 1309-1319
    • Mulcair, M.D.1    Schaeffer, P.M.2    Oakley, A.J.3    Cross, H.F.4    Neylon, C.5    Hill, T.M.6    Dixon, N.E.7
  • 34
    • 24944550999 scopus 로고    scopus 로고
    • Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-ter complex
    • Neylon C., Kralicek A.V., Hill T.M., and Dixon N.E. Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-ter complex. Microbiol. Mol. Biol. Rev. 69 (2005) 501-526
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 501-526
    • Neylon, C.1    Kralicek, A.V.2    Hill, T.M.3    Dixon, N.E.4
  • 36
    • 33745743449 scopus 로고    scopus 로고
    • Tracking of controlled Escherichia coli replication fork stalling and restart at repressor-bound DNA in vivo
    • Possoz C., Filipe S.R., Grainge I., and Sherratt D.J. Tracking of controlled Escherichia coli replication fork stalling and restart at repressor-bound DNA in vivo. EMBO J. 25 (2006) 2596-2604
    • (2006) EMBO J. , vol.25 , pp. 2596-2604
    • Possoz, C.1    Filipe, S.R.2    Grainge, I.3    Sherratt, D.J.4
  • 37
    • 0037099681 scopus 로고    scopus 로고
    • Replication fork collapse at replication terminator sequences
    • Bidnenko V., Ehrlich S.D., and Michel B. Replication fork collapse at replication terminator sequences. EMBO J. 21 (2002) 3898-3907
    • (2002) EMBO J. , vol.21 , pp. 3898-3907
    • Bidnenko, V.1    Ehrlich, S.D.2    Michel, B.3
  • 38
    • 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. 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 (1995) 45-61
    • (1995) Mol. Microbiol. , vol.18 , pp. 45-61
    • Sharma, B.1    Hill, T.M.2
  • 39
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller R.C., and Marians K.J. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7 (2006) 932-943
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 41
    • 37249025795 scopus 로고    scopus 로고
    • Dormant origins licensed by excess Mcm2-7 are required for human cells to survive replicative stress
    • Ge X.Q., Jackson D.A., and Blow J.J. Dormant origins licensed by excess Mcm2-7 are required for human cells to survive replicative stress. Genes Dev. 21 (2007) 3331-3341
    • (2007) Genes Dev. , vol.21 , pp. 3331-3341
    • Ge, X.Q.1    Jackson, D.A.2    Blow, J.J.3
  • 42
    • 0024276903 scopus 로고
    • When polymerases collide: replication and the transcriptional organization of the E. coli chromosome
    • Brewer B.J. When polymerases collide: replication and the transcriptional organization of the E. coli chromosome. Cell 53 (1988) 679-686
    • (1988) Cell , vol.53 , pp. 679-686
    • Brewer, B.J.1
  • 43
    • 0026733965 scopus 로고
    • Consequences of replication fork movement through transcription units in vivo
    • French S. Consequences of replication fork movement through transcription units in vivo. Science 258 (1992) 1362-1365
    • (1992) Science , vol.258 , pp. 1362-1365
    • French, S.1
  • 44
    • 12844265439 scopus 로고    scopus 로고
    • Mechanisms of transcription-replication collisions in bacteria
    • Mirkin E.V., and Mirkin S.M. Mechanisms of transcription-replication collisions in bacteria. Mol. Cell. Biol. 25 (2005) 888-895
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 888-895
    • Mirkin, E.V.1    Mirkin, S.M.2
  • 46
    • 0032417093 scopus 로고    scopus 로고
    • Base composition skews, replication orientation, and gene orientation in 12 prokaryote genomes
    • McLean M.J., Wolfe K.H., and Devine K.M. Base composition skews, replication orientation, and gene orientation in 12 prokaryote genomes. J. Mol. Evol. 47 (1998) 691-696
    • (1998) J. Mol. Evol. , vol.47 , pp. 691-696
    • McLean, M.J.1    Wolfe, K.H.2    Devine, K.M.3
  • 47
    • 34249941504 scopus 로고    scopus 로고
    • Avoiding and resolving conflicts between DNA replication and transcription
    • Rudolph C.J., Dhillon P., Moore T., and Lloyd R.G. Avoiding and resolving conflicts between DNA replication and transcription. DNA Repair (Amst.) 6 (2007) 981-993
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 981-993
    • Rudolph, C.J.1    Dhillon, P.2    Moore, T.3    Lloyd, R.G.4
  • 48
    • 0028908039 scopus 로고
    • Head-on collision between a DNA replication apparatus and RNA polymerase transcription complex
    • Liu B., and Alberts B.M. Head-on collision between a DNA replication apparatus and RNA polymerase transcription complex. Science 267 (1995) 1131-1137
    • (1995) Science , vol.267 , pp. 1131-1137
    • Liu, B.1    Alberts, B.M.2
  • 49
    • 0036965964 scopus 로고    scopus 로고
    • DNA knotting caused by head-on collision of transcription and replication
    • Olavarrieta L., Hernandez P., Krimer D.B., and Schvartzman J.B. DNA knotting caused by head-on collision of transcription and replication. J. Mol. Biol. 322 (2002) 1-6
