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Volumn 1, Issue , 2016, Pages 396-417

Comparison of Bacterial and Eukaryotic Replisome Components

Author keywords

Clamp loader; CMG; DNA polymerase; DNA replication; Evolution; Helicase; Primase; Replisome; Single strand binding protein; Sliding clamp

Indexed keywords


EID: 85042340667     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-394447-4.10038-0     Document Type: Chapter
Times cited : (4)

References (232)
  • 1
    • 0031465797 scopus 로고    scopus 로고
    • Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5'- and 3'-tails of the forked DNA substrate
    • Ahnert P., Patel S.S. Asymmetric interactions of hexameric bacteriophage T7 DNA helicase with the 5'- and 3'-tails of the forked DNA substrate. Journal of Biological Chemistry 1997, 272:32267-32273.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 32267-32273
    • Ahnert, P.1    Patel, S.S.2
  • 3
    • 0032530488 scopus 로고    scopus 로고
    • Toprim - A conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins
    • Aravind L., Leipe D.D., Koonin E.V. Toprim - A conserved catalytic domain in type IA and II topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins. Nucleic Acids Research 1998, 26:4205-4213.
    • (1998) Nucleic Acids Research , vol.26 , pp. 4205-4213
    • Aravind, L.1    Leipe, D.D.2    Koonin, E.V.3
  • 4
    • 0142135087 scopus 로고    scopus 로고
    • Independent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains
    • Arunkumar A.I., Stauffer M.E., Bochkareva E., Bochkarev A., Chazin W.J. Independent and coordinated functions of replication protein A tandem high affinity single-stranded DNA binding domains. Journal of Biological Chemistry 2003, 278:41077-41082.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 41077-41082
    • Arunkumar, A.I.1    Stauffer, M.E.2    Bochkareva, E.3    Bochkarev, A.4    Chazin, W.J.5
  • 5
    • 0038193630 scopus 로고    scopus 로고
    • Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp
    • Ason B., Handayani R., Williams C.R., et al. Mechanism of loading the Escherichia coli DNA polymerase III beta sliding clamp on DNA. Bona fide primer/templates preferentially trigger the gamma complex to hydrolyze ATP and load the clamp. Journal of Biological Chemistry 2003, 278:10033-10040.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 10033-10040
    • Ason, B.1    Handayani, R.2    Williams, C.R.3
  • 7
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S., Eliason W.K., Steitz T.A. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 2007, 318:459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 8
    • 33748146034 scopus 로고    scopus 로고
    • The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
    • Bailey S., Wing R.A., Steitz T.A. The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell 2006, 126:893-904.
    • (2006) Cell , vol.126 , pp. 893-904
    • Bailey, S.1    Wing, R.A.2    Steitz, T.A.3
  • 10
    • 84877613987 scopus 로고    scopus 로고
    • A structural role for the PHP domain in E. coli DNA polymerase III
    • Barros T., Guenther J., Kelch B., et al. A structural role for the PHP domain in E. coli DNA polymerase III. BMC Structural Biology 2013, 13:8.
    • (2013) BMC Structural Biology , vol.13 , pp. 8
    • Barros, T.1    Guenther, J.2    Kelch, B.3
  • 11
    • 0035965188 scopus 로고    scopus 로고
    • Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding
    • Bastin-Shanower S.A., Brill S.J. Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding. Journal of Biological Chemistry 2001, 276:36446-36453.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 36446-36453
    • Bastin-Shanower, S.A.1    Brill, S.J.2
  • 13
    • 0026019625 scopus 로고
    • Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism. EMBO Journal 1991, 10:25-33.
    • (1991) EMBO Journal , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 17
  • 18
    • 77951244549 scopus 로고    scopus 로고
    • Influence of the human cohesion establishment factor Ctf4/AND-1 on DNA replication
    • Bermudez V.P., Farina A., Tappin I., Hurwitz J. Influence of the human cohesion establishment factor Ctf4/AND-1 on DNA replication. Journal of Biological Chemistry 2010, 285:9493-9505.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 9493-9505
    • Bermudez, V.P.1    Farina, A.2    Tappin, I.3    Hurwitz, J.4
  • 19
    • 84888190793 scopus 로고    scopus 로고
    • PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replication
    • Bianchi J., Rudd S.G., Jozwiakowski S.K., et al. PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA replication. Molecular Cell 2013, 52:566-573.
    • (2013) Molecular Cell , vol.52 , pp. 566-573
    • Bianchi, J.1    Rudd, S.G.2    Jozwiakowski, S.K.3
  • 20
    • 1342302794 scopus 로고    scopus 로고
    • From RPA to BRCA2: Lessons from single-stranded DNA binding by the OB-fold
    • Bochkarev A., Bochkareva E. From RPA to BRCA2: Lessons from single-stranded DNA binding by the OB-fold. Current Opinion in Structural Biology 2004, 14:36-42.
    • (2004) Current Opinion in Structural Biology , vol.14 , pp. 36-42
    • Bochkarev, A.1    Bochkareva, E.2
  • 21
    • 0037007223 scopus 로고    scopus 로고
    • Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA
    • Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A. Structure of the RPA trimerization core and its role in the multistep DNA-binding mechanism of RPA. EMBO Journal 2002, 21:1855-1863.
    • (2002) EMBO Journal , vol.21 , pp. 1855-1863
    • Bochkareva, E.1    Korolev, S.2    Lees-Miller, S.P.3    Bochkarev, A.4
  • 22
    • 52649096993 scopus 로고    scopus 로고
    • Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability
    • Bochman M.L., Bell S.P., Schwacha A. Subunit organization of Mcm2-7 and the unequal role of active sites in ATP hydrolysis and viability. Molecular and Cellular Biology 2008, 28:5865-5873.
    • (2008) Molecular and Cellular Biology , vol.28 , pp. 5865-5873
    • Bochman, M.L.1    Bell, S.P.2    Schwacha, A.3
  • 23
    • 47349114465 scopus 로고    scopus 로고
    • The Mcm2-7 complex has in vitro helicase activity
    • Bochman M.L., Schwacha A. The Mcm2-7 complex has in vitro helicase activity. Molecular Cell 2008, 31:287-293.
    • (2008) Molecular Cell , vol.31 , pp. 287-293
    • Bochman, M.L.1    Schwacha, A.2
  • 24
    • 0035916786 scopus 로고    scopus 로고
    • Archaeal primase: Bridging the gap between RNA and DNA polymerases
    • Bocquier A.A., Liu L., Cann I.K., et al. Archaeal primase: Bridging the gap between RNA and DNA polymerases. Current Biology 2001, 11:452-456.
    • (2001) Current Biology , vol.11 , pp. 452-456
    • Bocquier, A.A.1    Liu, L.2    Cann, I.K.3
  • 26
    • 3042588011 scopus 로고    scopus 로고
    • Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex
    • Bowman G.D., O'Donnell M., Kuriyan J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature 2004, 429:724-730.
    • (2004) Nature , vol.429 , pp. 724-730
    • Bowman, G.D.1    O'Donnell, M.2    Kuriyan, J.3
  • 28
    • 84875197858 scopus 로고    scopus 로고
    • Cdc45 protein-single-stranded DNA interaction is important for stalling the helicase during replication stress
    • Bruck I., Kaplan D.L. Cdc45 protein-single-stranded DNA interaction is important for stalling the helicase during replication stress. Journal of Biological Chemistry 2013, 288:7550-7563.
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 7550-7563
    • Bruck, I.1    Kaplan, D.L.2
  • 30
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers P.M. Polymerase dynamics at the eukaryotic DNA replication fork. Journal of Biological Chemistry 2009, 284:4041-4045.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 4041-4045
    • Burgers, P.M.1
  • 31
    • 84880524629 scopus 로고    scopus 로고
    • Insights into Okazaki fragment synthesis by the T4 replisome: The fate of lagging-strand holoenzyme components and their influence on Okazaki fragment size
    • Chen D., Yue H., Spiering M.M., Benkovic S.J. Insights into Okazaki fragment synthesis by the T4 replisome: The fate of lagging-strand holoenzyme components and their influence on Okazaki fragment size. Journal of Biological Chemistry 2013, 288:20807-20816.
