Abstract
Chromosomal DNA must be replicated faithfully and propagated to daughter cells equally. The mechanism of DNA replication is constrained by the characteristics of DNA polymerases, which synthesize chromosomal DNA; i.e., double-stranded DNA must be unwound to serve as a template and 3′-OH (RNA primer in cellular organisms) must be provided to DNA polymerases. Once these two conditions are fulfilled, DNA polymerase can start DNA synthesis everywhere. However, cells regulate this process strictly, mainly at replication origins. DNA replication initiates from replication origins, to which the initiator protein binds. DNA helicase is loaded onto origins and unwinds double-stranded DNA for the syntheses of an RNA primer and subsequent DNA by primase and DNA polymerases. As DNA polymerases elongate the DNA chain in the 5′ to 3′ direction, both strands are synthesized in opposite directions from the initiation site. The synthesis of both DNA strands (leading and lagging) continues in a manner that is coupled with DNA helicase up to its termination. These fundamental mechanisms and regulation of cellular chromosomal DNA replication are outlined using prokaryotic and eukaryotic examples.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Anand RP, Lovett ST, Haber JE (2013) Break-induced DNA replication. Cold Spring Harb Perspect Biol 5(12):a010397–a010397. doi:10.1101/cshperspect.a010397
Araki H (2010) Cyclin-dependent kinase-dependent initiation of chromosomal DNA replication. Curr Opin Cell Biol 22(6):766–771. doi:10.1016/j.ceb.2010.07.015
Arias-Palomo E, O’Shea VL, Hood IV, Berger JM (2013) The bacterial DnaC helicase loader is a DnaB ring breaker. Cell:1–11. doi:10.1016/j.cell.2013.03.006
Balakrishnan L, Bambara RA (2013) Okazaki fragment metabolism. Cold Spring Harb Perspect Biol 5(2). doi:10.1101/cshperspect.a010173
Baxter J, Diffley JF (2008) Topoisomerase II inactivation prevents the completion of DNA replication in budding yeast. Mol Cell 30(6):790–802. doi:10.1016/j.molcel.2008.04.019
Bell SD, Botchan MR (2013) The minichromosome maintenance replicative helicase. Cold Spring Harb Perspect Biol 5(11):a012807. doi:10.1101/cshperspect.a012807
Bell SP, Kaguni JM (2013) Helicase loading at chromosomal origins of replication. Cold Spring Harb Perspect Biology 5(6). doi:10.1101/cshperspect.a010124
Boos D, Sanchez-Pulido L, Rappas M, Pearl LH, Oliver AW, Ponting CP, Diffley JF (2011) Regulation of DNA replication through Sld3-Dpb11 interaction is conserved from yeast to humans. Curr Biol 21(13):1152–1157. doi:10.1016/j.cub.2011.05.057
Boos D, Yekezare M, Diffley JFX (2013) Identification of a heteromeric complex that promotes DNA replication origin firing in human cells. Science 340(6135):981–984. doi:10.1126/science.1237448
Chodavarapu S, Felczak MM, Yaniv JR, Kaguni JM (2008) Escherichia coli DnaA interacts with HU in initiation at the E. coli replication origin. Mol Microbiol 67(4):781–792. doi:10.1111/j.1365-2958.2007.06094.x
Clarey MG, Erzberger JP, Grob P, Leschziner AE, Berger JM, Nogales E, Botchan M (2006) Nucleotide-dependent conformational changes in the DnaA-like core of the origin recognition complex. Nat Struct Mol Biol 13(8):684–690. doi:10.1038/nsmb1121
Corn JE, Berger JM (2006) Regulation of bacterial priming and daughter strand synthesis through helicase-primase interactions. Nucleic Acids Res 34(15):4082–4088. doi:10.1093/nar/gkl363
Costa A, Ilves I, Tamberg N, Petojevic T, Nogales E, Botchan MR, Berger JM (2011) The structural basis for MCM2-7 helicase activation by GINS and Cdc45. Nat Struct Mol Biol 18(4):471–477. doi:10.1038/nsmb.2004