    • (2002) J. Mol. Biol. , vol.322 , pp. 1-6
    • Olavarrieta, L.1    Hernandez, P.2    Krimer, D.B.3    Schvartzman, J.B.4
  • 50
    • 34248394295 scopus 로고    scopus 로고
    • Genome-wide coorientation of replication and transcription reduces adverse effects on replication in Bacillus subtilis
    • Wang J.D., Berkmen M.B., and Grossman A.D. Genome-wide coorientation of replication and transcription reduces adverse effects on replication in Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 5608-5613
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 5608-5613
    • Wang, J.D.1    Berkmen, M.B.2    Grossman, A.D.3
  • 51
    • 62049085766 scopus 로고    scopus 로고
    • Termination structures in the Escherichia coli chromosome replication fork trap
    • Duggin I.G., and Bell S.D. Termination structures in the Escherichia coli chromosome replication fork trap. J. Mol. Biol. 387 (2009) 532-539
    • (2009) J. Mol. Biol. , vol.387 , pp. 532-539
    • Duggin, I.G.1    Bell, S.D.2
  • 52
    • 0035963338 scopus 로고    scopus 로고
    • Multiple pathways cooperate in the suppression of genome instability in Saccharomyces cerevisiae
    • Myung K., Chen C., and Kolodner R.D. Multiple pathways cooperate in the suppression of genome instability in Saccharomyces cerevisiae. Nature 411 (2001) 1073-1076
    • (2001) Nature , vol.411 , pp. 1073-1076
    • Myung, K.1    Chen, C.2    Kolodner, R.D.3
  • 53
    • 33947327048 scopus 로고    scopus 로고
    • Replication fork stalling and cell cycle arrest in UV-irradiated Escherichia coli
    • Rudolph C.J., Upton A.L., and Lloyd R.G. Replication fork stalling and cell cycle arrest in UV-irradiated Escherichia coli. Genes Dev. 21 (2007) 668-681
    • (2007) Genes Dev. , vol.21 , pp. 668-681
    • Rudolph, C.J.1    Upton, A.L.2    Lloyd, R.G.3
  • 54
    • 48149112447 scopus 로고    scopus 로고
    • Maintaining replication fork integrity in UV-irradiated Escherichia coli cells
    • Rudolph C.J., Upton A.L., and Lloyd R.G. Maintaining replication fork integrity in UV-irradiated Escherichia coli cells. DNA Repair (Amst.) 7 (2008) 1589-1602
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1589-1602
    • Rudolph, C.J.1    Upton, A.L.2    Lloyd, R.G.3
  • 55
    • 0028027784 scopus 로고
    • Tus prevents overreplication of oriC plasmid DNA
    • Hiasa H., and Marians K.J. Tus prevents overreplication of oriC plasmid DNA. J. Biol. Chem. 269 (1994) 26959-26968
    • (1994) J. Biol. Chem. , vol.269 , pp. 26959-26968
    • Hiasa, H.1    Marians, K.J.2
  • 56
    • 0030911141 scopus 로고    scopus 로고
    • Inactivation of the replication-termination system affects the replication mode and causes unstable maintenance of plasmid R1
    • Krabbe M., Zabielski J., Bernander R., and Nordstrom K. Inactivation of the replication-termination system affects the replication mode and causes unstable maintenance of plasmid R1. Mol. Microbiol. 24 (1997) 723-735
    • (1997) Mol. Microbiol. , vol.24 , pp. 723-735
    • Krabbe, M.1    Zabielski, J.2    Bernander, R.3    Nordstrom, K.4
  • 57
    • 15944409969 scopus 로고    scopus 로고
    • A new in vivo termination function for DNA polymerase I of Escherichia coli K12
    • Markovitz A. A new in vivo termination function for DNA polymerase I of Escherichia coli K12. Mol. Microbiol. 55 (2005) 1867-1882
    • (2005) Mol. Microbiol. , vol.55 , pp. 1867-1882
    • Markovitz, A.1
  • 58
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan D.L., and O'Donnell M. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol. Cell 10 (2002) 647-657
    • (2002) Mol. Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 59
    • 0015124414 scopus 로고
    • Genetic recombination in Escherichia coli. IV. Isolation and characterization of recombination-deficient mutants of Escherichia coli K12
    • Storm P.K., Hoekstra W.P.M., De Haan P.G., and Verhoef C. Genetic recombination in Escherichia coli. IV. Isolation and characterization of recombination-deficient mutants of Escherichia coli K12. Mutat. Res. 13 (1971) 9-17
    • (1971) Mutat. Res. , vol.13 , pp. 9-17
    • Storm, P.K.1    Hoekstra, W.P.M.2    De Haan, P.G.3    Verhoef, C.4
  • 60
    • 0027397630 scopus 로고
    • Dissociation of synthetic Holliday junctions by E. coli RecG protein
    • Lloyd R.G., and Sharples G.J. Dissociation of synthetic Holliday junctions by E. coli RecG protein. EMBO J. 12 (1993) 17-22
    • (1993) EMBO J. , vol.12 , pp. 17-22
    • Lloyd, R.G.1    Sharples, G.J.2
  • 61
    • 0029871788 scopus 로고    scopus 로고
    • Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82
