메뉴 건너뛰기




Volumn 426, Issue 24, 2015, Pages 3917-3928

Accessory replicative helicases and the replication of protein-bound DNA

Author keywords

DNA repair; DNA replication; mutation; recombination; transcription

Indexed keywords

HELICASE; NUCLEOPROTEIN; BACTERIAL PROTEIN; DNA; DNA BINDING PROTEIN; DNA HELICASE; PROTEIN BINDING;

EID: 84914689849     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.10.001     Document Type: Review
Times cited : (46)

References (118)
  • 4
    • 84862763199 scopus 로고    scopus 로고
    • The conflict between DNA replication and transcription
    • P. McGlynn, N.J. Savery, and M.S. Dillingham The conflict between DNA replication and transcription Mol Microbiol 85 2012 12 20
    • (2012) Mol Microbiol , vol.85 , pp. 12-20
    • McGlynn, P.1    Savery, N.J.2    Dillingham, M.S.3
  • 5
    • 84876188716 scopus 로고    scopus 로고
    • Transcription-replication encounters, consequences and genomic instability
    • A. Helmrich, M. Ballarino, E. Nudler, and L. Tora Transcription-replication encounters, consequences and genomic instability Nat Struct Mol Biol 20 2013 412 418
    • (2013) Nat Struct Mol Biol , vol.20 , pp. 412-418
    • Helmrich, A.1    Ballarino, M.2    Nudler, E.3    Tora, L.4
  • 6
    • 84876891791 scopus 로고    scopus 로고
    • Protein-DNA complexes are the primary sources of replication fork pausing in Escherichia coli
    • M.K. Gupta, C.P. Guy, J.T. Yeeles, J. Atkinson, H. Bell, and R.G. Lloyd Protein-DNA complexes are the primary sources of replication fork pausing in Escherichia coli Proc Natl Acad Sci U S A 110 2013 7252 7257
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7252-7257
    • Gupta, M.K.1    Guy, C.P.2    Yeeles, J.T.3    Atkinson, J.4    Bell, H.5    Lloyd, R.G.6
  • 7
    • 34948826443 scopus 로고    scopus 로고
    • Nucleotide excision repair and homologous recombination systems commit differentially to the repair of DNA-protein crosslinks
    • T. Nakano, S. Morishita, A. Katafuchi, M. Matsubara, Y. Horikawa, and H. Terato Nucleotide excision repair and homologous recombination systems commit differentially to the repair of DNA-protein crosslinks Mol Cell 28 2007 147 158
    • (2007) Mol Cell , vol.28 , pp. 147-158
    • Nakano, T.1    Morishita, S.2    Katafuchi, A.3    Matsubara, M.4    Horikawa, Y.5    Terato, H.6
  • 8
    • 0027515187 scopus 로고
    • A gene with specific and global effects on recombination of sequences from tandemly repeated genes in Saccharomyces cerevisiae
    • R.L. Keil, and A.D. McWilliams A gene with specific and global effects on recombination of sequences from tandemly repeated genes in Saccharomyces cerevisiae Genetics 135 1993 711 718
    • (1993) Genetics , vol.135 , pp. 711-718
    • Keil, R.L.1    McWilliams, A.D.2
  • 9
    • 0348047594 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes
    • A.S. Ivessa, B.A. Lenzmeier, J.B. Bessler, L.K. Goudsouzian, S.L. Schnakenberg, and V.A. Zakian The Saccharomyces cerevisiae helicase Rrm3p facilitates replication past nonhistone protein-DNA complexes Mol Cell 12 2003 1525 1536
    • (2003) Mol Cell , vol.12 , 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
  • 10
    • 1642416422 scopus 로고    scopus 로고
    • Requirement of Rrm3 helicase for repair of spontaneous DNA lesions in cells lacking Srs2 or Sgs1 helicase
    • K.H. Schmidt, and R.D. Kolodner Requirement of Rrm3 helicase for repair of spontaneous DNA lesions in cells lacking Srs2 or Sgs1 helicase Mol Cell Biol 24 2004 3213 3226
    • (2004) Mol Cell Biol , vol.24 , pp. 3213-3226
    • Schmidt, K.H.1    Kolodner, R.D.2
  • 11
    • 1642309305 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Rrm3p DNA helicase promotes genome integrity by preventing replication fork stalling: Viability of Rrm3 cells requires the intra-S-phase checkpoint and fork restart activities
    • J.Z. Torres, S.L. Schnakenberg, and V.A. Zakian Saccharomyces cerevisiae Rrm3p DNA helicase promotes genome integrity by preventing replication fork stalling: viability of Rrm3 cells requires the intra-S-phase checkpoint and fork restart activities Mol Cell Biol 24 2004 3198 3212
    • (2004) Mol Cell Biol , vol.24 , pp. 3198-3212
    • Torres, J.Z.1    Schnakenberg, S.L.2    Zakian, V.A.3
  • 12
    • 70449633073 scopus 로고    scopus 로고
    • Rep provides a second motor at the replisome to promote duplication of protein-bound DNA
    • C.P. Guy, J. Atkinson, M.K. Gupta, A.A. Mahdi, E.J. Gwynn, and C.J. Rudolph Rep provides a second motor at the replisome to promote duplication of protein-bound DNA Mol Cell 36 2009 654 666
    • (2009) Mol Cell , vol.36 , pp. 654-666
    • Guy, C.P.1    Atkinson, J.2    Gupta, M.K.3    Mahdi, A.A.4    Gwynn, E.J.5    Rudolph, C.J.6
  • 13
    • 0028786478 scopus 로고
    • Lethality of rep recB and rep recC double mutants of Escherichia coli
    • M. Uzest, S.D. Ehrlich, and B. Michel Lethality of rep recB and rep recC double mutants of Escherichia coli Mol Microbiol 17 1995 1177 1188
    • (1995) Mol Microbiol , vol.17 , pp. 1177-1188