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 20807-20816
    • Chen, D.1    Yue, H.2    Spiering, M.M.3    Benkovic, S.J.4
  • 32
    • 77956217627 scopus 로고    scopus 로고
    • Evolution of DNA replication protein complexes in eukaryotes and Archaea
    • Chia N., Cann I., Olsen G.J. Evolution of DNA replication protein complexes in eukaryotes and Archaea. PLoS One 2010, 5:e10866.
    • (2010) PLoS One , vol.5
    • Chia, N.1    Cann, I.2    Olsen, G.J.3
  • 33
    • 36248991353 scopus 로고    scopus 로고
    • The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA
    • Chilkova O., Stenlund P., Isoz I., et al. The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA. Nucleic Acids Research 2007, 35:6588-6597.
    • (2007) Nucleic Acids Research , vol.35 , pp. 6588-6597
    • Chilkova, O.1    Stenlund, P.2    Isoz, I.3
  • 36
    • 0027379095 scopus 로고
    • Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication
    • Copeland W.C., Wang T.S. Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication. Journal of Biological Chemistry 1993, 268:26179-26189.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 26179-26189
    • Copeland, W.C.1    Wang, T.S.2
  • 38
    • 79953769723 scopus 로고    scopus 로고
    • The structural basis for MCM2-7 helicase activation by GINS and Cdc45
    • Costa A., Ilves I., Tamberg N., et al. The structural basis for MCM2-7 helicase activation by GINS and Cdc45. Nature Structural & Molecular Biology 2011, 18:471-477.
    • (2011) Nature Structural & Molecular Biology , vol.18 , pp. 471-477
    • Costa, A.1    Ilves, I.2    Tamberg, N.3
  • 39
    • 0029150469 scopus 로고
    • Characterization of the five replication factor C genes of Saccharomyces cerevisiae
    • Cullmann G., Fien K., Kobayashi R., Stillman B. Characterization of the five replication factor C genes of Saccharomyces cerevisiae. Molecular and Cellular Biology 1995, 15:4661-4671.
    • (1995) Molecular and Cellular Biology , vol.15 , pp. 4661-4671
    • Cullmann, G.1    Fien, K.2    Kobayashi, R.3    Stillman, B.4
  • 40
    • 0034686075 scopus 로고    scopus 로고
    • Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks
    • Dallmann H.G., Kim S., Pritchard A.E., Marians K.J., McHenry C.S. Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks. Journal of Biological Chemistry 2000, 275:15512-15519.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 15512-15519
    • Dallmann, H.G.1    Kim, S.2    Pritchard, A.E.3    Marians, K.J.4    McHenry, C.S.5
  • 42
    • 84879403234 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen structure and interactions: Too many partners for one dancer?
    • De Biasio A., Blanco F.J. Proliferating cell nuclear antigen structure and interactions: Too many partners for one dancer?. Advances in Protein Chemistry and Structural Biology 2013, 91:1-36.
    • (2013) Advances in Protein Chemistry and Structural Biology , vol.91 , pp. 1-36
    • De Biasio, A.1    Blanco, F.J.2
  • 43
    • 0035836479 scopus 로고    scopus 로고
    • Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork
    • Delagoutte E., von Hippel P.H. Molecular mechanisms of the functional coupling of the helicase (gp41) and polymerase (gp43) of bacteriophage T4 within the DNA replication fork. Biochemistry 2001, 40:4459-4477.
    • (2001) Biochemistry , vol.40 , pp. 4459-4477
    • Delagoutte, E.1    von Hippel, P.H.2
  • 44
    • 84858053395 scopus 로고    scopus 로고
    • Replisome stability at defective DNA replication forks is independent of S phase checkpoint kinases
    • De Piccoli G., Katou Y., Itoh T., et al. Replisome stability at defective DNA replication forks is independent of S phase checkpoint kinases. Molecular Cell 2012, 45:696-704.
    • (2012) Molecular Cell , vol.45 , pp. 696-704
    • De Piccoli, G.1    Katou, Y.2    Itoh, T.3
  • 45
    • 84860527731 scopus 로고    scopus 로고
    • Mcm10 associates with the loaded DNA helicase at replication origins and defines a novel step in its activation
    • van Deursen F., Sengupta S., De Piccoli G., Sanchez-Diaz A., Labib K. Mcm10 associates with the loaded DNA helicase at replication origins and defines a novel step in its activation. EMBO Journal 2012, 31:2195-2206.
    • (2012) EMBO Journal , vol.31 , pp. 2195-2206
    • van Deursen, F.1    Sengupta, S.2    De Piccoli, G.3    Sanchez-Diaz, A.4    Labib, K.5
  • 47
    • 0029905072 scopus 로고    scopus 로고
    • A coupled complex of T4 DNA replication helicase (gp41) and polymerase (gp43) can perform rapid and processive DNA strand-displacement synthesis
    • Dong F., Weitzel S.E., von Hippel P.H. A coupled complex of T4 DNA replication helicase (gp41) and polymerase (gp43) can perform rapid and processive DNA strand-displacement synthesis. Proceedings of the National Academy of Sciences of the United States of America 1996, 93:14456-14461.
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 14456-14461
    • Dong, F.1    Weitzel, S.E.2    von Hippel, P.H.3
  • 48
    • 33749121811 scopus 로고    scopus 로고
    • Mechanisms of a ring shaped helicase
    • Donmez I., Patel S.S. Mechanisms of a ring shaped helicase. Nucleic Acids Research 2006, 34:4216-4224.
    • (2006) Nucleic Acids Research , vol.34 , pp. 4216-4224
    • Donmez, I.1    Patel, S.S.2
  • 49
    • 47049093279 scopus 로고    scopus 로고
    • Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase
    • Donmez I., Patel S.S. Coupling of DNA unwinding to nucleotide hydrolysis in a ring-shaped helicase. EMBO Journal 2008, 27:1718-1726.
    • (2008) EMBO Journal , vol.27 , pp. 1718-1726
    • Donmez, I.1    Patel, S.S.2
  • 50
    • 0033080970 scopus 로고    scopus 로고
    • An open and closed case for all polymerases
    • Doublie S., Sawaya M.R., Ellenberger T. An open and closed case for all polymerases. Structure 1999, 7:R31-R35.
    • (1999) Structure , vol.7 , pp. R31-R35
    • Doublie, S.1    Sawaya, M.R.2    Ellenberger, T.3
  • 52
    • 0032489391 scopus 로고    scopus 로고
    • Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity
    • Ellison V., Stillman B. Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity. Journal of Biological Chemistry 1998, 273:5979-5987.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 5979-5987
    • Ellison, V.1    Stillman, B.2
  • 53
    • 33746375404 scopus 로고    scopus 로고
    • Mechanism of DNA translocation in a replicative hexameric helicase
    • Enemark E.J., Joshua-Tor L. Mechanism of DNA translocation in a replicative hexameric helicase. Nature 2006, 442:270-275.
    • (2006) Nature , vol.442 , pp. 270-275
    • Enemark, E.J.1    Joshua-Tor, L.2
  • 57
    • 33749134033 scopus 로고    scopus 로고
    • A dynamic model for replication protein A (RPA) function in DNA processing pathways
    • Fanning E., Klimovich V., Nager A.R. A dynamic model for replication protein A (RPA) function in DNA processing pathways. Nucleic Acids Research 2006, 34:4126-4137.