Costa A, Hood IV, Berger JM (2013) Mechanisms for initiating cellular DNA replication. Annu Rev Biochem 82:25–54. doi:10.1146/annurev-biochem-052610-094414
Costantino L, Sotiriou SK, Rantala JK, Magin S, Mladenov E, Helleday T, Haber JE, Iliakis G, Kallioniemi OP, Halazonetis TD (2014) Break-induced replication repair of damaged forks induces genomic duplications in human cells. Science 343(6166):88–91. doi:10.1126/science.1243211
Dervyn E, Suski C, Daniel R, Bruand C, Chapuis J, Errington J, Janniere L, Ehrlich SD (2001) Two essential DNA polymerases at the bacterial replication fork. Science 294(5547):1716–1719. doi:10.1126/science.1066351
Duggin IG, Wake RG, Bell SD, Hill TM (2008) The replication fork trap and termination of chromosome replication. Mol Microbiol 70(6):1323–1333. doi:10.1111/j.1365-2958.2008.06500.x
Fernández-Cid A, Riera A, Tognetti S, Herrera MC, Samel S, Evrin C, Winkler C, Gardenal E, Uhle S, Speck C (2013) An ORC/Cdc6/MCM2-7 complex is formed in a multistep reaction to serve as a platform for MCM double-hexamer assembly. Mol Cell:1–12. doi:10.1016/j.molcel.2013.03.026
Foltman M, Evrin C, de Piccoli G, Jones RC, Edmondson RD, Katou Y, Nakato R, Shirahige K, Labib K (2013) Eukaryotic replisome components cooperate to process histones during chromosome replication. Cell Rep 3(3):892–904. doi:10.1016/j.celrep.2013.02.028
Frigola J, Remus D, Mehanna A, Diffley JFX (2013) ATPase-dependent quality control of DNA replication origin licensing. Nature 495(7441):339–343. doi:10.1038/nature11920
Fukushima S, Itaya M, Kato H, Ogasawara N, Yoshikawa H (2007) Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth. J Bacteriol 189(23):8575–8583. doi:10.1128/JB.00653-07
Gabbai CB, Marians KJ (2010) Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival. DNA Repair 9(3):202–209. doi:10.1016/j.dnarep.2009.12.009
Gaggioli V, Zeiser E, Rivers D, Bradshaw CR, Ahringer J, Zegerman P (2014) CDK phosphorylation of SLD-2 is required for replication initiation and germline development in C. elegans. J Cell Biol 204(4):507–522. doi:10.1083/jcb.201310083
Gambus A, Jones RC, Sanchez-Diaz A, Kanemaki M, van Deursen F, Edmondson RD, Labib K (2006) GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks. Nat Cell Biol 8(4):358–366. doi:10.1038/ncb1382
Gambus A, van Deursen F, Polychronopoulos D, Foltman M, Jones RC, Edmondson RD, Calzada A, Labib K (2009) A key role for Ctf4 in coupling the MCM2-7 helicase to DNA polymerase alpha within the eukaryotic replisome. EMBO J 28(19):2992–3004. doi:10.1038/emboj.2009.226
Georgescu RE, Langston L, Yao NY, Yurieva O, Zhang D, Finkelstein J, Agarwal T, O’Donnell ME (2014) Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork. Nat Struct Mol Biol:1–9. doi:10.1038/nsmb.2851
Handa T, Kanke M, Takahashi TS, Nakagawa T, Masukata H (2012) DNA polymerization-independent functions of DNA polymerase epsilon in assembly and progression of the replisome in fission yeast. Mol Biol Cell 23(16):3240–3253. doi:10.1091/mbc.E12-05-0339
Hashimoto Y, Takisawa H (2003) Xenopus Cut5 is essential for a CDK-dependent process in the initiation of DNA replication. EMBO J 22(10):2526–2535
Hawkins M, Malla S, Blythe MJ, Nieduszynski CA, Allers T (2013) Accelerated growth in the absence of DNA replication origins. Nature 503(7477):544–547. doi:10.1038/nature12650
Hedglin M, Kumar R, Benkovic SJ (2013) Replication clamps and clamp loaders. Cold Spring Harb Perspect Biol 5(4):a010165. doi:10.1101/cshperspect.a010165
Heller RC, Kang S, Lam WM, Chen S, Chan CS, Bell SP (2011) Eukaryotic origin-dependent DNA replication in vitro reveals sequential action of DDK and S-CDK kinases. Cell 146(1):80–91. doi:10.1016/j.cell.2011.06.012