    • Mahdi A.A., Sharples G.J., Mandal T.N., and Lloyd R.G. Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. J. Mol. Biol. 257 (1996) 561-573
    • (1996) J. Mol. Biol. , vol.257 , pp. 561-573
    • Mahdi, A.A.1    Sharples, G.J.2    Mandal, T.N.3    Lloyd, R.G.4
  • 62
    • 0027236687 scopus 로고
    • Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB and ruvC mutations
    • Mandal T.N., Mahdi A.A., Sharples G.J., and Lloyd R.G. Resolution of Holliday intermediates in recombination and DNA repair: indirect suppression of ruvA, ruvB and ruvC mutations. J. Bacteriol. 175 (1993) 4325-4334
    • (1993) J. Bacteriol. , vol.175 , pp. 4325-4334
    • Mandal, T.N.1    Mahdi, A.A.2    Sharples, G.J.3    Lloyd, R.G.4
  • 63
    • 0036348154 scopus 로고    scopus 로고
    • Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo
    • Bolt E.L., and Lloyd R.G. Substrate specificity of RusA resolvase reveals the DNA structures targeted by RuvAB and RecG in vivo. Mol. Cell 10 (2002) 187-198
    • (2002) Mol. Cell , vol.10 , pp. 187-198
    • Bolt, E.L.1    Lloyd, R.G.2
  • 64
    • 0032052829 scopus 로고    scopus 로고
    • Recognition and manipulation of branched DNA by the RusA Holliday junction resolvase of Escherichia coli
    • Chan S.N., Vincent S.D., and Lloyd R.G. Recognition and manipulation of branched DNA by the RusA Holliday junction resolvase of Escherichia coli. Nucleic Acids Res. 26 (1998) 1560-1566
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1560-1566
    • Chan, S.N.1    Vincent, S.D.2    Lloyd, R.G.3
  • 65
    • 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. Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression. Cell 101 (2000) 35-45
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.G.2
  • 66
    • 0035902573 scopus 로고    scopus 로고
    • Formation of Holliday junctions by regression of stalled replication forks: RecG stimulates fork regression even when the DNA is negatively supercoiled
    • McGlynn P., Lloyd R.G., and Marians K.J. Formation of Holliday junctions by regression of stalled replication forks: RecG stimulates fork regression even when the DNA is negatively supercoiled. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 8235-8240
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8235-8240
    • McGlynn, P.1    Lloyd, R.G.2    Marians, K.J.3
  • 67
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton M.R., Scaife S., and Wigley D.B. Structural analysis of DNA replication fork reversal by RecG. Cell 107 (2001) 79-89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 68
    • 0033988907 scopus 로고    scopus 로고
    • Recombination is essential for viability of an Escherichia coli dam (DNA adenine methyltransferase) mutant
    • Marinus M.G. Recombination is essential for viability of an Escherichia coli dam (DNA adenine methyltransferase) mutant. J. Bacteriol. 182 (2000) 463-468
    • (2000) J. Bacteriol. , vol.182 , pp. 463-468
    • Marinus, M.G.1
  • 69
    • 0031878178 scopus 로고    scopus 로고
    • Abortive recombination in Escherichia coli ruv mutants blocks chromosome partitioning
    • Ishioka K., Fukuoh A., Iwasaki H., Nakata A., and Shinagawa H. Abortive recombination in Escherichia coli ruv mutants blocks chromosome partitioning. Genes Cells 3 (1998) 209-220
    • (1998) Genes Cells , vol.3 , pp. 209-220
    • Ishioka, K.1    Fukuoh, A.2    Iwasaki, H.3    Nakata, A.4    Shinagawa, H.5
  • 71
    • 33749411110 scopus 로고    scopus 로고
    • RuvABC is required to resolve Holliday junctions that accumulate following replication on damaged templates in Escherichia coli
    • Donaldson J.R., Courcelle C.T., and Courcelle J. RuvABC is required to resolve Holliday junctions that accumulate following replication on damaged templates in Escherichia coli. J. Biol. Chem. 281 (2006) 28811-28821
    • (2006) J. Biol. Chem. , vol.281 , pp. 28811-28821
    • Donaldson, J.R.1    Courcelle, C.T.2    Courcelle, J.3
  • 72
    • 68449088790 scopus 로고    scopus 로고
    • Resolution of joint molecules by RuvABC and RecG following cleavage of the Escherichia coli chromosome by EcoKI
    • Wardrope L., Okely E., and Leach D. Resolution of joint molecules by RuvABC and RecG following cleavage of the Escherichia coli chromosome by EcoKI. PLoS One 4 (2009) e6542
    • (2009) PLoS One , vol.4
    • Wardrope, L.1    Okely, E.2    Leach, D.3
  • 73
    • 0027420692 scopus 로고
    • A sister-strand exchange mechanism for recA-independent deletion of repeated DNA sequences in Escherichia coli
    • Lovett S.T., Drapkin P.T., Sutera Jr. V.A., and Gluckman-Peskind T.J. A sister-strand exchange mechanism for recA-independent deletion of repeated DNA sequences in Escherichia coli. Genetics 135 (1993) 631-642