    • (2006) Nucleic Acids Research , vol.34 , pp. 4126-4137
    • Fanning, E.1    Klimovich, V.2    Nager, A.R.3
  • 58
    • 59449094309 scopus 로고    scopus 로고
    • SV40 DNA replication: From the A gene to a nanomachine
    • Fanning E., Zhao K. SV40 DNA replication: From the A gene to a nanomachine. Virology 2009, 384:352-359.
    • (2009) Virology , vol.384 , pp. 352-359
    • Fanning, E.1    Zhao, K.2
  • 59
    • 0026543506 scopus 로고
    • Identification of replication factor C from Saccharomyces cerevisiae: A component of the leading-strand DNA replication complex
    • Fien K., Stillman B. Identification of replication factor C from Saccharomyces cerevisiae: A component of the leading-strand DNA replication complex. Molecular and Cellular Biology 1992, 12:155-163.
    • (1992) Molecular and Cellular Biology , vol.12 , pp. 155-163
    • Fien, K.1    Stillman, B.2
  • 60
    • 77954589779 scopus 로고    scopus 로고
    • Oligonucleotide/oligosaccharide-binding fold proteins: A growing family of genome guardians
    • Flynn R.L., Zou L. Oligonucleotide/oligosaccharide-binding fold proteins: A growing family of genome guardians. Critical Reviews in Biochemistry and Molecular Biology 2010, 45:266-275.
    • (2010) Critical Reviews in Biochemistry and Molecular Biology , vol.45 , pp. 266-275
    • Flynn, R.L.1    Zou, L.2
  • 61
    • 84890035918 scopus 로고    scopus 로고
    • The common ancestor of archaea and eukarya was not an archaeon
    • Forterre P. The common ancestor of archaea and eukarya was not an archaeon. Archaea 2013, 2013:372396.
    • (2013) Archaea , vol.2013 , pp. 372396
    • Forterre, P.1
  • 64
    • 70350572751 scopus 로고    scopus 로고
    • A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome
    • Gambus A., van Deursen F., Polychronopoulos D., et al. A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome. EMBO Journal 2009, 28:2992-3004.
    • (2009) EMBO Journal , vol.28 , pp. 2992-3004
    • Gambus, A.1    van Deursen, F.2    Polychronopoulos, D.3
  • 65
    • 33645717628 scopus 로고    scopus 로고
    • GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks
    • Gambus A., Jones R.C., Sanchez-Diaz A., et al. GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks. Nature Cell Biology 2006, 8:358-366.
    • (2006) Nature Cell Biology , vol.8 , pp. 358-366
    • Gambus, A.1    Jones, R.C.2    Sanchez-Diaz, A.3
  • 66
    • 84855198651 scopus 로고    scopus 로고
    • Requirement of replication checkpoint protein kinases Mec1/Rad53 for postreplication repair in yeast
    • Gangavarapu V., Santa Maria S.R., Prakash S., Prakash L. Requirement of replication checkpoint protein kinases Mec1/Rad53 for postreplication repair in yeast. MBio 2011, 2:e00079-00011.
    • (2011) MBio , vol.2
    • Gangavarapu, V.1    Santa Maria, S.R.2    Prakash, S.3    Prakash, L.4
  • 67
    • 0035830834 scopus 로고    scopus 로고
    • Tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of tau, binds the replication fork, helicase, DnaB
    • Gao D., McHenry C.S. Tau binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of tau, binds the replication fork, helicase, DnaB. Journal of Biological Chemistry 2001, 276:4441-4446.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 4441-4446
    • Gao, D.1    McHenry, C.S.2
  • 68
    • 84888205939 scopus 로고    scopus 로고
    • PrimPol, an archaic primase/polymerase operating in human cells
    • Garcia-Gomez S., Reyes A., Martinez-Jimenez M.I., et al. PrimPol, an archaic primase/polymerase operating in human cells. Molecular Cell 2013, 52:541-553.
    • (2013) Molecular Cell , vol.52 , pp. 541-553
    • Garcia-Gomez, S.1    Reyes, A.2    Martinez-Jimenez, M.I.3
  • 71
    • 84885869576 scopus 로고    scopus 로고
    • A single-molecule view of DNA replication: The dynamic nature of multi-protein complexes revealed
    • Geertsema H.J., van Oijen A.M. A single-molecule view of DNA replication: The dynamic nature of multi-protein complexes revealed. Current Opinion in Structural Biology 2013, 23:788-793.
    • (2013) Current Opinion in Structural Biology , vol.23 , pp. 788-793
    • Geertsema, H.J.1    van Oijen, A.M.2
  • 72
    • 84855453503 scopus 로고    scopus 로고
    • Single-molecule studies reveal the function of a third polymerase in the replisome
    • Georgescu R.E., Kurth I., O'Donnell M.E. Single-molecule studies reveal the function of a third polymerase in the replisome. Nature Structural & Molecular Biology 2011, 19:113-116.
    • (2011) Nature Structural & Molecular Biology , vol.19 , pp. 113-116
    • Georgescu, R.E.1    Kurth, I.2    O'Donnell, M.E.3
  • 73
    • 70350564160 scopus 로고    scopus 로고
    • Mechanism of polymerase collision release from sliding clamps on the lagging strand
    • Georgescu R.E., Kurth I., Yao N.Y., et al. Mechanism of polymerase collision release from sliding clamps on the lagging strand. EMBO Journal 2009, 28:2981-2991.
    • (2009) EMBO Journal , vol.28 , pp. 2981-2991
    • Georgescu, R.E.1    Kurth, I.2    Yao, N.Y.3
  • 74
    • 84906101503 scopus 로고    scopus 로고
    • Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork
    • Georgescu R.E., Langston L.D., Yao N.Y., et al. Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork. Nature Structural & Molecular Biology 2014, 21:664-670.
    • (2014) Nature Structural & Molecular Biology , vol.21 , pp. 664-670
    • Georgescu, R.E.1    Langston, L.D.2    Yao, N.Y.3
  • 75
    • 0034640522 scopus 로고    scopus 로고
    • Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain
    • Gomes X.V., Gary S.L., Burgers P.M. Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain. Journal of Biological Chemistry 2000, 275:14541-14549.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 14541-14549
    • Gomes, X.V.1    Gary, S.L.2    Burgers, P.M.3
  • 77
    • 80053576584 scopus 로고    scopus 로고
    • Steric exclusion and wrapping of the excluded DNA strand occurs along discrete external binding paths during MCM helicase unwinding
    • Graham B.W., Schauer G.D., Leuba S.H., Trakselis M.A. Steric exclusion and wrapping of the excluded DNA strand occurs along discrete external binding paths during MCM helicase unwinding. Nucleic Acids Research 2011, 39:6585-6595.
    • (2011) Nucleic Acids Research , vol.39 , pp. 6585-6595
    • Graham, B.W.1    Schauer, G.D.2    Leuba, S.H.3    Trakselis, M.A.4
  • 78
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III
    • Guenther B., Onrust R., Sali A., O'Donnell M., Kuriyan J. Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 1997, 91:335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 79
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell 1996, 87:297-306.
    • (1996) Cell , vol.87 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 80
    • 0028147234 scopus 로고
    • The rapid dissociation of the T4 DNA polymerase holoenzyme when stopped by a DNA hairpin helix. A model for polymerase release following the termination of each Okazaki fragment
    • Hacker K.J., Alberts B.M. The rapid dissociation of the T4 DNA polymerase holoenzyme when stopped by a DNA hairpin helix. A model for polymerase release following the termination of each Okazaki fragment. Journal of Biological Chemistry 1994, 269:24221-24228.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 24221-24228
    • Hacker, K.J.1    Alberts, B.M.2
  • 81
    • 0030670510 scopus 로고    scopus 로고
    • A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
    • Hacker K.J., Johnson K.A. A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding. Biochemistry 1997, 36:14080-14087.
    • (1997) Biochemistry , vol.36 , pp. 14080-14087
    • Hacker, K.J.1    Johnson, K.A.2
  • 82
    • 58249114971 scopus 로고    scopus 로고
    • Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis
    • Hamdan S.M., Loparo J.J., Takahashi M., Richardson C.C., van Oijen A.M. Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis. Nature 2009, 457:336-339.
