Insights into the Initiation of Eukaryotic DNA Replication

References

• Bell SP, Dutta A. DNA replication in eukaryotic cells. Annu Rev Biochem 2002; 71:333-74; PMID:12045100; http://dx.doi.org/10.1146/annurev.biochem.71.110601.135425
   PubMed Web of Science ®Google Scholar
• Green B, Finn K, Li J. Loss of DNA replication control is a potent inducer of gene amplification. Science 2010; 329:943-46; PMID:20724634; http://dx.doi.org/10.1126/science.1190966
   PubMed Web of Science ®Google Scholar
• Georgescu R, Schauer G, Yao N, Langston L, Yurieva O, Zhang D, Finkelstein J, O'Donnell, M. Reconstitution of a eukaryotic replisome reveals suppression mechanisms that define leading/lagging strand operation. Elife 2015; 4:e04988; PMID:25871847; http://dx.doi.org/10.7554/eLife.04988
   PubMed Web of Science ®Google Scholar
• Pursell Z, Isoz I, Lundström E, Johansson E, Kunkel T. Yeast DNA polymerase epsilon participates in leading-strand DNA replication. Science 2007; 317:127-30; PMID:17615360; http://dx.doi.org/10.1126/science.1144067
   PubMed Web of Science ®Google Scholar
• Johnson R, Klassen R, Prakash L, Prakash S. A Major Role of DNA Polymerase δ in Replication of Both the Leading and Lagging DNA Strands. Mol Cell 2015; 59:163-75; PMID:26145172; http://dx.doi.org/10.1016/j.molcel.2015.05.038
   PubMed Web of Science ®Google Scholar
• Tognetti S, Riera A, Speck C. Switch on the engine: how the eukaryotic replicative helicase MCM2-7 becomes activated. Chromosoma 2015; 124:13-26; PMID:25308420; http://dx.doi.org/10.1007/s00412-014-0489-2
   PubMed Web of Science ®Google Scholar
• Ilves I, Petojevic T, Pesavento J, Botchan M. Activation of the MCM2-7 Helicase by Association with Cdc45 and GINS Proteins. Mol Cell 2010; 37:247-58; PMID:20122406; http://dx.doi.org/10.1016/j.molcel.2009.12.030
   PubMed Web of Science ®Google Scholar
• Bochman M, Schwacha A. The Mcm2-7 complex has in vitro helicase activity. Mol Cell 2008; 31:287-93; PMID:18657510; http://dx.doi.org/10.1016/j.molcel.2008.05.020
   PubMed Web of Science ®Google Scholar
• Fletcher R, Shen J, Gomez-Llorente Y, Martin CS, Carazo JM, Chen X. Double hexamer disruption and biochemical activities of Methanobacterium thermoautotrophicum MCM. J Biol Chem 2005; 280:42405-10; PMID:16221679; http://dx.doi.org/10.1074/jbc.M509773200
   PubMed Web of Science ®Google Scholar
• Remus D, Beuron F, Tolun G, Griffith J, Morris E, Diffley J. Concerted loading of Mcm2-7 double hexamers around DNA during DNA replication origin licensing. Cell 2009; 139:719-730; PMID:19896182; http://dx.doi.org/10.1016/j.cell.2009.10.015
   PubMed Web of Science ®Google Scholar
• Evrin C, Clarke P, Zech J, Lurz R, Sun J, Uhle S, Li H, Stillman B, Speck C. A double-hexameric MCM2-7 complex is loaded onto origin DNA during licensing of eukaryotic DNA replication. Proc Natl Acad Sci U S A 2009; 106:20240-20245; PMID:19910535; http://dx.doi.org/10.1073/pnas.0911500106
   PubMed Web of Science ®Google Scholar
• Ticau S, Friedman L, Ivica N, Gelles J, Bell S. Single-molecule studies of origin licensing reveal mechanisms ensuring bidirectional helicase loading. Cell 2015; 161:513-525; PMID:25892223; http://dx.doi.org/10.1016/j.cell.2015.03.012
   PubMed Web of Science ®Google Scholar
• Frigola J, Remus D, Mehanna A, Diffley J. ATPase-dependent quality control of DNA replication origin licensing. Nature 2013; 495:339-343; PMID:23474987; http://dx.doi.org/10.1038/nature11920
   PubMed Web of Science ®Google Scholar
• Fernández-Cid A, Riera A, Tognetti S, Herrera M, Samel S, Evrin C, Winkler C, Gardenal E, Uhle S, Speck C. An ORC/Cdc6/MCM2-7 Complex Is Formed in a Multistep Reaction to Serve as a Platform for MCM Double-Hexamer Assembly. Mol Cell 2013; 50:577-588; http://dx.doi.org/10.1016/j.molcel.2013.03.026
   PubMed Web of Science ®Google Scholar
• Diffley J. The many faces of redundancy in DNA replication control. Cold Spring Harb Symp Quant Biol 2010; 75:135-142; PMID:21502406; http://dx.doi.org/10.1101/sqb.2010.75.062
   PubMedGoogle Scholar
• Ge X, Jackson D, Blow J. Dormant origins licensed by excess Mcm2-7 are required for human cells to survive replicative stress. Genes Dev 2007; 21:3331-3341; PMID:18079179; http://dx.doi.org/10.1101/gad.457807
   PubMed Web of Science ®Google Scholar