    • (1993) Genetics , vol.135 , pp. 631-642
    • Lovett, S.T.1    Drapkin, P.T.2    Sutera Jr., V.A.3    Gluckman-Peskind, T.J.4
  • 74
    • 33750946025 scopus 로고    scopus 로고
    • Replication arrest-stimulated recombination: Dependence on the RecA paralog, RadA/Sms and translesion polymerase, DinB
    • Lovett S.T. Replication arrest-stimulated recombination: Dependence on the RecA paralog, RadA/Sms and translesion polymerase, DinB. DNA Repair (Amst.) 5 (2006) 1421-1427
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 1421-1427
    • Lovett, S.T.1
  • 75
    • 4344706540 scopus 로고    scopus 로고
    • IS911 partial transposition products and their processing by the Escherichia coli RecG helicase
    • Turlan C., Loot C., and Chandler M. IS911 partial transposition products and their processing by the Escherichia coli RecG helicase. Mol. Microbiol. 53 (2004) 1021-1033
    • (2004) Mol. Microbiol. , vol.53 , pp. 1021-1033
    • Turlan, C.1    Loot, C.2    Chandler, M.3
  • 76
    • 48149090365 scopus 로고    scopus 로고
    • DNA double strand break repair and crossing over mediated by RuvABC resolvase and RecG translocase
    • Grove J.I., Harris L., Buckman C., and Lloyd R.G. DNA double strand break repair and crossing over mediated by RuvABC resolvase and RecG translocase. DNA Repair (Amst.) 7 (2008) 1517-1530
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 1517-1530
    • Grove, J.I.1    Harris, L.2    Buckman, C.3    Lloyd, R.G.4
  • 77
    • 0346367178 scopus 로고    scopus 로고
    • ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication
    • Tanaka T., Taniyama C., Arai K., and Masai H. ATPase/helicase motif mutants of Escherichia coli PriA protein essential for recombination-dependent DNA replication. Genes Cells 8 (2003) 251-261
    • (2003) Genes Cells , vol.8 , pp. 251-261
    • Tanaka, T.1    Taniyama, C.2    Arai, K.3    Masai, H.4
  • 78
    • 33746629428 scopus 로고    scopus 로고
    • Rep and PriA helicase activities prevent RecA from provoking unnecessary recombination during replication fork repair
    • Mahdi A.A., Buckman C., Harris L., and Lloyd R.G. Rep and PriA helicase activities prevent RecA from provoking unnecessary recombination during replication fork repair. Genes Dev. 20 (2006) 2135-2147
    • (2006) Genes Dev. , vol.20 , pp. 2135-2147
    • Mahdi, A.A.1    Buckman, C.2    Harris, L.3    Lloyd, R.G.4
  • 79
    • 0033546121 scopus 로고    scopus 로고
    • Duplex opening by primosome protein PriA for replisome assembly on a recombination intermediate
    • Jones J.M., and Nakai H. Duplex opening by primosome protein PriA for replisome assembly on a recombination intermediate. J. Mol. Biol. 289 (1999) 503-516
    • (1999) J. Mol. Biol. , vol.289 , pp. 503-516
    • Jones, J.M.1    Nakai, H.2
  • 80
    • 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. Replication fork assembly at recombination intermediates is required for bacterial growth. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 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
  • 81
    • 0037352498 scopus 로고    scopus 로고
    • PriA mediates DNA replication pathway choice at recombination intermediates
    • Xu L., and Marians K.J. PriA mediates DNA replication pathway choice at recombination intermediates. Mol. Cell 11 (2003) 817-826
    • (2003) Mol. Cell , vol.11 , pp. 817-826
    • Xu, L.1    Marians, K.J.2
  • 82
    • 0026726616 scopus 로고
    • ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes
    • Zavitz K.H., and Marians K.J. ATPase-deficient mutants of the Escherichia coli DNA replication protein PriA are capable of catalyzing the assembly of active primosomes. J. Biol. Chem. 267 (1992) 6933-6940
    • (1992) J. Biol. Chem. , vol.267 , pp. 6933-6940
    • Zavitz, K.H.1    Marians, K.J.2
  • 83
    • 0029850005 scopus 로고    scopus 로고
    • Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12
    • Al-Deib A.A., Mahdi A.A., and Lloyd R.G. Modulation of recombination and DNA repair by the RecG and PriA helicases of Escherichia coli K-12. J. Bacteriol. 178 (1996) 6782-6789
    • (1996) J. Bacteriol. , vol.178 , pp. 6782-6789
    • Al-Deib, A.A.1    Mahdi, A.A.2    Lloyd, R.G.3
  • 84
    • 0037329487 scopus 로고    scopus 로고
    • PriA supports two distinct pathways for replication restart in UV-irradiated Escherichia coli cells
    • Jaktaji R.P., and Lloyd R.G. PriA supports two distinct pathways for replication restart in UV-irradiated Escherichia coli cells. Mol. Microbiol. 47 (2003) 1091-1100
    • (2003) Mol. Microbiol. , vol.47 , pp. 1091-1100
    • Jaktaji, R.P.1    Lloyd, R.G.2
  • 85
    • 0030741602 scopus 로고    scopus 로고