    • (2009) Nature , vol.457 , pp. 336-339
    • Hamdan, S.M.1    Loparo, J.J.2    Takahashi, M.3    Richardson, C.C.4    van Oijen, A.M.5
  • 83
    • 79959957543 scopus 로고    scopus 로고
    • Eukaryotic origin-dependent DNA replication in vitro reveals sequential action of DDK and S-CDK kinases
    • Heller R.C., Kang S., Lam W.M., et al. Eukaryotic origin-dependent DNA replication in vitro reveals sequential action of DDK and S-CDK kinases. Cell 2011, 146:80-91.
    • (2011) Cell , vol.146 , pp. 80-91
    • Heller, R.C.1    Kang, S.2    Lam, W.M.3
  • 84
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • von Hippel P.H., Delagoutte E. A general model for nucleic acid helicases and their "coupling" within macromolecular machines. Cell 2001, 104:177-190.
    • (2001) Cell , vol.104 , pp. 177-190
    • von Hippel, P.H.1    Delagoutte, E.2
  • 85
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege C., Pfander B., Moldovan G.L., Pyrowolakis G., Jentsch S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002, 419:135-141.
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 86
    • 81855189485 scopus 로고    scopus 로고
    • Visualization of eukaryotic DNA mismatch repair reveals distinct recognition and repair intermediates
    • Hombauer H., Campbell C.S., Smith C.E., Desai A., Kolodner R.D. Visualization of eukaryotic DNA mismatch repair reveals distinct recognition and repair intermediates. Cell 2011, 147:1040-1053.
    • (2011) Cell , vol.147 , pp. 1040-1053
    • Hombauer, H.1    Campbell, C.S.2    Smith, C.E.3    Desai, A.4    Kolodner, R.D.5
  • 87
    • 84869049178 scopus 로고    scopus 로고
    • The human lagging strand DNA polymerase delta holoenzyme is distributive
    • Hu Z., Perumal S.K., Yue H., Benkovic S.J. The human lagging strand DNA polymerase delta holoenzyme is distributive. Journal of Biological Chemistry 2012, 287:38442-38448.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 38442-38448
    • Hu, Z.1    Perumal, S.K.2    Yue, H.3    Benkovic, S.J.4
  • 90
    • 0034601672 scopus 로고    scopus 로고
    • 5' --> 3' molecular polarity of human replication protein A (hRPA) binding to pseudo-origin DNA substrates
    • Iftode C., Borowiec J.A. 5' --> 3' molecular polarity of human replication protein A (hRPA) binding to pseudo-origin DNA substrates. Biochemistry 2000, 39:11970-11981.
    • (2000) Biochemistry , vol.39 , pp. 11970-11981
    • Iftode, C.1    Borowiec, J.A.2
  • 91
    • 74749095240 scopus 로고    scopus 로고
    • Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins
    • Ilves I., Petojevic T., Pesavento J.J., Botchan M.R. Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins. Molecular Cell 2010, 37:247-258.
    • (2010) Molecular Cell , vol.37 , pp. 247-258
    • Ilves, I.1    Petojevic, T.2    Pesavento, J.J.3    Botchan, M.R.4
  • 94
    • 84899696054 scopus 로고    scopus 로고
    • The archaeal DNA replication machinery: Past, present and future
    • Ishino S., Kelman L.M., Kelman Z., Ishino Y. The archaeal DNA replication machinery: Past, present and future. Genes & Genetic Systems 2013, 88:315-319.
    • (2013) Genes & Genetic Systems , vol.88 , pp. 315-319
    • Ishino, S.1    Kelman, L.M.2    Kelman, Z.3    Ishino, Y.4
  • 95
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O., Wing R.A., Eliason W.K., Wang J., Steitz T.A. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 2012, 151:267-277.
    • (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
  • 97
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III
    • Jeruzalmi D., O'Donnell M., Kuriyan J. Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 2001, 106:429-441.
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 99
  • 100
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • Johnson A., O'Donnell M. Cellular DNA replicases: Components and dynamics at the replication fork. Annual Review of Biochemistry 2005, 74:283-315.
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 283-315
    • Johnson, A.1    O'Donnell, M.2
  • 102
    • 34250766751 scopus 로고    scopus 로고
    • Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase
    • Johnson D.S., Bai L., Smith B.Y., Patel S.S., Wang M.D. Single-molecule studies reveal dynamics of DNA unwinding by the ring-shaped T7 helicase. Cell 2007, 129:1299-1309.
    • (2007) Cell , vol.129 , pp. 1299-1309
    • Johnson, D.S.1    Bai, L.2    Smith, B.Y.3    Patel, S.S.4    Wang, M.D.5
  • 105
    • 44949114390 scopus 로고    scopus 로고
    • Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity
    • Joyce C.M., Potapova O., Delucia A.M., et al. Fingers-closing and other rapid conformational changes in DNA polymerase I (Klenow fragment) and their role in nucleotide selectivity. Biochemistry 2008, 47:6103-6116.
    • (2008) Biochemistry , vol.47 , pp. 6103-6116
    • Joyce, C.M.1    Potapova, O.2    Delucia, A.M.3
  • 106
    • 0021099814 scopus 로고
    • Association of DNA primase with the beta/gamma subunits of DNA polymerase alpha from Drosophila melanogaster embryos
    • Kaguni L.S., Rossignol J.M., Conaway R.C., Banks G.R., Lehman I.R. Association of DNA primase with the beta/gamma subunits of DNA polymerase alpha from Drosophila melanogaster embryos. Journal of Biological Chemistry 1983, 258:9037-9039.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 9037-9039
    • Kaguni, L.S.1    Rossignol, J.M.2    Conaway, R.C.3    Banks, G.R.4    Lehman, I.R.5
  • 110
    • 84862786939 scopus 로고    scopus 로고
    • Mcm10 plays an essential role in origin DNA unwinding after loading of the CMG components
    • Kanke M., Kodama Y., Takahashi T.S., Nakagawa T., Masukata H. Mcm10 plays an essential role in origin DNA unwinding after loading of the CMG components. EMBO Journal 2012, 31:2182-2194.
    • (2012) EMBO Journal , vol.31 , pp. 2182-2194
    • Kanke, M.1    Kodama, Y.2    Takahashi, T.S.3    Nakagawa, T.4    Masukata, H.5
  • 111
    • 0034737468 scopus 로고    scopus 로고
    • Structure of the RNA polymerase domain of E. coli primase
    • Keck J.L., Roche D.D., Lynch A.S., Berger J.M. Structure of the RNA polymerase domain of E. coli primase. Science 2000, 287:2482-2486.
    • (2000) Science , vol.287 , pp. 2482-2486
    • Keck, J.L.1    Roche, D.D.2    Lynch, A.S.3    Berger, J.M.4
  • 113
    • 84455163347 scopus 로고    scopus 로고
    • How a DNA polymerase clamp loader opens a sliding clamp
    • Kelch B.A., Makino D.L., O'Donnell M., Kuriyan J. How a DNA polymerase clamp loader opens a sliding clamp. Science 2011, 334:1675-1680.
    • (2011) Science , vol.334 , pp. 1675-1680
    • Kelch, B.A.1    Makino, D.L.2    O'Donnell, M.3    Kuriyan, J.4
  • 114
    • 84859914242 scopus 로고    scopus 로고
    • Clamp loader ATPases and the evolution of DNA replication machinery
    • Kelch B.A., Makino D.L., O'Donnell M., Kuriyan J. Clamp loader ATPases and the evolution of DNA replication machinery. BMC Biology 2012, 10(34). 10.1186/1741-7007-10-34.