Hizume K, Yagura M, Araki H (2013) Concerted interaction between origin recognition complex (ORC), nucleosomes and replication origin DNA ensures stable ORC-origin binding. Genes Cells 18(9):764–779. doi:10.1111/gtc.12073
Hogg M, Osterman P, Bylund GO, Ganai RA, Lundstrom EB, Sauer-Eriksson AE, Johansson E (2014) Structural basis for processive DNA synthesis by yeast DNA polymerase epsilon. Nat Struct Mol Biol 21(1):49–55. doi:10.1038/nsmb.2712
Huo YG, Bai L, Xu M, Jiang T (2010) Crystal structure of the N-terminal region of human Topoisomerase II beta binding protein 1. Biochem Biophys Res Commun 401(3):401–405. doi:10.1016/j.bbrc.2010.09.066
Ilves I, Petojevic T, Pesavento JJ, Botchan MR (2010) Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins. Mol Cell 37(2):247–258. doi:10.1016/j.molcel.2009.12.030
Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA (2012) The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 151(2):267–277. doi:10.1016/j.cell.2012.09.014
Johansson E, Dixon N (2013) Replicative DNA polymerases. Cold Spring Harb Perspect Biol 5(6). doi:10.1101/cshperspect.a012799
Kamimura Y, Tak YS, Sugino A, Araki H (2001) Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae. EMBO J 20(8):2097–2107. doi:10.1093/emboj/20.8.2097
Kanemaki M, Labib K (2006) Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks. EMBO J 25(8):1753–1763. doi:10.1038/sj.emboj.7601063
Kang Y-H, Galal WC, Farina A, Tappin I, Hurwitz J (2012) Properties of the human Cdc45/Mcm2-7/GINS helicase complex and its action with DNA polymerase epsilon in rolling circle DNA synthesis. Proc Natl Acad Sci U S A 109(16):6042–6047. doi:10.1073/pnas.1203734109
Kanke M, Kodama Y, Takahashi TS, Nakagawa T, Masukata H (2012) Mcm10 plays an essential role in origin DNA unwinding after loading of the CMG components. EMBO J 31(9):2182–2194. doi:10.1038/emboj.2012.68
Katayama T, Ozaki S, Keyamura K, Fujimitsu K (2010) Regulation of the replication cycle: conserved and diverse regulatory systems for DnaA and oriC. Nat Rev Microbiol 8(3):163–170. doi:10.1038/nrmicro2314
Katou Y, Kanoh Y, Bando M, Noguchi H, Tanaka H, Ashikari T, Sugimoto K, Shirahige K (2003) S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex. Nature 424(6952):1078–1083. doi:10.1038/nature01900
Kaur G, Vora MP, Czerwonka CA, Rozgaja TA, Grimwade JE, Leonard AC (2014) Building the bacterial orisome: high-affinity DnaA recognition plays a role in setting the conformation of oriC DNA. Mol Microbiol 91(6):1148–1163. doi:10.1111/mmi.12525
Kelch BA, Makino DL, O’Donnell M, Kuriyan J (2011) How a DNA polymerase clamp loader opens a sliding clamp. Science 334(6063):1675–1680. doi:10.1126/science.1211884
Kim S, Dallmann HG, McHenry CS, Marians KJ (1996) Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 84(4):643–650
Kogoma T (1997) Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription. Microbiol Mol Biol Rev 61(2):212–238
Kubota Y, Takase Y, Komori Y, Hashimoto Y, Arata T, Kamimura Y, Araki H, Takisawa H (2003) A novel ring-like complex of Xenopus proteins essential for the initiation of DNA replication. Genes Dev 17(9):1141–1152. doi:10.1101/gad.1070003
Kubota T, Nishimura K, Kanemaki MT, Donaldson AD (2013) The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication. Mol Cell 50(2):273–280. doi:10.1016/j.molcel.2013.02.012
Kumagai A, Shevchenko A, Dunphy WG (2010) Treslin collaborates with TopBP1 in triggering the initiation of DNA replication. Cell 140(3):349–359. doi:10.1016/j.cell.2009.12.049
Kumagai A, Shevchenko A, Dunphy WG (2011) Direct regulation of Treslin by cyclin-dependent kinase is essential for the onset of DNA replication. J Cell Biol 193(6):995–1007. doi:10.1083/jcb.201102003