    • Roles of the recG gene product of Escherichia coli in recombination repair: effects of the delta recG mutation on cell division and chromosome partition
    • Ishioka K., Iwasaki H., and Shinagawa H. Roles of the recG gene product of Escherichia coli in recombination repair: effects of the delta recG mutation on cell division and chromosome partition. Genes Genet. Syst. 72 (1997) 91-99
    • (1997) Genes Genet. Syst. , vol.72 , pp. 91-99
    • Ishioka, K.1    Iwasaki, H.2    Shinagawa, H.3
  • 87
    • 0016605312 scopus 로고
    • Postreplication repair in human cells: on the presence of gaps opposite dimers and recombination
    • Meneghini R., and Hanawalt P.C. Postreplication repair in human cells: on the presence of gaps opposite dimers and recombination. Basic Life Sci. 5B (1975) 639-642
    • (1975) Basic Life Sci. , vol.5 B , pp. 639-642
    • Meneghini, R.1    Hanawalt, P.C.2
  • 88
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • Higuchi K., Katayama T., Iwai S., Hidaka M., Horiuchi T., and Maki H. Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro. Genes Cells 8 (2003) 437-449
    • (2003) Genes Cells , vol.8 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 89
    • 0037799191 scopus 로고    scopus 로고
    • Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo
    • Pages V., and Fuchs R.P. Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo. Science 300 (2003) 1300-1303
    • (2003) Science , vol.300 , pp. 1300-1303
    • Pages, V.1    Fuchs, R.P.2
  • 90
    • 2442686846 scopus 로고    scopus 로고
    • Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block
    • McInerney P., and O'Donnell M. Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block. J. Biol. Chem. 279 (2004) 21543-21551
    • (2004) J. Biol. Chem. , vol.279 , pp. 21543-21551
    • McInerney, P.1    O'Donnell, M.2
  • 91
    • 0033603630 scopus 로고    scopus 로고
    • Analysis of DNA replication forks encountering a pyrimidine dimer in the template to the leading strand
    • Cordeiro-Stone M., Makhov A.M., Zaritskaya L.S., and Griffith J.D. Analysis of DNA replication forks encountering a pyrimidine dimer in the template to the leading strand. J. Mol. Biol. 289 (1999) 1207-1218
    • (1999) J. Mol. Biol. , vol.289 , pp. 1207-1218
    • Cordeiro-Stone, M.1    Makhov, A.M.2    Zaritskaya, L.S.3    Griffith, J.D.4
  • 92
    • 0029586324 scopus 로고
    • Differential replication of a single, UV-induced lesion in the leading or lagging strand by a human cell extract: fork uncoupling or gap formation
    • Svoboda D.L., and Vos J.M. Differential replication of a single, UV-induced lesion in the leading or lagging strand by a human cell extract: fork uncoupling or gap formation. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 11975-11979
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11975-11979
    • Svoboda, D.L.1    Vos, J.M.2
  • 93
    • 0017298802 scopus 로고
    • A model for replication repair in mammalian cells
    • Higgins N.P., Kato K., and Strauss B. A model for replication repair in mammalian cells. J. Mol. Biol. 101 (1976) 417-425
    • (1976) J. Mol. Biol. , vol.101 , pp. 417-425
    • Higgins, N.P.1    Kato, K.2    Strauss, B.3
  • 94
    • 0017109724 scopus 로고
    • Replicative bypass repair of ultraviolet damage to DNA of mammalian cells: caffeine sensitive and caffeine resistant mechanisms
    • Fujiwara Y., and Tatsumi M. Replicative bypass repair of ultraviolet damage to DNA of mammalian cells: caffeine sensitive and caffeine resistant mechanisms. Mutat. Res. 37 (1976) 91-110
    • (1976) Mutat. Res. , vol.37 , pp. 91-110
    • Fujiwara, Y.1    Tatsumi, M.2
  • 97
    • 1642443168 scopus 로고    scopus 로고
    • Mechanisms of replication fork restart in Escherichia coli
    • Marians K.J. Mechanisms of replication fork restart in Escherichia coli. Philos. Trans. R. Soc. Lond B Biol. Sci. 359 (2004) 71-77
    • (2004) Philos. Trans. R. Soc. Lond B Biol. Sci. , vol.359 , pp. 71-77
    • Marians, K.J.1
  • 98
    • 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. Replisome fate upon encountering a leading strand block and clearance from DNA by recombination proteins. J. Biol. Chem. 282 (2007) 25903-25916
    • (2007) J. Biol. Chem. , vol.282 , pp. 25903-25916
    • McInerney, P.1    O'Donnell, M.2
  • 99
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair
    • Morimatsu K., and Kowalczykowski S.C. RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair. Mol. Cell 11 (2003) 1337-1347
    • (2003) Mol. Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 100
    • 33847778234 scopus 로고    scopus 로고
    • Motoring along with the bacterial RecA protein