    • Uzest, M.1    Ehrlich, S.D.2    Michel, B.3
  • 14
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • M.R. Singleton, M.S. Dillingham, and D.B. Wigley Structure and mechanism of helicases and nucleic acid translocases Annu Rev Biochem 76 2007 23 50
    • (2007) Annu Rev Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 15
    • 42449141601 scopus 로고    scopus 로고
    • Non-hexameric DNA helicases and translocases: Mechanisms and regulation
    • T.M. Lohman, E.J. Tomko, and C.G. Wu Non-hexameric DNA helicases and translocases: mechanisms and regulation Nat Rev Mol Cell Biol 9 2008 391 401
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 391-401
    • Lohman, T.M.1    Tomko, E.J.2    Wu, C.G.3
  • 16
    • 84914691906 scopus 로고    scopus 로고
    • Grip it and rip it: Structural mechanisms of DNA helicase substrate binding and unwinding
    • B. Bhattacharyya, and J.L. Keck Grip it and rip it: structural mechanisms of DNA helicase substrate binding and unwinding Protein Sci 2014 10.1002/pro.2533
    • (2014) Protein Sci
    • Bhattacharyya, B.1    Keck, J.L.2
  • 17
    • 84873692452 scopus 로고    scopus 로고
    • Helicases at the replication fork
    • P. McGlynn Helicases at the replication fork Adv Exp Med Biol 767 2013 97 121
    • (2013) Adv Exp Med Biol , vol.767 , pp. 97-121
    • McGlynn, P.1
  • 18
    • 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
    • D.L. Kaplan 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 2000 285 299
    • (2000) J Mol Biol , vol.301 , pp. 285-299
    • Kaplan, D.L.1
  • 19
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • O. Itsathitphaisarn, R.A. Wing, W.K. Eliason, J. Wang, and T.A. Steitz The hexameric helicase DnaB adopts a nonplanar conformation during translocation Cell 151 2012 267 277
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 20
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein J Biol Chem 273 1998 9058 9069
    • (1998) J Biol Chem , vol.273 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 21
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • P.H. von Hippel, and E. Delagoutte A general model for nucleic acid helicases and their "coupling" within macromolecular machines Cell 104 2001 177 190
    • (2001) Cell , vol.104 , pp. 177-190
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 23
    • 0027078134 scopus 로고
    • Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases
    • J.E. Yancey-Wrona, and S.W. Matson Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases Nucleic Acids Res 20 1992 6713 6721
    • (1992) Nucleic Acids Res , vol.20 , pp. 6713-6721
    • Yancey-Wrona, J.E.1    Matson, S.W.2
  • 24
    • 84901933120 scopus 로고    scopus 로고
    • Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA
    • J.Y. Lee, I.J. Finkelstein, L.K. Arciszewska, D.J. Sherratt, and E.C. Greene Single-molecule imaging of FtsK translocation reveals mechanistic features of protein-protein collisions on DNA Mol Cell 54 2014 832 843
    • (2014) Mol Cell , vol.54 , pp. 832-843
    • Lee, J.Y.1    Finkelstein, I.J.2    Arciszewska, L.K.3    Sherratt, D.J.4    Greene, E.C.5
  • 25
    • 0029022696 scopus 로고
    • Unwinding of chromatin by the SV40 large T antigen DNA helicase
    • U. Ramsperger, and H. Stahl Unwinding of chromatin by the SV40 large T antigen DNA helicase EMBO J 14 1995 3215 3225
    • (1995) EMBO J , vol.14 , pp. 3215-3225
    • Ramsperger, U.1    Stahl, H.2
  • 26
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A t-DnaB interaction mediates rapid replication fork movement
    • S. Kim, H.G. Dallmann, C.S. McHenry, and K.J. Marians Coupling of a replicative polymerase and helicase: a t-DnaB interaction mediates rapid replication fork movement Cell 84 1996 643 650
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 27
    • 0030739376 scopus 로고    scopus 로고
    • The acidic carboxyl terminus of the bacteriophage T7 gene 4 helicase/primase interacts with T7 DNA polymerase
    • S.M. Notarnicola, H.L. Mulcahy, J. Lee, and C.C. Richardson The acidic carboxyl terminus of the bacteriophage T7 gene 4 helicase/primase interacts with T7 DNA polymerase J Biol Chem 272 1997 18425 18433
    • (1997) J Biol Chem , vol.272 , pp. 18425-18433
    • Notarnicola, S.M.1    Mulcahy, H.L.2    Lee, J.3    Richardson, C.C.4
  • 28
    • 3242739284 scopus 로고    scopus 로고
    • Reconstitution of a minimal mtDNA replisome in vitro
    • J.A. Korhonen, X.H. Pham, M. Pellegrini, and M. Falkenberg Reconstitution of a minimal mtDNA replisome in vitro EMBO J 23 2004 2423 2429
    • (2004) EMBO J , vol.23 , pp. 2423-2429
    • Korhonen, J.A.1    Pham, X.H.2    Pellegrini, M.3    Falkenberg, M.4
  • 29
    • 19644399070 scopus 로고    scopus 로고
    • DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase
    • N.M. Stano, Y.J. Jeong, I. Donmez, P. Tummalapalli, M.K. Levin, and S.S. Patel DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase Nature 435 2005 370 373
    • (2005) Nature , vol.435 , pp. 370-373