LeBowitz JH, McMacken R (1986) The Escherichia coli dnaB replication protein is a DNA helicase. J Biol Chem 261(10):4738–4748
Leman AR, Noguchi E (2012) Local and global functions of Timeless and Tipin in replication fork protection. Cell Cycle 11(21):3945–3955. doi:10.4161/cc.21989
Li Y, Araki H (2013) Loading and activation of DNA replicative helicases: the key step of initiation of DNA replication. Genes Cells 18(4):266–277. doi:10.1111/gtc.12040
MacAlpine DM, Almouzni G (2013) Chromatin and DNA replication. Cold Spring Harb Perspect Biol 5(8):a010207. doi:10.1101/cshperspect.a010207
Makiniemi M, Hillukkala T, Tuusa J, Reini K, Vaara M, Huang D, Pospiech H, Majuri I, Westerling T, Makela TP, Syvaoja JE (2001) BRCT domain-containing protein TopBP1 functions in DNA replication and damage response. J Biol Chem 276(32):30399–30406
Makowska-Grzyska M, Kaguni JM (2010) Primase directs the release of DnaC from DnaB. Mol Cell 37(1):90–101. doi:10.1016/j.molcel.2009.12.031
Mantiero D, Mackenzie A, Donaldson A, Zegerman P (2011) Limiting replication initiation factors execute the temporal programme of origin firing in budding yeast. EMBO J 30(23):4805–4814. doi:10.1038/emboj.2011.404
Masai H, Matsumoto S, You Z, Yoshizawa-Sugata N, Oda M (2010) Eukaryotic chromosome DNA replication: where, when, and how? Annu Rev Biochem 79:89–130. doi:10.1146/annurev.biochem.052308.103205
Masumoto H, Muramatsu S, Kamimura Y, Araki H (2002) S-Cdk-dependent phosphorylation of Sld2 essential for chromosomal DNA replication in budding yeast. Nature 415(6872):651–655. doi:10.1038/nature713
Matsuno K, Kumano M, Kubota Y, Hashimoto Y, Takisawa H (2006) The N-terminal noncatalytic region of Xenopus RecQ4 is required for chromatin binding of DNA polymerase alpha in the initiation of DNA replication. Mol Cell Biol 26(13):4843–4852
McHenry CS (2011) DNA replicases from a bacterial perspective. Annu Rev Biochem 80:403–436. doi:10.1146/annurev-biochem-061208-091655
McInerney P, Johnson A, Katz F, O’Donnell M (2007) Characterization of a triple DNA polymerase replisome. Mol Cell 27(4):527–538. doi:10.1016/j.molcel.2007.06.019
Moyer SE, Lewis PW, Botchan MR (2006) Isolation of the Cdc45/Mcm2-7/GINS (CMG) complex, a candidate for the eukaryotic DNA replication fork helicase. Proc Natl Acad Sci U S A 103(27):10236–10241. doi:10.1073/pnas.0602400103
Murakami T, Takano R, Takeo S, Taniguchi R, Ogawa K, Ohashi E, Tsurimoto T (2010) Stable interaction between the human proliferating cell nuclear antigen loader complex Ctf18-replication factor C (RFC) and DNA polymerase ε is mediated by the cohesion-specific subunits, Ctf18, Dcc1, and Ctf8. J Biol Chem 285(45):34608–34615. doi:10.1074/jbc.M110.166710
Muramatsu S, Hirai K, Tak YS, Kamimura Y, Araki H (2010) CDK-dependent complex formation between replication proteins Dpb11, Sld2, Pol ε, and GINS in budding yeast. Genes Dev 24(6):602–612. doi:10.1101/gad.1883410
Nakajima R, Masukata H (2002) SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in DNA replication in fission yeast. Mol Biol Cell 13(5):1462–1472
Neylon C, Kralicek AV, Hill TM, Dixon NE (2005) Replication termination in Escherichia coli: structure and antihelicase activity of the Tus-Ter complex. Microbiol Mol Biol Rev 69(3):501–526. doi:10.1128/MMBR.69.3.501-526.2005
Ozaki S, Noguchi Y, Hayashi Y, Miyazaki E, Katayama T (2012) Differentiation of the DnaA-oriC subcomplex for DNA unwinding in a replication initiation complex. J Biol Chem 287(44):37458–37471. doi:10.1074/jbc.M112.372052