    • Cox M.M. Motoring along with the bacterial RecA protein. Nat. Rev. Mol. Cell Biol. 8 (2007) 127-138
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 127-138
    • Cox, M.M.1
  • 102
    • 34548061530 scopus 로고    scopus 로고
    • UvrD controls the access of recombination proteins to blocked replication forks
    • Lestini R., and Michel B. UvrD controls the access of recombination proteins to blocked replication forks. EMBO J. 26 (2007) 3804-3814
    • (2007) EMBO J. , vol.26 , pp. 3804-3814
    • Lestini, R.1    Michel, B.2
  • 103
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
    • Veaute X., Delmas S., Selva M., Jeusset J., Le Cam E., Matic I., Fabre F., and Petit M.A. UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli. EMBO J. 24 (2005) 180-189
    • (2005) EMBO J. , vol.24 , pp. 180-189
    • Veaute, X.1    Delmas, S.2    Selva, M.3    Jeusset, J.4    Le Cam, E.5    Matic, I.6    Fabre, F.7    Petit, M.A.8
  • 104
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • Heller R.C., and Marians K.J. Replication fork reactivation downstream of a blocked nascent leading strand. Nature 439 (2006) 557-562
    • (2006) Nature , vol.439 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 105
    • 33745153750 scopus 로고    scopus 로고
    • Nascent DNA processing by RecJ favors lesion repair over translesion synthesis at arrested replication forks in Escherichia coli
    • Courcelle C.T., Chow K.H., Casey A., and Courcelle J. Nascent DNA processing by RecJ favors lesion repair over translesion synthesis at arrested replication forks in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 9154-9159
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 9154-9159
    • Courcelle, C.T.1    Chow, K.H.2    Casey, A.3    Courcelle, J.4
  • 107
    • 0034655991 scopus 로고    scopus 로고
    • BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures
    • Wang Y., Cortez D., Yazdi P., Neff N., Elledge S.J., and Qin J. BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. Genes Dev. 14 (2000) 927-939
    • (2000) Genes Dev. , vol.14 , pp. 927-939
    • Wang, Y.1    Cortez, D.2    Yazdi, P.3    Neff, N.4    Elledge, S.J.5    Qin, J.6
  • 108
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in Escherichia coli RecQ DNA helicase function
    • Shereda R.D., Bernstein D.A., and Keck J.L. A central role for SSB in Escherichia coli RecQ DNA helicase function. J. Biol. Chem. 282 (2007) 19247-19258
    • (2007) J. Biol. Chem. , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 109
    • 59649104376 scopus 로고    scopus 로고
    • Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus
    • Shereda R.D., Reiter N.J., Butcher S.E., and Keck J.L. Identification of the SSB binding site on E. coli RecQ reveals a conserved surface for binding SSB's C terminus. J. Mol. Biol. 386 (2009) 612-625
    • (2009) J. Mol. Biol. , vol.386 , pp. 612-625
    • Shereda, R.D.1    Reiter, N.J.2    Butcher, S.E.3    Keck, J.L.4
  • 110
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman C.J., and McGlynn P. PriA helicase and SSB interact physically and functionally. Nucleic Acids Res. 32 (2004) 6378-6387
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 111
    • 48249095036 scopus 로고    scopus 로고
    • Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I
    • Lu D., and Keck J.L. Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 9169-9174
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9169-9174
    • Lu, D.1    Keck, J.L.2
  • 112
    • 67651229333 scopus 로고    scopus 로고
    • Peptide inhibitors identify roles for SSB C-terminal residues in SSB/exonuclease I complex formation
    • Lu D., Windsor M.A., Gellman S.H., and Keck J.L. Peptide inhibitors identify roles for SSB C-terminal residues in SSB/exonuclease I complex formation. Biochemistry 48 (2009) 6764-6771
    • (2009) Biochemistry , vol.48 , pp. 6764-6771
    • Lu, D.1    Windsor, M.A.2    Gellman, S.H.3    Keck, J.L.4
  • 113
    • 58749113648 scopus 로고    scopus 로고
    • RecG interacts directly with SSB: implications for stalled replication fork regression
    • Buss J.A., Kimura Y., and Bianco P.R. RecG interacts directly with SSB: implications for stalled replication fork regression. Nucleic Acids Res. 36 (2008) 7029-7042
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7029-7042
    • Buss, J.A.1    Kimura, Y.2    Bianco, P.R.3
  • 114
    • 58549101083 scopus 로고    scopus 로고
    • Orchestration of Haemophilus influenzae RecJ exonuclease by interaction with single-stranded DNA-binding protein
    • Sharma R., and Rao D.N. Orchestration of Haemophilus influenzae RecJ exonuclease by interaction with single-stranded DNA-binding protein. J. Mol. Biol. 385 (2009) 1375-1396