    • (2012) BMC Biology , vol.10 , Issue.34
    • Kelch, B.A.1    Makino, D.L.2    O'Donnell, M.3    Kuriyan, J.4
  • 116
    • 0027939024 scopus 로고
    • Interactions of human replication protein A with oligonucleotides
    • Kim C., Paulus B.F., Wold M.S. Interactions of human replication protein A with oligonucleotides. Biochemistry 1994, 33:14197-14206.
    • (1994) Biochemistry , vol.33 , pp. 14197-14206
    • Kim, C.1    Paulus, B.F.2    Wold, M.S.3
  • 117
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A tau-DnaB interaction mediates rapid replication fork movement
    • Kim S., Dallmann H.G., McHenry C.S., Marians K.J. Coupling of a replicative polymerase and helicase: A tau-DnaB interaction mediates rapid replication fork movement. Cell 1996, 84:643-650.
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 118
    • 0033564245 scopus 로고    scopus 로고
    • Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology
    • Kirk B.W., Kuchta R.D. Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology. Biochemistry 1999, 38:7727-7736.
    • (1999) Biochemistry , vol.38 , pp. 7727-7736
    • Kirk, B.W.1    Kuchta, R.D.2
  • 121
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong X.P., Onrust R., O'Donnell M., Kuriyan J. Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: A sliding DNA clamp. Cell 1992, 69:425-437.
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    O'Donnell, M.3    Kuriyan, J.4
  • 123
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna T.S., Kong X.P., Gary S., Burgers P.M., Kuriyan J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 1994, 79:1233-1243.
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 124
    • 0020417286 scopus 로고
    • Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena
    • Kruger K., Grabowski P.J., Zaug A.J., et al. Self-splicing RNA: Autoexcision and autocyclization of the ribosomal RNA intervening sequence of Tetrahymena. Cell 1982, 31:147-157.
    • (1982) Cell , vol.31 , pp. 147-157
    • Kruger, K.1    Grabowski, P.J.2    Zaug, A.J.3
  • 126
    • 84869049993 scopus 로고    scopus 로고
    • An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome
    • Kulczyk A.W., Akabayov B., Lee S.J., et al. An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome. Journal of Biological Chemistry 2012, 287:39050-39060.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 39050-39060
    • Kulczyk, A.W.1    Akabayov, B.2    Lee, S.J.3
  • 127
    • 33749354956 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modes
    • Kumaran S., Kozlov A.G., Lohman T.M. Saccharomyces cerevisiae replication protein A binds to single-stranded DNA in multiple salt-dependent modes. Biochemistry 2006, 45:11958-11973.
    • (2006) Biochemistry , vol.45 , pp. 11958-11973
    • Kumaran, S.1    Kozlov, A.G.2    Lohman, T.M.3
  • 128
    • 80053562457 scopus 로고    scopus 로고
    • Balancing eukaryotic replication asymmetry with replication fidelity
    • Kunkel T.A. Balancing eukaryotic replication asymmetry with replication fidelity. Current Opinion in Chemical Biology 2011, 15:620-626.
    • (2011) Current Opinion in Chemical Biology , vol.15 , pp. 620-626
    • Kunkel, T.A.1
  • 129
    • 54249092768 scopus 로고    scopus 로고
    • Dividing the workload at a eukaryotic replication fork
    • Kunkel T.A., Burgers P.M. Dividing the workload at a eukaryotic replication fork. Trends in Cell Biology 2008, 18:521-527.
    • (2008) Trends in Cell Biology , vol.18 , pp. 521-527
    • Kunkel, T.A.1    Burgers, P.M.2
  • 130
    • 84875900370 scopus 로고    scopus 로고
    • A solution to release twisted DNA during chromosome replication by coupled DNA polymerases
    • Kurth I., Georgescu R.E., O'Donnell M.E. A solution to release twisted DNA during chromosome replication by coupled DNA polymerases. Nature 2013, 496:119-122.
    • (2013) Nature , vol.496 , pp. 119-122
    • Kurth, I.1    Georgescu, R.E.2    O'Donnell, M.E.3
  • 131
    • 0032529167 scopus 로고    scopus 로고
    • DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair
    • de Laat W.L., Appeldoorn E., Sugasawa K., et al. DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair. Genes & Development 1998, 12:2598-2609.
    • (1998) Genes & Development , vol.12 , pp. 2598-2609
    • de Laat, W.L.1    Appeldoorn, E.2    Sugasawa, K.3
  • 133
    • 33748146483 scopus 로고    scopus 로고
    • Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III
    • Lamers M.H., Georgescu R.E., Lee S.G., O'Donnell M., Kuriyan J. Crystal structure of the catalytic alpha subunit of E. coli replicative DNA polymerase III. Cell 2006, 126:881-892.
    • (2006) Cell , vol.126 , pp. 881-892
    • Lamers, M.H.1    Georgescu, R.E.2    Lee, S.G.3    O'Donnell, M.4    Kuriyan, J.5
  • 135
    • 69749124647 scopus 로고    scopus 로고
    • Whither the replisome: Emerging perspectives on the dynamic nature of the DNA replication machinery
    • Langston L.D., Indiani C., O'Donnell M. Whither the replisome: Emerging perspectives on the dynamic nature of the DNA replication machinery. Cell Cycle 2009, 8:2686-2691.
    • (2009) Cell Cycle , vol.8 , pp. 2686-2691
    • Langston, L.D.1    Indiani, C.2    O'Donnell, M.3
  • 136
    • 57649139149 scopus 로고    scopus 로고
    • DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA
    • Langston L.D., O'Donnell M. DNA polymerase delta is highly processive with proliferating cell nuclear antigen and undergoes collision release upon completing DNA. Journal of Biological Chemistry 2008, 283:29522-29531.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 29522-29531
    • Langston, L.D.1    O'Donnell, M.2
  • 137
    • 9244224132 scopus 로고    scopus 로고
    • The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities
    • Lao-Sirieix S.H., Bell S.D. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase and 3'-terminal nucleotidyl transferase activities. Journal of Molecular Biology 2004, 344:1251-1263.
    • (2004) Journal of Molecular Biology , vol.344 , pp. 1251-1263
    • Lao-Sirieix, S.H.1    Bell, S.D.2
  • 138
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz J.H., McMacken R. The Escherichia coli dnaB replication protein is a DNA helicase. Journal of Biological Chemistry 1986, 261:4738-4748.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 140
    • 0001187127 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli
    • Lehman I.R., Bessman M.J., Simms E.S., Kornberg A. Enzymatic synthesis of deoxyribonucleic acid. I. Preparation of substrates and partial purification of an enzyme from Escherichia coli. Journal of Biological Chemistry 1958, 233:163-170.
    • (1958) Journal of Biological Chemistry , vol.233 , pp. 163-170
    • Lehman, I.R.1    Bessman, M.J.2    Simms, E.S.3    Kornberg, A.4
  • 143
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • Li Y., Korolev S., Waksman G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation. EMBO Journal 1998, 17:7514-7525.
    • (1998) EMBO Journal , vol.17 , pp. 7514-7525
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 144
    • 84856072129 scopus 로고    scopus 로고
    • Polymerase exchange during Okazaki fragment synthesis observed in living cells
    • Lia G., Michel B., Allemand J.F. Polymerase exchange during Okazaki fragment synthesis observed in living cells. Science 2012, 335:328-331.
    • (2012) Science , vol.335 , pp. 328-331
    • Lia, G.1    Michel, B.2    Allemand, J.F.3
  • 145
    • 84872497264 scopus 로고    scopus 로고
    • Exonuclease 1 preferentially repairs mismatches generated by DNA polymerase alpha
    • Liberti S.E., Larrea A.A., Kunkel T.A. Exonuclease 1 preferentially repairs mismatches generated by DNA polymerase alpha. DNA Repair (Amst) 2013, 12:92-96.