    • Stano, N.M.1    Jeong, Y.J.2    Donmez, I.3    Tummalapalli, P.4    Levin, M.K.5    Patel, S.S.6
  • 31
    • 41349092240 scopus 로고    scopus 로고
    • Opening of nucleic-acid double strands by helicases: Active versus passive opening
    • M.D. Betterton, and F. Julicher Opening of nucleic-acid double strands by helicases: active versus passive opening Phys Rev E Stat Nonlin Soft Matter Phys 71 2005 011904
    • (2005) Phys Rev e Stat Nonlin Soft Matter Phys , vol.71 , pp. 011904
    • Betterton, M.D.1    Julicher, F.2
  • 33
    • 84886383360 scopus 로고    scopus 로고
    • Single-molecule FRET and linear dichroism studies of DNA breathing and helicase binding at replication fork junctions
    • C. Phelps, W. Lee, D. Jose, P.H. von Hippel, and A.H. Marcus Single-molecule FRET and linear dichroism studies of DNA breathing and helicase binding at replication fork junctions Proc Natl Acad Sci U S A 110 2013 17320 17325
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17320-17325
    • Phelps, C.1    Lee, W.2    Jose, D.3    Von Hippel, P.H.4    Marcus, A.H.5
  • 34
    • 84882823133 scopus 로고    scopus 로고
    • DNA unwinding heterogeneity by RecBCD results from static molecules able to equilibrate
    • B. Liu, R.J. Baskin, and S.C. Kowalczykowski DNA unwinding heterogeneity by RecBCD results from static molecules able to equilibrate Nature 500 2013 482 485
    • (2013) Nature , vol.500 , pp. 482-485
    • Liu, B.1    Baskin, R.J.2    Kowalczykowski, S.C.3
  • 35
    • 0032484096 scopus 로고    scopus 로고
    • Single-molecule enzymatic dynamics
    • H.P. Lu, L. Xun, and X.S. Xie Single-molecule enzymatic dynamics Science 282 1998 1877 1882
    • (1998) Science , vol.282 , pp. 1877-1882
    • Lu, H.P.1    Xun, L.2    Xie, X.S.3
  • 36
    • 2542432027 scopus 로고    scopus 로고
    • Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA
    • A.K. Byrd, and K.D. Raney Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA Nat Struct Mol Biol 11 2004 531 538
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 531-538
    • Byrd, A.K.1    Raney, K.D.2
  • 37
    • 33745176286 scopus 로고    scopus 로고
    • Displacement of a DNA binding protein by Dda helicase
    • A.K. Byrd, and K.D. Raney Displacement of a DNA binding protein by Dda helicase Nucleic Acids Res 34 2006 3020 3029
    • (2006) Nucleic Acids Res , vol.34 , pp. 3020-3029
    • Byrd, A.K.1    Raney, K.D.2
  • 38
    • 50149109300 scopus 로고    scopus 로고
    • Single-molecule studies of RNA polymerase: Motoring along
    • K.M. Herbert, W.J. Greenleaf, and S.M. Block Single-molecule studies of RNA polymerase: motoring along Annu Rev Biochem 77 2008 149 176
    • (2008) Annu Rev Biochem , vol.77 , pp. 149-176
    • Herbert, K.M.1    Greenleaf, W.J.2    Block, S.M.3
  • 40
    • 0026761603 scopus 로고
    • Replication forks pause at yeast centromeres
    • S.A. Greenfeder, and C.S. Newlon Replication forks pause at yeast centromeres Mol Cell Biol 12 1992 4056 4066
    • (1992) Mol Cell Biol , vol.12 , pp. 4056-4066
    • Greenfeder, S.A.1    Newlon, C.S.2
  • 41
    • 0031892179 scopus 로고    scopus 로고
    • Role of the core DNA polymerase III subunits at the replication fork. A is the only subunit required for processive replication
    • K.J. Marians, H. Hiasa, D.R. Kim, and C.S. McHenry Role of the core DNA polymerase III subunits at the replication fork. A is the only subunit required for processive replication J Biol Chem 273 1998 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
  • 42
    • 47049124441 scopus 로고    scopus 로고
    • Replication forks blocked by protein-DNA complexes have limited stability in vitro
    • P. McGlynn, and C.P. Guy Replication forks blocked by protein-DNA complexes have limited stability in vitro J Mol Biol 381 2008 249 255
    • (2008) J Mol Biol , vol.381 , pp. 249-255
    • McGlynn, P.1    Guy, C.P.2
  • 43
    • 75749150810 scopus 로고    scopus 로고
    • Direct restart of a replication fork stalled by a head-on RNA polymerase
    • R.T. Pomerantz, and M. O'Donnell Direct restart of a replication fork stalled by a head-on RNA polymerase Science 327 2010 590 592
    • (2010) Science , vol.327 , pp. 590-592
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 44
    • 80054091679 scopus 로고    scopus 로고
    • The Escherichia coli replisome is inherently DNA damage tolerant
    • J.T. Yeeles, and K.J. Marians The Escherichia coli replisome is inherently DNA damage tolerant Science 334 2011 235 238
    • (2011) Science , vol.334 , pp. 235-238
    • Yeeles, J.T.1    Marians, K.J.2
  • 45
    • 0025836589 scopus 로고
    • Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response
    • P. Nurse, K.H. Zavitz, and K.J. Marians Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response J Bacteriol 173 1991 6686 6693
    • (1991) J Bacteriol , vol.173 , pp. 6686-6693
    • Nurse, P.1    Zavitz, K.H.2    Marians, K.J.3
  • 46
    • 0026356063 scopus 로고
    • Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n′ protein