Rappas M, Oliver AW, Pearl LH (2011) Structure and function of the Rad9-binding region of the DNA-damage checkpoint adaptor TopBP1. Nucleic Acids Res 39(1):313–324. doi:10.1093/nar/gkq743
Reyes-Lamothe R, Sherratt DJ, Leake MC (2010) Stoichiometry and architecture of active DNA replication machinery in Escherichia coli. Science Science 328(5977):498–501. doi:10.1126/science.1185757
Riera A, Tognetti S, Speck C (2014) Helicase loading: how to build a MCM2-7 double-hexamer. Semin Cell Dev Biol 30:104–109. doi:10.1016/j.semcdb.2014.03.008
Saini N, Ramakrishnan S, Elango R, Ayyar S, Zhang Y, Deem A, Ira G, Haber JE, Lobachev KS, Malkova A (2013) Migrating bubble during break-induced replication drives conservative DNA synthesis. Nature 502(7471):389–392. doi:10.1038/nature12584
Sanchez-Pulido L, Diffley JF, Ponting CP (2010) Homology explains the functional similarities of Treslin/Ticrr and Sld3. Curr Biol 20(12):R509–R510. doi:10.1016/j.cub.2010.05.021
Sanders GM, Dallmann HG, McHenry CS (2010) Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases. Mol Cell 37(2):273–281. doi:10.1016/j.molcel.2009.12.025
Sangrithi MN, Bernal JA, Madine M, Philpott A, Lee J, Dunphy WG, Venkitaraman AR (2005) Initiation of DNA replication requires the RECQL4 protein mutated in Rothmund-Thomson syndrome. Cell 121(6):887–898
Sansam CL, Cruz NM, Danielian PS, Amsterdam A, Lau ML, Hopkins N, Lees JA (2010) A vertebrate gene, ticrr, is an essential checkpoint and replication regulator. Genes Dev 24(2):183–194. doi:10.1101/gad.1860310
Sengupta S, van Deursen F, de Piccoli G, Labib K (2013) Dpb2 integrates the leading-strand DNA polymerase into the eukaryotic replisome. Curr Biol 23(7):543–552. doi:10.1016/j.cub.2013.02.011
Sheu YJ, Stillman B (2006) Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated mechanism to promote S phase progression. Mol Cell 24(1):101–113. doi:10.1016/j.molcel.2006.07.033
Sheu YJ, Stillman B (2010) The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory activity in Mcm4. Nature 463(7277):113–117. doi:10.1038/nature08647
Siddiqui K, On KF, Diffley JF (2013) Regulating DNA replication in Eukarya. Cold Spring Harb Perspect Biol 5(9). doi:10.1101/cshperspect.a012930
Simon AC, Zhou JC, Perera RL, van Deursen F, Evrin C, Ivanova ME, Kilkenny ML, Renault L, Kjaer S, Matak-Vinkovic D, Labib K, Costa A, Pellegrini L (2014) A Ctf4 trimer couples the CMG helicase to DNA polymerase alpha in the eukaryotic replisome. Nature 510(7504):293–297. doi:10.1038/nature13234
Skarstad K, Katayama T (2013) Regulating DNA replication in bacteria. Cold Spring Harb Perspect Biol 5(4):a012922. doi:10.1101/cshperspect.a012922
Smith DJ, Whitehouse I (2012) Intrinsic coupling of lagging-strand synthesis to chromatin assembly. Nature 483(7390):434–438. doi:10.1038/nature10895
Soni RK, Mehra P, Choudhury NR, Mukhopadhyay G, Dhar SK (2003) Functional characterization of Helicobacter pylori DnaB helicase. Nucleic Acids Res 31(23):6828–6840
Soni RK, Mehra P, Mukhopadhyay G, Dhar SK (2005) Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo. Biochem J 389(Pt 2):541–548. doi:10.1042/BJ20050062
Sun J, Evrin C, Samel SA, Fernández-Cid A, Riera A, Kawakami H, Stillman B, Speck C, Li H (2013) Cryo-EM structure of a helicase loading intermediate containing ORC–Cdc6–Cdt1–MCM2-7 bound to DNA. Nat Struct Mol Biol 20(8):944–951. doi:10.1038/nsmb.2629
Takara TJ, Bell SP (2011) Multiple Cdt1 molecules act at each origin to load replication-competent Mcm2-7 helicases. EMBO J 30(24):4885–4896. doi:10.1038/emboj.2011.394
Takayama Y, Kamimura Y, Okawa M, Muramatsu S, Sugino A, Araki H (2003) GINS, a novel multiprotein complex required for chromosomal DNA replication in budding yeast. Genes Dev 17(9):1153–1165. doi:10.1101/gad.1065903