    • (2013) DNA Repair (Amst) , vol.12 , pp. 92-96
    • Liberti, S.E.1    Larrea, A.A.2    Kunkel, T.A.3
  • 146
    • 0035976978 scopus 로고    scopus 로고
    • The archaeal DNA primase: Biochemical characterization of the p41-p46 complex from Pyrococcus furiosus
    • Liu L., Komori K., Ishino S., et al. The archaeal DNA primase: Biochemical characterization of the p41-p46 complex from Pyrococcus furiosus. Journal of Biological Chemistry 2001, 276:45484-45490.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 45484-45490
    • Liu, L.1    Komori, K.2    Ishino, S.3
  • 149
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • Maga G., Hubscher U. Proliferating cell nuclear antigen (PCNA): A dancer with many partners. Journal of Cell Science 2003, 116:3051-3060.
    • (2003) Journal of Cell Science , vol.116 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 152
    • 84856768293 scopus 로고    scopus 로고
    • The CMG (CDC45/RecJ, MCM, GINS) complex is a conserved component of the DNA replication system in all archaea and eukaryotes
    • Makarova K.S., Koonin E.V., Kelman Z. The CMG (CDC45/RecJ, MCM, GINS) complex is a conserved component of the DNA replication system in all archaea and eukaryotes. Biology Direct 2012, 7:7.
    • (2012) Biology Direct , vol.7 , pp. 7
    • Makarova, K.S.1    Koonin, E.V.2    Kelman, Z.3
  • 154
    • 0037295722 scopus 로고    scopus 로고
    • Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin
    • Matsunaga F., Norais C., Forterre P., Myllykallio H. Identification of short 'eukaryotic' Okazaki fragments synthesized from a prokaryotic replication origin. EMBO Reports 2003, 4:154-158.
    • (2003) EMBO Reports , vol.4 , pp. 154-158
    • Matsunaga, F.1    Norais, C.2    Forterre, P.3    Myllykallio, H.4
  • 155
    • 80053560927 scopus 로고    scopus 로고
    • Bacterial replicases and related polymerases
    • McHenry C.S. Bacterial replicases and related polymerases. Current Opinion in Chemical Biology 2011, 15:587-594.
    • (2011) Current Opinion in Chemical Biology , vol.15 , pp. 587-594
    • McHenry, C.S.1
  • 156
  • 157
    • 0026502128 scopus 로고
    • Protein affinity chromatography with purified yeast DNA polymerase alpha detects proteins that bind to DNA polymerase
    • Miles J., Formosa T. Protein affinity chromatography with purified yeast DNA polymerase alpha detects proteins that bind to DNA polymerase. Proceedings of the National Academy of Sciences of the United States of America 1992, 89:1276-1280.
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , pp. 1276-1280
    • Miles, J.1    Formosa, T.2
  • 162
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin A.G. OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences. EMBO Journal 1993, 12:861-867.
    • (1993) EMBO Journal , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 163
    • 83655212423 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes
    • Netz D.J., Stith C.M., Stumpfig M., et al. Eukaryotic DNA polymerases require an iron-sulfur cluster for the formation of active complexes. Nature Chemical Biology 2011, 8:125-132.
    • (2011) Nature Chemical Biology , vol.8 , pp. 125-132
    • Netz, D.J.1    Stith, C.M.2    Stumpfig, M.3
  • 164
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., Aravind L., Spouge J.L., Koonin E.V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Research 1999, 9:27-43.
    • (1999) Genome Research , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 166
    • 0035856473 scopus 로고    scopus 로고
    • Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC
    • O'Donnell M., Jeruzalmi D., Kuriyan J. Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC. Current Biology 2001, 11:R935-R946.
    • (2001) Current Biology , vol.11 , pp. R935-R946
    • O'Donnell, M.1    Jeruzalmi, D.2    Kuriyan, J.3
  • 169
    • 0023646086 scopus 로고
    • Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli
    • O'Donnell M.E. Accessory proteins bind a primed template and mediate rapid cycling of DNA polymerase III holoenzyme from Escherichia coli. Journal of Biological Chemistry 1987, 262:16558-16565.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 16558-16565
    • O'Donnell, M.E.1
  • 171
    • 82355188414 scopus 로고    scopus 로고
    • Thermococcus kodakarensis encodes three MCM homologs but only one is essential
    • Pan M., Santangelo T.J., Li Z., Reeve J.N., Kelman Z. Thermococcus kodakarensis encodes three MCM homologs but only one is essential. Nucleic Acids Research 2011, 39:9671-9680.
    • (2011) Nucleic Acids Research , vol.39 , pp. 9671-9680
    • Pan, M.1    Santangelo, T.J.2    Li, Z.3    Reeve, J.N.4    Kelman, Z.5
  • 172
    • 0032570821 scopus 로고    scopus 로고
    • Formation of a DNA loop at the replication fork generated by bacteriophage T7 replication proteins
    • Park K., Debyser Z., Tabor S., Richardson C.C., Griffith J.D. Formation of a DNA loop at the replication fork generated by bacteriophage T7 replication proteins. Journal of Biological Chemistry 1998, 273:5260-5270.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 5260-5270
    • Park, K.1    Debyser, Z.2    Tabor, S.3    Richardson, C.C.4    Griffith, J.D.5
  • 173
    • 82755183582 scopus 로고    scopus 로고
    • The Escherichia coli clamp loader can actively pry open the beta-sliding clamp
    • Paschall C.O., Thompson J.A., Marzahn M.R., et al. The Escherichia coli clamp loader can actively pry open the beta-sliding clamp. Journal of Biological Chemistry 2011, 286:42704-42714.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 42704-42714
    • Paschall, C.O.1    Thompson, J.A.2    Marzahn, M.R.3
  • 174
    • 84881519871 scopus 로고    scopus 로고
    • Mechanism for Priming DNA Synthesis by Yeast DNA Polymerase alpha
    • Perera R.L., Torella R., Klinge S., et al. Mechanism for Priming DNA Synthesis by Yeast DNA Polymerase alpha. Elife 2 2013, e00482.
    • (2013) Elife 2
    • Perera, R.L.1    Torella, R.2    Klinge, S.3
  • 175
    • 0034616957 scopus 로고    scopus 로고
    • A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases
    • Podobnik M., McInerney P., O'Donnell M., Kuriyan J. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. Journal of Molecular Biology 2000, 300:353-362.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 353-362
    • Podobnik, M.1    McInerney, P.2    O'Donnell, M.3    Kuriyan, J.4
  • 176
    • 34447336941 scopus 로고    scopus 로고
    • Yeast DNA polymerase epsilon participates in leading-strand DNA replication
    • Pursell Z.F., Isoz I., Lundstrom E.B., Johansson E., Kunkel T.A. Yeast DNA polymerase epsilon participates in leading-strand DNA replication. Science 2007, 317:127-130.
    • (2007) Science , vol.317 , pp. 127-130
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.B.3    Johansson, E.4    Kunkel, T.A.5
  • 179
  • 180
    • 77951537332 scopus 로고    scopus 로고
    • Stoichiometry and architecture of active DNA replication machinery in Escherichia coli
    • Reyes-Lamothe R., Sherratt D.J., Leake M.C. Stoichiometry and architecture of active DNA replication machinery in Escherichia coli. Science 2010, 328:498-501.
    • (2010) Science , vol.328 , pp. 498-501
    • Reyes-Lamothe, R.1    Sherratt, D.J.2    Leake, M.C.3
  • 181
    • 0018101448 scopus 로고
    • Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains
    • Rowen L., Kornberg A. Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains. Journal of Biological Chemistry 1978, 253:758-764.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 758-764
    • Rowen, L.1    Kornberg, A.2
  • 182
    • 34248664689 scopus 로고    scopus 로고
    • Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein
    • Roy R., Kozlov A.G., Lohman T.M., Ha T. Dynamic structural rearrangements between DNA binding modes of E. coli SSB protein. Journal of Molecular Biology 2007, 369:1244-1257.