    • E.H. Lee, and A. Kornberg Replication deficiencies in priA mutants of Escherichia coli lacking the primosomal replication n′ protein Proc Natl Acad Sci U S A 88 1991 3029 3032
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3029-3032
    • Lee, E.H.1    Kornberg, A.2
  • 47
    • 84872138637 scopus 로고    scopus 로고
    • Recombination-restarted replication makes inverted chromosome fusions at inverted repeats
    • K. Mizuno, I. Miyabe, S.A. Schalbetter, A.M. Carr, and J.M. Murray Recombination-restarted replication makes inverted chromosome fusions at inverted repeats Nature 493 2012 246 249
    • (2012) Nature , vol.493 , pp. 246-249
    • Mizuno, K.1    Miyabe, I.2    Schalbetter, S.A.3    Carr, A.M.4    Murray, J.M.5
  • 48
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • X. Veaute, J. Jeusset, C. Soustelle, S.C. Kowalczykowski, E. Le Cam, and F. Fabre The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments Nature 423 2003 309 312
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 50
    • 78650307167 scopus 로고    scopus 로고
    • Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase
    • I.J. Finkelstein, M.L. Visnapuu, and E.C. Greene Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase Nature 468 2010 983 987
    • (2010) Nature , vol.468 , pp. 983-987
    • Finkelstein, I.J.1    Visnapuu, M.L.2    Greene, E.C.3
  • 51
    • 0014713029 scopus 로고
    • Characterization of REP - Mutants and their interaction with P2 phage
    • R. Calendar, B. Lindqvist, G. Sironi, and A.J. Clark Characterization of REP - mutants and their interaction with P2 phage Virology 40 1970 72 83
    • (1970) Virology , vol.40 , pp. 72-83
    • Calendar, R.1    Lindqvist, B.2    Sironi, G.3    Clark, A.J.4
  • 52
    • 0023405041 scopus 로고
    • The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels
    • J. Colasanti, and D.T. Denhardt The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels Mol Gen Genet 209 1987 382 390
    • (1987) Mol Gen Genet , vol.209 , pp. 382-390
    • Colasanti, J.1    Denhardt, D.T.2
  • 53
    • 0016710698 scopus 로고
    • The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains
    • H.E. Lane, and D.T. Denhardt The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains J Mol Biol 97 1975 99 112
    • (1975) J Mol Biol , vol.97 , pp. 99-112
    • Lane, H.E.1    Denhardt, D.T.2
  • 54
    • 57349157777 scopus 로고    scopus 로고
    • RecBCD enzyme and the repair of double-stranded DNA breaks
    • M.S. Dillingham, and S.C. Kowalczykowski RecBCD enzyme and the repair of double-stranded DNA breaks Microbiol Mol Biol Rev 72 2008 642 671
    • (2008) Microbiol Mol Biol Rev , vol.72 , pp. 642-671
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 55
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • B. Michel, S.D. Ehrlich, and M. Uzest DNA double-strand breaks caused by replication arrest EMBO J 16 1997 430 438
    • (1997) EMBO J , vol.16 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 57
    • 0034681257 scopus 로고    scopus 로고
    • The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have opposite effects on replication fork progression in ribosomal DNA
    • A.S. Ivessa, J.Q. Zhou, and V.A. Zakian The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have opposite effects on replication fork progression in ribosomal DNA Cell 100 2000 479 489
    • (2000) Cell , vol.100 , pp. 479-489
    • Ivessa, A.S.1    Zhou, J.Q.2    Zakian, V.A.3
  • 58
    • 0036606186 scopus 로고    scopus 로고
    • Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA
    • A.S. Ivessa, J.Q. Zhou, V.P. Schulz, E.K. Monson, and V.A. Zakian Saccharomyces Rrm3p, a 5′ to 3′ DNA helicase that promotes replication fork progression through telomeric and subtelomeric DNA Genes Dev 16 2002 1383 1396
    • (2002) Genes Dev , vol.16 , pp. 1383-1396
    • Ivessa, A.S.1    Zhou, J.Q.2    Schulz, V.P.3    Monson, E.K.4    Zakian, V.A.5
  • 59
    • 67449113551 scopus 로고    scopus 로고
    • Highly transcribed RNA polymerase II genes are impediments to replication fork progression in Saccharomyces cerevisiae
    • A. Azvolinsky, P.G. Giresi, J.D. Lieb, and V.A. Zakian Highly transcribed RNA polymerase II genes are impediments to replication fork progression in Saccharomyces cerevisiae Mol Cell 34 2009 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
  • 60
    • 33751237066 scopus 로고    scopus 로고
    • The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes
    • A. Azvolinsky, S. Dunaway, J.Z. Torres, J.B. Bessler, and V.A. Zakian The S. cerevisiae Rrm3p DNA helicase moves with the replication fork and affects replication of all yeast chromosomes Genes Dev 20 2006 3104 3116
    • (2006) Genes Dev , vol.20 , pp. 3104-3116
    • Azvolinsky, A.1    Dunaway, S.2    Torres, J.Z.3    Bessler, J.B.4    Zakian, V.A.5
  • 61
    • 0037160099 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RRM3, a 5′ to 3′ DNA helicase, physically interacts with proliferating cell nuclear antigen