Tanaka S, Araki H (2010) Regulation of the initiation step of DNA replication by cyclin-dependent kinases. Chromosoma 119(6):565–574. doi:10.1007/s00412-010-0291-8
Tanaka S, Araki H (2013) Helicase activation and establishment of replication forks at chromosomal origins of replication. Cold Spring Harb Perspect Biol 5(12):a010371. doi:10.1101/cshperspect.a010371
Tanaka S, Tak YS, Araki H (2007) The role of CDK in the initiation step of DNA replication in eukaryotes. Cell Div 2:16. doi:10.1186/1747-1028-2-16
Tanaka H, Katou Y, Yagura M, Saitoh K, Itoh T, Araki H, Bando M, Shirahige K (2009) Ctf4 coordinates the progression of helicase and DNA polymerase alpha. Genes Cells 14(7):807–820. doi:10.1111/j.1365-2443.2009.01310.x
Tanaka S, Nakato R, Katou Y, Shirahige K, Araki H (2011a) Origin association of Sld3, Sld7, and Cdc45 proteins is a key step for determination of origin-firing timing. Curr Biol 21(24):2055–2063. doi:10.1016/j.cub.2011.11.038
Tanaka T, Umemori T, Endo S, Muramatsu S, Kanemaki M, Kamimura Y, Obuse C, Araki H (2011b) Sld7, an Sld3-associated protein required for efficient chromosomal DNA replication in budding yeast. EMBO J 30(10):2019–2030. doi:10.1038/emboj.2011.115
Tanaka S, Komeda Y, Umemori T, Kubota Y, Takisawa H, Araki H (2013) Efficient initiation of DNA replication in eukaryotes requires Dpb11/TopBP1-GINS interaction. Mol Cell Biol 33(13):2614–2622. doi:10.1128/MCB.00431-13
Thomson AM, Gillespie PJ, Blow JJ (2010) Replication factory activation can be decoupled from the replication timing program by modulating Cdk levels. J Cell Biol 188(2):209–221. doi:10.1083/jcb.200911037
Thu YM, Bielinsky A-K (2013) Enigmatic roles of Mcm10 in DNA replication. Trends Biochem Sci:1–11. doi:10.1016/j.tibs.2012.12.003
Tsurimoto T (2006) The role of RF-C and PCNA proteins in maintaining genomic stability. In: DePamphilis ML (ed) DNA replication and human disease. Cold Spring Harbor Press, Cold Spring Harbor, pp 411–434
van Deursen F, Sengupta S, De Piccoli G, Sanchez-Diaz A, Labib K (2012) Mcm10 associates with the loaded DNA helicase at replication origins and defines a novel step in its activation. EMBO J 31(9):2195–2206. doi:10.1038/emboj.2012.69
Watase G, Takisawa H, Kanemaki MT (2012) Mcm10 plays a role in functioning of the eukaryotic replicative DNA helicase, Cdc45-Mcm-GINS. Curr Biol 22(4):343–349. doi:10.1016/j.cub.2012.01.023
Wilson MA, Kwon Y, Xu Y, Chung WH, Chi P, Niu H, Mayle R, Chen X, Malkova A, Sung P, Ira G (2013) Pif1 helicase and Poldelta promote recombination-coupled DNA synthesis via bubble migration. Nature 502(7471):393–396. doi:10.1038/nature12585
Yabuuchi H, Yamada Y, Uchida T, Sunathvanichkul T, Nakagawa T, Masukata H (2006) Ordered assembly of Sld3, GINS and Cdc45 is distinctly regulated by DDK and CDK for activation of replication origins. EMBO J 25(19):4663–4674
Zegerman P, Diffley JF (2007) Phosphorylation of Sld2 and Sld3 by cyclin-dependent kinases promotes DNA replication in budding yeast. Nature 445(7125):281–285. doi:10.1038/nature05432
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Japan
About this chapter
Cite this chapter
Araki, H. (2016). Molecular Mechanism of DNA Replication. In: Hanaoka, F., Sugasawa, K. (eds) DNA Replication, Recombination, and Repair. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55873-6_1
Download citation
DOI: https://doi.org/10.1007/978-4-431-55873-6_1
Published:
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-55871-2
Online ISBN: 978-4-431-55873-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)