    • (2007) Journal of Molecular Biology , vol.369 , pp. 1244-1257
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 183
    • 84888156088 scopus 로고    scopus 로고
    • PPL2 translesion polymerase is essential for the completion of chromosomal DNA replication in the African trypanosome
    • Rudd S.G., Glover L., Jozwiakowski S.K., Horn D., Doherty A.J. PPL2 translesion polymerase is essential for the completion of chromosomal DNA replication in the African trypanosome. Molecular Cell 2013, 52:554-565.
    • (2013) Molecular Cell , vol.52 , pp. 554-565
    • Rudd, S.G.1    Glover, L.2    Jozwiakowski, S.K.3    Horn, D.4    Doherty, A.J.5
  • 184
    • 64149093563 scopus 로고    scopus 로고
    • Unwinding the structure and function of the archaeal MCM helicase
    • Sakakibara N., Kelman L.M., Kelman Z. Unwinding the structure and function of the archaeal MCM helicase. Molecular Microbiology 2009, 72:286-296.
    • (2009) Molecular Microbiology , vol.72 , pp. 286-296
    • Sakakibara, N.1    Kelman, L.M.2    Kelman, Z.3
  • 185
    • 3543069892 scopus 로고    scopus 로고
    • The C-terminal zinc finger of the catalytic subunit of DNA polymerase delta is responsible for direct interaction with the B-subunit
    • Sanchez Garcia J., Ciufo L.F., Yang X., Kearsey S.E., MacNeill S.A. The C-terminal zinc finger of the catalytic subunit of DNA polymerase delta is responsible for direct interaction with the B-subunit. Nucleic Acids Research 2004, 32:3005-3016.
    • (2004) Nucleic Acids Research , vol.32 , pp. 3005-3016
    • Sanchez Garcia, J.1    Ciufo, L.F.2    Yang, X.3    Kearsey, S.E.4    MacNeill, S.A.5
  • 187
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya M.R., Guo S., Tabor S., Richardson C.C., Ellenberger T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell 1999, 99:167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 188
    • 46249122812 scopus 로고    scopus 로고
    • Separate roles for the DNA damage checkpoint protein kinases in stabilizing DNA replication forks
    • Segurado M., Diffley J.F. Separate roles for the DNA damage checkpoint protein kinases in stabilizing DNA replication forks. Genes & Development 2008, 22:1816-1827.
    • (2008) Genes & Development , vol.22 , pp. 1816-1827
    • Segurado, M.1    Diffley, J.F.2
  • 189
    • 77949368063 scopus 로고    scopus 로고
    • GINS motion reveals replication fork progression is remarkably uniform throughout the yeast genome
    • Sekedat M.D., Fenyo D., Rogers R.S., et al. GINS motion reveals replication fork progression is remarkably uniform throughout the yeast genome. Molecular Systems Biology 2010, 6:353.
    • (2010) Molecular Systems Biology , vol.6 , pp. 353
    • Sekedat, M.D.1    Fenyo, D.2    Rogers, R.S.3
  • 190
    • 84876108565 scopus 로고    scopus 로고
    • Dpb2 integrates the leading-strand DNA polymerase into the eukaryotic replisome
    • Sengupta S., van Deursen F., de Piccoli G., Labib K. Dpb2 integrates the leading-strand DNA polymerase into the eukaryotic replisome. Current Biology 2013, 23:543-552.
    • (2013) Current Biology , vol.23 , pp. 543-552
    • Sengupta, S.1    van Deursen, F.2    de Piccoli, G.3    Labib, K.4
  • 191
    • 0037109208 scopus 로고    scopus 로고
    • Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus
    • Seybert A., Scott D.J., Scaife S., Singleton M.R., Wigley D.B. Biochemical characterisation of the clamp/clamp loader proteins from the euryarchaeon Archaeoglobus fulgidus. Nucleic Acids Research 2002, 30:4329-4338.
    • (2002) Nucleic Acids Research , vol.30 , pp. 4329-4338
    • Seybert, A.1    Scott, D.J.2    Scaife, S.3    Singleton, M.R.4    Wigley, D.B.5
  • 193
    • 73849129578 scopus 로고    scopus 로고
    • The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory activity in Mcm4
    • Sheu Y.J., Stillman B. The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory activity in Mcm4. Nature 2010, 463:113-117.
    • (2010) Nature , vol.463 , pp. 113-117
    • Sheu, Y.J.1    Stillman, B.2
  • 195
    • 84902304914 scopus 로고    scopus 로고
    • A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome
    • Simon A.C., Zhou J.C., Perera R.L., et al. A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome. Nature 2014, 510:293-297.
    • (2014) Nature , vol.510 , pp. 293-297
    • Simon, A.C.1    Zhou, J.C.2    Perera, R.L.3
  • 196
    • 65549110769 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent primer-template recognition by a clamp loader complex
    • Simonetta K.R., Kazmirski S.L., Goedken E.R., et al. The mechanism of ATP-dependent primer-template recognition by a clamp loader complex. Cell 2009, 137:659-671.
    • (2009) Cell , vol.137 , pp. 659-671
    • Simonetta, K.R.1    Kazmirski, S.L.2    Goedken, E.R.3
  • 198
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 2000, 101:589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 199
    • 0019223518 scopus 로고
    • Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system
    • Sinha N.K., Morris C.F., Alberts B.M. Efficient in vitro replication of double-stranded DNA templates by a purified T4 bacteriophage replication system. Journal of Biological Chemistry 1980, 255:4290-4293.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 4290-4293
    • Sinha, N.K.1    Morris, C.F.2    Alberts, B.M.3
  • 200
    • 84870829991 scopus 로고    scopus 로고
    • A wolf in sheep's clothing: SV40 co-opts host genome maintenance proteins to replicate viral DNA
    • Sowd G.A., Fanning E. A wolf in sheep's clothing: SV40 co-opts host genome maintenance proteins to replicate viral DNA. PLoS Pathogens 2012, 8:e1002994.
    • (2012) PLoS Pathogens , vol.8
    • Sowd, G.A.1    Fanning, E.2
  • 201
    • 33745087407 scopus 로고    scopus 로고
    • A coproofreading Zn(2+)-dependent exonuclease within a bacterial replicase
    • Stano N.M., Chen J., McHenry C.S. A coproofreading Zn(2+)-dependent exonuclease within a bacterial replicase. Nature Structural & Molecular Biology 2006, 13:458-459.
    • (2006) Nature Structural & Molecular Biology , vol.13 , pp. 458-459
    • Stano, N.M.1    Chen, J.2    McHenry, C.S.3
  • 202
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz T.A. DNA polymerases: Structural diversity and common mechanisms. Journal of Biological Chemistry 1999, 274:17395-17398.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 203
    • 33747621427 scopus 로고    scopus 로고
    • Visualizing polynucleotide polymerase machines at work
    • Steitz T.A. Visualizing polynucleotide polymerase machines at work. EMBO Journal 2006, 25:3458-3468.
    • (2006) EMBO Journal , vol.25 , pp. 3458-3468
    • Steitz, T.A.1
  • 204
    • 42949142111 scopus 로고    scopus 로고
    • DNA polymerases at the replication fork in eukaryotes
    • Stillman B. DNA polymerases at the replication fork in eukaryotes. Molecular Cell 2008, 30:259-260.
    • (2008) Molecular Cell , vol.30 , pp. 259-260
    • Stillman, B.1
  • 205
    • 57749100294 scopus 로고    scopus 로고
    • Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis
    • Stith C.M., Sterling J., Resnick M.A., Gordenin D.A., Burgers P.M. Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis. Journal of Biological Chemistry 2008, 283:34129-34140.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 34129-34140
    • Stith, C.M.1    Sterling, J.2    Resnick, M.A.3    Gordenin, D.A.4    Burgers, P.M.5
  • 208
    • 0028093437 scopus 로고
    • An explanation for lagging strand replication: Polymerase hopping among DNA sliding clamps
    • Stukenberg P.T., Turner J., O'Donnell M. An explanation for lagging strand replication: Polymerase hopping among DNA sliding clamps. Cell 1994, 78:877-887.