    • K.H. Schmidt, K.L. Derry, and R.D. Kolodner Saccharomyces cerevisiae RRM3, a 5′ to 3′ DNA helicase, physically interacts with proliferating cell nuclear antigen J Biol Chem 277 2002 45331 45337
    • (2002) J Biol Chem , vol.277 , pp. 45331-45337
    • Schmidt, K.H.1    Derry, K.L.2    Kolodner, R.D.3
  • 62
    • 35448976515 scopus 로고    scopus 로고
    • Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: Interaction between subunits and identification of binding proteins
    • K. Matsuda, M. Makise, Y. Sueyasu, M. Takehara, T. Asano, and T. Mizushima Yeast two-hybrid analysis of the origin recognition complex of Saccharomyces cerevisiae: interaction between subunits and identification of binding proteins FEMS Yeast Res 7 2007 1263 1269
    • (2007) FEMS Yeast Res , vol.7 , pp. 1263-1269
    • Matsuda, K.1    Makise, M.2    Sueyasu, Y.3    Takehara, M.4    Asano, T.5    Mizushima, T.6
  • 63
    • 84873667075 scopus 로고    scopus 로고
    • RecQ helicases: Conserved guardians of genomic integrity
    • N.B. Larsen, and I.D. Hickson RecQ helicases: conserved guardians of genomic integrity Adv Exp Med Biol 767 2013 161 184
    • (2013) Adv Exp Med Biol , vol.767 , pp. 161-184
    • Larsen, N.B.1    Hickson, I.D.2
  • 65
    • 75649142564 scopus 로고    scopus 로고
    • The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo
    • H. Boubakri, A.L. de Septenville, E. Viguera, and B. Michel The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo EMBO J 29 2010 145 157
    • (2010) EMBO J , vol.29 , pp. 145-157
    • Boubakri, H.1    De Septenville, A.L.2    Viguera, E.3    Michel, B.4
  • 66
    • 77954371207 scopus 로고    scopus 로고
    • RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases
    • Z. Baharoglu, R. Lestini, S. Duigou, and B. Michel RNA polymerase mutations that facilitate replication progression in the rep uvrD recF mutant lacking two accessory replicative helicases Mol Microbiol 77 2010 324 336
    • (2010) Mol Microbiol , vol.77 , pp. 324-336
    • Baharoglu, Z.1    Lestini, R.2    Duigou, S.3    Michel, B.4
  • 67
    • 22544464455 scopus 로고    scopus 로고
    • RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription
    • B.W. Trautinger, R.P. Jaktaji, E. Rusakova, and R.G. Lloyd RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription Mol Cell 19 2005 247 258
    • (2005) Mol Cell , vol.19 , pp. 247-258
    • Trautinger, B.W.1    Jaktaji, R.P.2    Rusakova, E.3    Lloyd, R.G.4
  • 68
    • 84858315982 scopus 로고    scopus 로고
    • DNA replication through hard-to-replicate sites, including both highly transcribed RNA Pol II and Pol III genes, requires the S. pombe Pfh1 helicase
    • N. Sabouri, K.R. McDonald, C.J. Webb, I.M. Cristea, and V.A. Zakian DNA replication through hard-to-replicate sites, including both highly transcribed RNA Pol II and Pol III genes, requires the S. pombe Pfh1 helicase Genes Dev 26 2012 581 593
    • (2012) Genes Dev , vol.26 , pp. 581-593
    • Sabouri, N.1    McDonald, K.R.2    Webb, C.J.3    Cristea, I.M.4    Zakian, V.A.5
  • 69
    • 84858330322 scopus 로고    scopus 로고
    • The DNA helicase Pfh1 promotes fork merging at replication termination sites to ensure genome stability
    • R. Steinacher, F. Osman, J.Z. Dalgaard, A. Lorenz, and M.C. Whitby The DNA helicase Pfh1 promotes fork merging at replication termination sites to ensure genome stability Genes Dev 26 2012 594 602
    • (2012) Genes Dev , vol.26 , pp. 594-602
    • Steinacher, R.1    Osman, F.2    Dalgaard, J.Z.3    Lorenz, A.4    Whitby, M.C.5
  • 70
    • 34547133987 scopus 로고    scopus 로고
    • The DinG protein from Escherichia coli is a structure-specific helicase
    • O.N. Voloshin, and R.D. Camerini-Otero The DinG protein from Escherichia coli is a structure-specific helicase J Biol Chem 282 2007 18437 18447
    • (2007) J Biol Chem , vol.282 , pp. 18437-18447
    • Voloshin, O.N.1    Camerini-Otero, R.D.2
  • 71
    • 0018353521 scopus 로고
    • Enzyme-catalyzed DNA unwinding: Studies on Escherichia coli Rep protein
    • G.T. Yarranton, and M.L. Gefter Enzyme-catalyzed DNA unwinding: studies on Escherichia coli Rep protein Proc Natl Acad Sci U S A 76 1979 1658 1662
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1658-1662
    • Yarranton, G.T.1    Gefter, M.L.2
  • 72
    • 0022840629 scopus 로고
    • Escherichia coli helicase II (urvD gene product) translocates unidirectionally in a 3′ to 5′ direction
    • S.W. Matson Escherichia coli helicase II (urvD gene product) translocates unidirectionally in a 3′ to 5′ direction J Biol Chem 261 1986 10169 10175
    • (1986) J Biol Chem , vol.261 , pp. 10169-10175
    • Matson, S.W.1
  • 73
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication
    • M.A. Petit, E. Dervyn, M. Rose, K.D. Entian, S. McGovern, and S.D. Ehrlich PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication Mol Microbiol 29 1998 261 273
    • (1998) Mol Microbiol , vol.29 , pp. 261-273
    • Petit, M.A.1    Dervyn, E.2    Rose, M.3    Entian, K.D.4    McGovern, S.5    Ehrlich, S.D.6
  • 74
    • 0035985219 scopus 로고    scopus 로고