    • (2009) J. Mol. Biol. , vol.385 , pp. 1375-1396
    • Sharma, R.1    Rao, D.N.2
  • 115
    • 43749084397 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein recruits DNA polymerase V to primer termini on RecA-coated DNA
    • Arad G., Hendel A., Urbanke C., Curth U., and Livneh Z. Single-stranded DNA-binding protein recruits DNA polymerase V to primer termini on RecA-coated DNA. J. Biol. Chem. 283 (2008) 8274-8282
    • (2008) J. Biol. Chem. , vol.283 , pp. 8274-8282
    • Arad, G.1    Hendel, A.2    Urbanke, C.3    Curth, U.4    Livneh, Z.5
  • 116
    • 2442489945 scopus 로고    scopus 로고
    • RuvAB and RecG are not essential for the recovery of DNA synthesis following UV-induced DNA damage in Escherichia coli
    • Donaldson J.R., Courcelle C.T., and Courcelle J. RuvAB and RecG are not essential for the recovery of DNA synthesis following UV-induced DNA damage in Escherichia coli. Genetics 166 (2004) 1631-1640
    • (2004) Genetics , vol.166 , pp. 1631-1640
    • Donaldson, J.R.1    Courcelle, C.T.2    Courcelle, J.3
  • 117
    • 0014484120 scopus 로고
    • Replication of the bacterial chromosome: location of new initiation sites after irradiation
    • Billen D. Replication of the bacterial chromosome: location of new initiation sites after irradiation. J. Bacteriol. 97 (1969) 1169-1175
    • (1969) J. Bacteriol. , vol.97 , pp. 1169-1175
    • Billen, D.1
  • 118
    • 0028023335 scopus 로고
    • Roles of ruvA, ruvC and recG gene functions in normal and DNA damage-inducible replication of the Escherichia coli chromosome
    • Asai T., and Kogoma T. Roles of ruvA, ruvC and recG gene functions in normal and DNA damage-inducible replication of the Escherichia coli chromosome. Genetics 137 (1994) 895-902
    • (1994) Genetics , vol.137 , pp. 895-902
    • Asai, T.1    Kogoma, T.2
  • 119
    • 6044220123 scopus 로고    scopus 로고
    • Isolation of SOS constitutive mutants of Escherichia coli
    • O'Reilly E.K., and Kreuzer K.N. Isolation of SOS constitutive mutants of Escherichia coli. J. Bacteriol. 186 (2004) 7149-7160
    • (2004) J. Bacteriol. , vol.186 , pp. 7149-7160
    • O'Reilly, E.K.1    Kreuzer, K.N.2
  • 120
    • 33645636759 scopus 로고    scopus 로고
    • Stabilization of a stalled replication fork by concerted actions of two helicases
    • Tanaka T., and Masai H. Stabilization of a stalled replication fork by concerted actions of two helicases. J. Biol. Chem. 281 (2006) 3484-3493
    • (2006) J. Biol. Chem. , vol.281 , pp. 3484-3493
    • Tanaka, T.1    Masai, H.2
  • 121
    • 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. Unwinding of the nascent lagging strand by Rep and PriA enables the direct restart of stalled replication forks. J. Biol. Chem. 280 (2005) 34143-34151
    • (2005) J. Biol. Chem. , vol.280 , pp. 34143-34151
    • Heller, R.C.1    Marians, K.J.2
  • 122
    • 0027957144 scopus 로고
    • The DNA replication fork blocked at the Ter site may be an entrance for the RecBCD enzyme into duplex DNA
    • Horiuchi T., Fujimura Y., Nishitani H., Kobayashi T., and Hidaka M. The DNA replication fork blocked at the Ter site may be an entrance for the RecBCD enzyme into duplex DNA. J. Bacteriol. 176 (1994) 4656-4663
    • (1994) J. Bacteriol. , vol.176 , pp. 4656-4663
    • Horiuchi, T.1    Fujimura, Y.2    Nishitani, H.3    Kobayashi, T.4    Hidaka, M.5
  • 123
    • 1942488150 scopus 로고    scopus 로고
    • RecG helicase promotes DNA double-strand break repair
    • Meddows T.R., Savory A.P., and Lloyd R.G. RecG helicase promotes DNA double-strand break repair. Mol. Microbiol. 52 (2004) 119-132
    • (2004) Mol. Microbiol. , vol.52 , pp. 119-132
    • Meddows, T.R.1    Savory, A.P.2    Lloyd, R.G.3
  • 124
    • 9644296031 scopus 로고    scopus 로고
    • Genetic recombination and the cell cycle: what we have learned from chromosome dimers
    • Lesterlin C., Barre F.X., and Cornet F. Genetic recombination and the cell cycle: what we have learned from chromosome dimers. Mol. Microbiol. 54 (2004) 1151-1160
    • (2004) Mol. Microbiol. , vol.54 , pp. 1151-1160
    • Lesterlin, C.1    Barre, F.X.2    Cornet, F.3
  • 125
    • 0035793090 scopus 로고    scopus 로고
    • Effects of replication termination mutants on chromosome partitioning in Bacillus subtilis
    • Lemon K.P., Kurtser I., and Grossman A.D. Effects of replication termination mutants on chromosome partitioning in Bacillus subtilis. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 212-217
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 212-217
    • Lemon, K.P.1    Kurtser, I.2    Grossman, A.D.3
  • 126
    • 0034074478 scopus 로고    scopus 로고
    • Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease
    • Genschel J., Curth U., and Urbanke C. Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease. Biol. Chem. 381 (2000) 183-192
    • (2000) Biol. Chem. , vol.381 , pp. 183-192
    • Genschel, J.1    Curth, U.2    Urbanke, C.3
  • 127
    • 0035902462 scopus 로고    scopus 로고
    • Stationary-phase mutation in the bacterial chromosome: recombination protein and DNA polymerase IV dependence
    • Bull H.J., Lombardo M.J., and Rosenberg S.M. Stationary-phase mutation in the bacterial chromosome: recombination protein and DNA polymerase IV dependence. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 8334-8341
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8334-8341
    • Bull, H.J.1    Lombardo, M.J.2    Rosenberg, S.M.3
  • 128
    • 10444253273 scopus 로고    scopus 로고
    • Stress responses and genetic variation in bacteria
    • Foster P.L. Stress responses and genetic variation in bacteria. Mutat. Res. 569 (2005) 3-11
    • (2005) Mutat. Res. , vol.569 , pp. 3-11
    • Foster, P.L.1
  • 129
    • 0030051842 scopus 로고    scopus 로고
    • Two enzymes, both of which process recombination intermediates, have opposite effects on adaptive mutation in Escherichia coli
    • Foster P.L., Trimarchi J.M., and Maurer R.A. Two enzymes, both of which process recombination intermediates, have opposite effects on adaptive mutation in Escherichia coli. Genetics 142 (1996) 25-37
    • (1996) Genetics , vol.142 , pp. 25-37
    • Foster, P.L.1    Trimarchi, J.M.2    Maurer, R.A.3
  • 130
    • 0030000945 scopus 로고    scopus 로고
    • Opposing roles of the Holliday junction processing systems of Escherichia coli in recombination-dependent adaptive mutation
    • Harris R.S., Ross K.J., and Rosenberg S.M. Opposing roles of the Holliday junction processing systems of Escherichia coli in recombination-dependent adaptive mutation. Genetics 142 (1996) 681-691
    • (1996) Genetics , vol.142 , pp. 681-691
    • Harris, R.S.1    Ross, K.J.2    Rosenberg, S.M.3
  • 131
    • 0142062024 scopus 로고    scopus 로고
    • Error-prone DNA polymerase IV is controlled by the stress-response sigma factor, RpoS, in Escherichia coli
    • Layton J.C., and Foster P.L. Error-prone DNA polymerase IV is controlled by the stress-response sigma factor, RpoS, in Escherichia coli. Mol. Microbiol. 50 (2003) 549-561
    • (2003) Mol. Microbiol. , vol.50 , pp. 549-561
    • Layton, J.C.1    Foster, P.L.2
  • 132
    • 33745208689 scopus 로고    scopus 로고
    • Loss of both Holliday junction processing pathways is synthetically lethal in the presence of gonococcal pilin antigenic variation
    • Sechman E.V., Kline K.A., and Seifert H.S. Loss of both Holliday junction processing pathways is synthetically lethal in the presence of gonococcal pilin antigenic variation. Mol. Microbiol. 61 (2006) 185-193
    • (2006) Mol. Microbiol. , vol.61 , pp. 185-193
    • Sechman, E.V.1    Kline, K.A.2    Seifert, H.S.3
  • 133
    • 64149093563 scopus 로고    scopus 로고
    • Unwinding the structure and function of the archaeal MCM helicase
    • Sakakibara N., Kelman L.M., and Kelman Z. Unwinding the structure and function of the archaeal MCM helicase. Mol. Microbiol. 72 (2009) 286-296
    • (2009) Mol. Microbiol. , vol.72 , pp. 286-296
    • Sakakibara, N.1    Kelman, L.M.2    Kelman, Z.3
  • 134
    • 39449123549 scopus 로고    scopus 로고
    • The MCM complex: (just) a replicative helicase?
    • Costa A., and Onesti S. The MCM complex: (just) a replicative helicase?. Biochem. Soc. Trans. 36 (2008) 136-140
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 136-140
    • Costa, A.1    Onesti, S.2
  • 135
    • 2442676334 scopus 로고    scopus 로고
    • Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery
    • Tuteja N., and Tuteja R. Prokaryotic and eukaryotic DNA helicases. Essential molecular motor proteins for cellular machinery. Eur. J. Biochem. 271 (2004) 1835-1848
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1835-1848
    • Tuteja, N.1    Tuteja, R.2
  • 136
    • 3943086339 scopus 로고    scopus 로고
    • Flap endonuclease 1: a central component of DNA metabolism
    • Liu Y., Kao H.I., and Bambara R.A. Flap endonuclease 1: a central component of DNA metabolism. Annu. Rev. Biochem. 73 (2004) 589-615
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 589-615
    • Liu, Y.1    Kao, H.I.2    Bambara, R.A.3
  • 137
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers P.M. Polymerase dynamics at the eukaryotic DNA replication fork. J. Biol. Chem. 284 (2009) 4041-4045
    • (2009) J. Biol. Chem. , vol.284 , pp. 4041-4045
    • Burgers, P.M.1


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