    • (1994) Cell , vol.78 , pp. 877-887
    • Stukenberg, P.T.1    Turner, J.2    O'Donnell, M.3
  • 209
    • 0345276497 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional primase-helicase of bacteriophage T7
    • Toth E.A., Li Y., Sawaya M.R., Cheng Y., Ellenberger T. The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Molecular Cell 2003, 12:1113-1123.
    • (2003) Molecular Cell , vol.12 , pp. 1113-1123
    • Toth, E.A.1    Li, Y.2    Sawaya, M.R.3    Cheng, Y.4    Ellenberger, T.5
  • 210
    • 0025967720 scopus 로고
    • Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis
    • Tsurimoto T., Stillman B. Replication factors required for SV40 DNA replication in vitro. II. Switching of DNA polymerase alpha and delta during initiation of leading and lagging strand synthesis. Journal of Biological Chemistry 1991, 266:1961-1968.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 1961-1968
    • Tsurimoto, T.1    Stillman, B.2
  • 211
    • 0033081486 scopus 로고    scopus 로고
    • The internal workings of a DNA polymerase clamp-loading machine
    • Turner J., Hingorani M.M., Kelman Z., O'Donnell M. The internal workings of a DNA polymerase clamp-loading machine. EMBO Journal 1999, 18:771-783.
    • (1999) EMBO Journal , vol.18 , pp. 771-783
    • Turner, J.1    Hingorani, M.M.2    Kelman, Z.3    O'Donnell, M.4
  • 212
    • 84889093850 scopus 로고    scopus 로고
    • HPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity
    • Wan L., Lou J., Xia Y., et al. hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the maintenance of genome integrity. EMBO Reports 2013, 14:1104-1112.
    • (2013) EMBO Reports , vol.14 , pp. 1104-1112
    • Wan, L.1    Lou, J.2    Xia, Y.3
  • 213
    • 37849024100 scopus 로고    scopus 로고
    • The structure of a DnaB-family replicative helicase and its interactions with primase
    • Wang G., Klein M.G., Tokonzaba E., et al. The structure of a DnaB-family replicative helicase and its interactions with primase. Nature Structural & Molecular Biology 2008, 15:94-100.
    • (2008) Nature Structural & Molecular Biology , vol.15 , pp. 94-100
    • Wang, G.1    Klein, M.G.2    Tokonzaba, E.3
  • 215
    • 33749048664 scopus 로고
    • Genetical implications of the structure of deoxyribonucleic acid
    • Watson J.D., Crick F.H. Genetical implications of the structure of deoxyribonucleic acid. Nature 1953, 171:964-967.
    • (1953) Nature , vol.171 , pp. 964-967
    • Watson, J.D.1    Crick, F.H.2
  • 216
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid
    • Watson J.D., Crick F.H. Molecular structure of nucleic acids; a structure for deoxyribose nucleic acid. Nature 1953, 171:737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.2
  • 217
    • 36348995555 scopus 로고    scopus 로고
    • An iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase
    • Weiner B.E., Huang H., Dattilo B.M., et al. An iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase. Journal of Biological Chemistry 2007, 282:33444-33451.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 33444-33451
    • Weiner, B.E.1    Huang, H.2    Dattilo, B.M.3
  • 218
    • 51249093024 scopus 로고    scopus 로고
    • Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit
    • Wing R.A., Bailey S., Steitz T.A. Insights into the replisome from the structure of a ternary complex of the DNA polymerase III alpha-subunit. Journal of Molecular Biology 2008, 382:859-869.
    • (2008) Journal of Molecular Biology , vol.382 , pp. 859-869
    • Wing, R.A.1    Bailey, S.2    Steitz, T.A.3
  • 219
    • 0003984178 scopus 로고
    • Joanna Cotler Books, New York, NY
    • Woese C.R. Genetic Code 1968, Joanna Cotler Books, New York, NY. New Edition Edit.
    • (1968) Genetic Code
    • Woese, C.R.1
  • 220
    • 0030908093 scopus 로고    scopus 로고
    • Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism
    • Wold M.S. Replication protein A: A heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism. Annual Review of Biochemistry 1997, 66:61-92.
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 61-92
    • Wold, M.S.1
  • 221
    • 0036668464 scopus 로고    scopus 로고
    • Mapping of early firing origins on a replication profile of budding yeast
    • Yabuki N., Terashima H., Kitada K. Mapping of early firing origins on a replication profile of budding yeast. Genes to Cells 2002, 7:781-789.
    • (2002) Genes to Cells , vol.7 , pp. 781-789
    • Yabuki, N.1    Terashima, H.2    Kitada, K.3
  • 222
    • 30744446944 scopus 로고    scopus 로고
    • The control mechanism for lagging strand polymerase recycling during bacteriophage T4 DNA replication
    • Yang J., Nelson S.W., Benkovic S.J. The control mechanism for lagging strand polymerase recycling during bacteriophage T4 DNA replication. Molecular Cell 2006, 21:153-164.
    • (2006) Molecular Cell , vol.21 , pp. 153-164
    • Yang, J.1    Nelson, S.W.2    Benkovic, S.J.3
  • 224
    • 84899827339 scopus 로고    scopus 로고
    • An overview of Y-family DNA polymerases and a case study of human DNA polymerase eta
    • Yang W. An overview of Y-family DNA polymerases and a case study of human DNA polymerase eta. Biochemistry 2014, 53:2793-2803.
    • (2014) Biochemistry , vol.53 , pp. 2793-2803
    • Yang, W.1
  • 227
    • 66049138588 scopus 로고    scopus 로고
    • Replisome structure and conformational dynamics underlie fork progression past obstacles
    • Yao N.Y., O'Donnell M. Replisome structure and conformational dynamics underlie fork progression past obstacles. Current Opinion in Cell Biology 2009, 21:336-343.
    • (2009) Current Opinion in Cell Biology , vol.21 , pp. 336-343
    • Yao, N.Y.1    O'Donnell, M.2
  • 228
    • 0037117724 scopus 로고    scopus 로고
    • The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting
    • Zerbe L.K., Kuchta R.D. The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting. Biochemistry 2002, 41:4891-4900.
    • (2002) Biochemistry , vol.41 , pp. 4891-4900
    • Zerbe, L.K.1    Kuchta, R.D.2
  • 229
    • 12844250647 scopus 로고    scopus 로고
    • A primer-dependent polymerase function of pseudomonas aeruginosa ATP-dependent DNA ligase (LigD)
    • Zhu H., Shuman S. A primer-dependent polymerase function of pseudomonas aeruginosa ATP-dependent DNA ligase (LigD). Journal of Biological Chemistry 2005, 280:418-427.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 418-427
    • Zhu, H.1    Shuman, S.2
  • 230
    • 44449138846 scopus 로고    scopus 로고
    • Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme
    • Zhuang Z., Johnson R.E., Haracska L., et al. Regulation of polymerase exchange between Poleta and Poldelta by monoubiquitination of PCNA and the movement of DNA polymerase holoenzyme. Proceedings of the National Academy of Sciences of the United States of America 2008, 105:5361-5366.
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , pp. 5361-5366
    • Zhuang, Z.1    Johnson, R.E.2    Haracska, L.3
  • 232
    • 0029944855 scopus 로고    scopus 로고
    • DNA polymerase epsilon may be dispensable for SV40-but not cellular-DNA replication
    • Zlotkin T., Kaufmann G., Jiang Y., et al. DNA polymerase epsilon may be dispensable for SV40-but not cellular-DNA replication. EMBO Journal 1996, 15:2298-2305.
    • (1996) EMBO Journal , vol.15 , pp. 2298-2305
    • Zlotkin, T.1    Kaufmann, G.2    Jiang, Y.3


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