    • Schizosaccharomyces pombe pfh1+ encodes an essential 5′ to 3′ DNA helicase that is a member of the PIF1 subfamily of DNA helicases
    • J.Q. Zhou, H. Qi, V.P. Schulz, M.K. Mateyak, E.K. Monson, and V.A. Zakian Schizosaccharomyces pombe pfh1+ encodes an essential 5′ to 3′ DNA helicase that is a member of the PIF1 subfamily of DNA helicases Mol Biol Cell 13 2002 2180 2191
    • (2002) Mol Biol Cell , vol.13 , pp. 2180-2191
    • Zhou, J.Q.1    Qi, H.2    Schulz, V.P.3    Mateyak, M.K.4    Monson, E.K.5    Zakian, V.A.6
  • 76
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • S. Korolev, J. Hsieh, G.H. Gauss, T.M. Lohman, and G. Waksman Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP Cell 90 1997 635 647
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 77
    • 79951572633 scopus 로고    scopus 로고
    • Localization of an accessory helicase at the replisome is critical in sustaining efficient genome duplication
    • J. Atkinson, M.K. Gupta, C.J. Rudolph, H. Bell, R.G. Lloyd, and P. McGlynn Localization of an accessory helicase at the replisome is critical in sustaining efficient genome duplication Nucleic Acids Res 39 2011 949 957
    • (2011) Nucleic Acids Res , vol.39 , pp. 949-957
    • Atkinson, J.1    Gupta, M.K.2    Rudolph, C.J.3    Bell, H.4    Lloyd, R.G.5    McGlynn, P.6
  • 78
    • 0028047403 scopus 로고
    • A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization
    • J.W. George, R.M. Brosh, and S.W. Matson A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization J Mol Biol 235 1994 424 435
    • (1994) J Mol Biol , vol.235 , pp. 424-435
    • George, J.W.1    Brosh, R.M.2    Matson, S.W.3
  • 79
    • 84885778726 scopus 로고    scopus 로고
    • The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase
    • E.J. Gwynn, A.J. Smith, C.P. Guy, N.J. Savery, P. McGlynn, and M.S. Dillingham The conserved C-terminus of the PcrA/UvrD helicase interacts directly with RNA polymerase PLoS One 8 2013 e78141
    • (2013) PLoS One , vol.8 , pp. 78141
    • Gwynn, E.J.1    Smith, A.J.2    Guy, C.P.3    Savery, N.J.4    McGlynn, P.5    Dillingham, M.S.6
  • 81
    • 0024396565 scopus 로고
    • DNA mismatch correction in a defined system
    • R.S. Lahue, K.G. Au, and P. Modrich DNA mismatch correction in a defined system Science 245 1989 160 164
    • (1989) Science , vol.245 , pp. 160-164
    • Lahue, R.S.1    Au, K.G.2    Modrich, P.3
  • 82
    • 0040581590 scopus 로고
    • Effect of DNA polymerase i and DNA helicase II on the turnover rate of UvrABC excision nuclease
    • I. Husain, B. Van Houten, D.C. Thomas, M. Abdel-Monem, and A. Sancar Effect of DNA polymerase I and DNA helicase II on the turnover rate of UvrABC excision nuclease Proc Natl Acad Sci U S A 82 1985 6774 6778
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 6774-6778
    • Husain, I.1    Van Houten, B.2    Thomas, D.C.3    Abdel-Monem, M.4    Sancar, A.5
  • 83
    • 0032524071 scopus 로고    scopus 로고
    • Escherichia coli ribosomal protein L3 stimulates the helicase activity of the Bacillus stearothermophilus PcrA helicase
    • P. Soultanas, M.S. Dillingham, and D.B. Wigley Escherichia coli ribosomal protein L3 stimulates the helicase activity of the Bacillus stearothermophilus PcrA helicase Nucleic Acids Res 26 1998 2374 2379
    • (1998) Nucleic Acids Res , vol.26 , pp. 2374-2379
    • Soultanas, P.1    Dillingham, M.S.2    Wigley, D.B.3
  • 84
    • 69449095740 scopus 로고    scopus 로고
    • Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression
    • N.Y. Yao, R.E. Georgescu, J. Finkelstein, and M.E. O'Donnell Single-molecule analysis reveals that the lagging strand increases replisome processivity but slows replication fork progression Proc Natl Acad Sci U S A 106 2009 13236 13241
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13236-13241
    • Yao, N.Y.1    Georgescu, R.E.2    Finkelstein, J.3    O'Donnell, M.E.4
  • 85
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • W. Cheng, J. Hsieh, K.M. Brendza, and T.M. Lohman E. coli Rep oligomers are required to initiate DNA unwinding in vitro J Mol Biol 310 2001 327 350
    • (2001) J Mol Biol , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 88
    • 58049202845 scopus 로고    scopus 로고
    • Impediment of E. coli UvrD by DNA-destabilizing force reveals a strained-inchworm mechanism of DNA unwinding
    • B. Sun, K.J. Wei, B. Zhang, X.H. Zhang, S.X. Dou, and M. Li Impediment of E. coli UvrD by DNA-destabilizing force reveals a strained-inchworm mechanism of DNA unwinding EMBO J 27 2008 3279 3287
    • (2008) EMBO J , vol.27 , pp. 3279-3287
    • Sun, B.1    Wei, K.J.2    Zhang, B.3    Zhang, X.H.4    Dou, S.X.5    Li, M.6
  • 89
    • 0033527761 scopus 로고    scopus 로고
    • An oligomeric form of E. coli UvrD is required for optimal helicase activity
    • J.A. Ali, N.K. Maluf, and T.M. Lohman An oligomeric form of E. coli UvrD is required for optimal helicase activity J Mol Biol 293 1999 815 834
    • (1999) J Mol Biol , vol.293 , pp. 815-834
    • Ali, J.A.1    Maluf, N.K.2    Lohman, T.M.3
  • 90
    • 0037474547 scopus 로고    scopus 로고
    • A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • N.K. Maluf, C.J. Fischer, and T.M. Lohman A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro J Mol Biol 325 2003 913 935
    • (2003) J Mol Biol , vol.325 , pp. 913-935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 91
    • 34848840105 scopus 로고    scopus 로고
    • Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro
    • A. Niedziela-Majka, M.A. Chesnik, E.J. Tomko, and T.M. Lohman Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro J Biol Chem 282 2007 27076 27085
    • (2007) J Biol Chem , vol.282 , pp. 27076-27085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Tomko, E.J.3    Lohman, T.M.4
  • 92
    • 0037057630 scopus 로고    scopus 로고
    • Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase
    • T. Ha, I. Rasnik, W. Cheng, H.P. Babcock, G.H. Gauss, and T.M. Lohman Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase Nature 419 2002 638 641
    • (2002) Nature , vol.419 , pp. 638-641
    • Ha, T.1    Rasnik, I.2    Cheng, W.3    Babcock, H.P.4    Gauss, G.H.5    Lohman, T.M.6
  • 93
    • 41849106909 scopus 로고    scopus 로고
    • Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding
    • Y. Yang, S.X. Dou, H. Ren, P.Y. Wang, X.D. Zhang, and M. Qian Evidence for a functional dimeric form of the PcrA helicase in DNA unwinding Nucleic Acids Res 36 2008 1976 1989
    • (2008) Nucleic Acids Res , vol.36 , pp. 1976-1989
    • Yang, Y.1    Dou, S.X.2    Ren, H.3    Wang, P.Y.4    Zhang, X.D.5    Qian, M.6
  • 94
    • 79959338446 scopus 로고    scopus 로고
    • Recombination hotspots and single-stranded DNA binding proteins couple DNA translocation to DNA unwinding by the AddAB helicase-nuclease
    • J.T. Yeeles, K. van Aelst, M.S. Dillingham, and F. Moreno-Herrero Recombination hotspots and single-stranded DNA binding proteins couple DNA translocation to DNA unwinding by the AddAB helicase-nuclease Mol Cell 42 2011 806 816
    • (2011) Mol Cell , vol.42 , pp. 806-816
    • Yeeles, J.T.1    Van Aelst, K.2    Dillingham, M.S.3    Moreno-Herrero, F.4
  • 96
    • 34447266733 scopus 로고    scopus 로고
    • Directional loading and stimulation of PcrA helicase by the replication initiator protein RepD
    • W. Zhang, M.S. Dillingham, C.D. Thomas, S. Allen, C.J. Roberts, and P. Soultanas Directional loading and stimulation of PcrA helicase by the replication initiator protein RepD J Mol Biol 371 2007 336 348
    • (2007) J Mol Biol , vol.371 , pp. 336-348
    • Zhang, W.1    Dillingham, M.S.2    Thomas, C.D.3    Allen, S.4    Roberts, C.J.5    Soultanas, P.6
  • 97
    • 77952803647 scopus 로고    scopus 로고
    • Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA
    • R.L. Eoff, and K.D. Raney Kinetic mechanism for DNA unwinding by multiple molecules of Dda helicase aligned on DNA Biochemistry 49 2010 4543 4553
    • (2010) Biochemistry , vol.49 , pp. 4543-4553
    • Eoff, R.L.1    Raney, K.D.2
  • 98
    • 0019864917 scopus 로고
    • Escherichia coli single-strand deoxyribonucleic acid binding protein: Stability, specificity, and kinetics of complexes with oligonucleotides and deoxyribonucleic acid
    • G. Krauss, H. Sindermann, U. Schomburg, and G. Maass Escherichia coli single-strand deoxyribonucleic acid binding protein: stability, specificity, and kinetics of complexes with oligonucleotides and deoxyribonucleic acid Biochemistry 20 1981 5346 5352
    • (1981) Biochemistry , vol.20 , pp. 5346-5352
    • Krauss, G.1    Sindermann, H.2    Schomburg, U.3    Maass, G.4
  • 99
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • T.M. Lohman, and L.B. Overman Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration J Biol Chem 260 1985 3594 3603
    • (1985) J Biol Chem , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 101
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • S. Myong, I. Rasnik, C. Joo, T.M. Lohman, and T. Ha Repetitive shuttling of a motor protein on DNA Nature 437 2005 1321 1325
    • (2005) Nature , vol.437 , pp. 1321-1325
    • Myong, S.1    Rasnik, I.2    Joo, C.3    Lohman, T.M.4    Ha, T.5
  • 102
    • 80052449840 scopus 로고    scopus 로고
    • Single-molecule nanopositioning: Structural transitions of a helicase-DNA complex during ATP hydrolysis
    • H. Balci, S. Arslan, S. Myong, T.M. Lohman, and T. Ha Single-molecule nanopositioning: structural transitions of a helicase-DNA complex during ATP hydrolysis Biophys J 101 2011 976 984
    • (2011) Biophys J , vol.101 , pp. 976-984
    • Balci, H.1    Arslan, S.2    Myong, S.3    Lohman, T.M.4    Ha, T.5
  • 103
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • S.S. Velankar, P. Soultanas, M.S. Dillingham, H.S. Subramanya, and D.B. Wigley Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism Cell 97 1999 75 84
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 104
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • P. Soultanas, M.S. Dillingham, P. Wiley, M.R. Webb, and D.B. Wigley Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism EMBO J 19 2000 3799 3810
    • (2000) EMBO J , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 105
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • J.Y. Lee, and W. Yang UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke Cell 127 2006 1349 1360
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 106
    • 77952906090 scopus 로고    scopus 로고
    • Lessons learned from UvrD helicase: Mechanism for directional movement
    • W. Yang Lessons learned from UvrD helicase: mechanism for directional movement Annu Rev Biophys 39 2010 367 385
    • (2010) Annu Rev Biophys , vol.39 , pp. 367-385
    • Yang, W.1
  • 108
    • 77957123627 scopus 로고    scopus 로고
    • Pathways of mammalian replication fork restart
    • E. Petermann, and T. Helleday Pathways of mammalian replication fork restart Nat Rev Mol Cell Biol 11 2010 683 687
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 683-687
    • Petermann, E.1    Helleday, T.2
  • 109
    • 79551661935 scopus 로고    scopus 로고
    • Cell-type-specific replication initiation programs set fragility of the FRA3B fragile site
    • A. Letessier, G.A. Millot, S. Koundrioukoff, A.M. Lachages, N. Vogt, and R.S. Hansen Cell-type-specific replication initiation programs set fragility of the FRA3B fragile site Nature 470 2011 120 123
    • (2011) Nature , vol.470 , pp. 120-123
    • Letessier, A.1    Millot, G.A.2    Koundrioukoff, S.3    Lachages, A.M.4    Vogt, N.5    Hansen, R.S.6
  • 110
    • 79959885574 scopus 로고    scopus 로고
    • Failure of origin activation in response to fork stalling leads to chromosomal instability at fragile sites
    • E. Ozeri-Galai, R. Lebofsky, A. Rahat, A.C. Bester, A. Bensimon, and B. Kerem Failure of origin activation in response to fork stalling leads to chromosomal instability at fragile sites Mol Cell 43 2011 122 131
    • (2011) Mol Cell , vol.43 , pp. 122-131
    • Ozeri-Galai, E.1    Lebofsky, R.2    Rahat, A.3    Bester, A.C.4    Bensimon, A.5    Kerem, B.6
  • 111
    • 38549138271 scopus 로고    scopus 로고
    • Smc5/6: A link between DNA repair and unidirectional replication?
    • J.M. Murray, and A.M. Carr Smc5/6: a link between DNA repair and unidirectional replication? Nat Rev Mol Cell Biol 9 2008 177 182
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 177-182
    • Murray, J.M.1    Carr, A.M.2
  • 112
    • 0028954628 scopus 로고
    • Recombinational rescue of the stalled DNA replication fork: A model based on analysis of an Escherichia coli strain with a chromosome region difficult to replicate
    • T. Horiuchi, and Y. Fujimura Recombinational rescue of the stalled DNA replication fork: a model based on analysis of an Escherichia coli strain with a chromosome region difficult to replicate J Bacteriol 177 1995 783 791
    • (1995) J Bacteriol , vol.177 , pp. 783-791
    • Horiuchi, T.1    Fujimura, Y.2
  • 113
    • 20444424939 scopus 로고    scopus 로고
    • Gross chromosomal rearrangements and elevated recombination at an inducible site-specific replication fork barrier
    • S. Lambert, A. Watson, D.M. Sheedy, B. Martin, and A.M. Carr Gross chromosomal rearrangements and elevated recombination at an inducible site-specific replication fork barrier Cell 121 2005 689 702
    • (2005) Cell , vol.121 , pp. 689-702
    • Lambert, S.1    Watson, A.2    Sheedy, D.M.3    Martin, B.4    Carr, A.M.5
  • 114
    • 84887402750 scopus 로고    scopus 로고
    • Replication stress-induced genome instability: The dark side of replication maintenance by homologous recombination
    • A.M. Carr, and S. Lambert Replication stress-induced genome instability: the dark side of replication maintenance by homologous recombination J Mol Biol 425 2013 4733 4744
    • (2013) J Mol Biol , vol.425 , pp. 4733-4744
    • Carr, A.M.1    Lambert, S.2
  • 115
    • 0037124327 scopus 로고    scopus 로고
    • Essential bacterial helicases that counteract the toxicity of recombination proteins
    • M.A. Petit, and D. Ehrlich Essential bacterial helicases that counteract the toxicity of recombination proteins EMBO J 21 2002 3137 3147
    • (2002) EMBO J , vol.21 , pp. 3137-3147
    • Petit, M.A.1    Ehrlich, D.2
  • 116
    • 84856801304 scopus 로고    scopus 로고
    • A genomewide screen for suppressors of Alu-mediated rearrangements reveals a role for PIF1
    • K.M. Chisholm, S.D. Aubert, K.P. Freese, V.A. Zakian, M.C. King, and P.L. Welcsh A genomewide screen for suppressors of Alu-mediated rearrangements reveals a role for PIF1 PLoS One 7 2012 e30748
    • (2012) PLoS One , vol.7 , pp. 30748
    • Chisholm, K.M.1    Aubert, S.D.2    Freese, K.P.3    Zakian, V.A.4    King, M.C.5    Welcsh, P.L.6
  • 117
    • 79957556530 scopus 로고    scopus 로고
    • DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase
    • K. Paeschke, J.A. Capra, and V.A. Zakian DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase Cell 145 2011 678 691
    • (2011) Cell , vol.145 , pp. 678-691
    • Paeschke, K.1    Capra, J.A.2    Zakian, V.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.