• Kawabata T, Luebben S, Yamaguchi S, Ilves I, Matise I, Buske T, Botchan M, Shima N. Stalled fork rescue via dormant replication origins in unchallenged S phase promotes proper chromosome segregation and tumor suppression. Mol Cell 2011; 41:543-553; PMID:21362550; http://dx.doi.org/10.1016/j.molcel.2011.02.006
   PubMed Web of Science ®Google Scholar
• Moyer S, Lewis P, Botchan M. 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 2006; 103:10236-10241; PMID:16798881; http://dx.doi.org/10.1073/pnas.0602400103
   PubMed Web of Science ®Google Scholar
• Gambus A, Jones RC, Sanchez-Diaz A, Kanemaki M, Deursen FV, Edmondson RD, Labib K. GINS maintains association of Cdc45 with MCM in replisome progression complexes at eukaryotic DNA replication forks. Nat Cell Biol 2006; 8:358-366; PMID:16531994; http://dx.doi.org/10.1038/ncb1382
   PubMed Web of Science ®Google Scholar
• Pacek M, Tutter A, Kubota Y, Takisawa H, Walter J. Localization of MCM2-7, Cdc45, and GINS to the site of DNA unwinding during eukaryotic DNA replication. Mol Cell 2006; 21:581-587; PMID:16483939; http://dx.doi.org/10.1016/j.molcel.2006.01.030
   PubMed Web of Science ®Google Scholar
• Costa A, Renault L, Swuec P, Petojevic T, Pesavento J, Ilves I, MacLellan-Gibson K, Fleck R, Botchan M, Berger J. DNA binding polarity, dimerization, and ATPase ring remodeling in the CMG helicase of the eukaryotic replisome. Elife 2014; 3 Aug 12:e03273
   PubMed Web of Science ®Google Scholar
• Kanemaki M, Labib K. Distinct roles for Sld3 and GINS during establishment and progression of eukaryotic DNA replication forks. EMBO J 2006; 25:1753-1763; PMID:16601689; http://dx.doi.org/10.1038/sj.emboj.7601063
   PubMed Web of Science ®Google Scholar
• Zegerman P, Diffley JF. Phosphorylation of Sld2 and Sld3 by cyclin-dependent kinases promotes DNA replication in budding yeast. Nature 2007; 445:281-285; PMID:17167417; http://dx.doi.org/10.1038/nature05432
   PubMed Web of Science ®Google Scholar
• Tanaka S, Umemori T, Hirai K, Muramatsu S, Kamimura Y, Araki H. CDK-dependent phosphorylation of Sld2 and Sld3 initiates DNA replication in budding yeast. Nature 2007; 445:328-332; PMID:17167415; http://dx.doi.org/10.1038/nature05465
   PubMed Web of Science ®Google Scholar
• Kumagai A, Shevchenko A, Shevchenko A, Dunphy W. Treslin collaborates with TopBP1 in triggering the initiation of DNA replication. Cell 2010; 140:349-359; PMID:20116089; http://dx.doi.org/10.1016/j.cell.2009.12.049
   PubMed Web of Science ®Google Scholar
• Kumagai A, Shevchenko A, Shevchenko A, Dunphy W. Direct regulation of Treslin by cyclin-dependent kinase is essential for the onset of DNA replication. J Cell Biol 2011; 193:995-1007; PMID:21646402; http://dx.doi.org/10.1083/jcb.201102003
   PubMed Web of Science ®Google Scholar
• Matsuno K, Kumano M, Kubota Y, Hashimoto Y, Takisawa H. The N-terminal noncatalytic region of Xenopus RecQ4 is required for chromatin binding of DNA polymerase α in the initiation of DNA replication. Mol Cell Biol 2006; 26:4843-4852; PMID:16782873; http://dx.doi.org/10.1128/MCB.02267-05
   PubMed Web of Science ®Google Scholar
• Boos D, Sanchez-Pulido L, Rappas M, Pearl L, Oliver A, Ponting C, Diffley J. Regulation of DNA Replication through Sld3-Dpb11 Interaction Is Conserved from Yeast to Humans. Curr Biol 2011; 21:1152-1157; PMID:21700459; http://dx.doi.org/10.1016/j.cub.2011.05.057
   PubMed Web of Science ®Google Scholar
• Itou H, Shirakihara Y, Araki H. The quaternary structure of the eukaryotic DNA replication proteins Sld7 and Sld3. Acta Crystallogr D Biol Crystallogr 2015; 71:1649-1656; PMID:26249346; http://dx.doi.org/10.1107/S1399004715010457
   PubMed Web of Science ®Google Scholar
• Mantiero D, Mackenzie A, Donaldson A, Zegerman P. Limiting replication initiation factors execute the temporal programme of origin firing in budding yeast. EMBO J 2011; 30:4805-4814; PMID:22081107; http://dx.doi.org/10.1038/emboj.2011.404
   PubMed Web of Science ®Google Scholar
• Zegerman P, Diffley JFX. DNA replication as a target of the DNA damage checkpoint. DNA Repair (Amst) 2009; 8:1077-1088; PMID:19505853; http://dx.doi.org/10.1016/j.dnarep.2009.04.023
   PubMed Web of Science ®Google Scholar
• Yeeles J, Deegan T, Janska A, Early A, Diffley J. Regulated eukaryotic DNA replication origin firing with purified proteins. Nature 2015; 519:431-435; PMID:25739503; http://dx.doi.org/10.1038/nature14285
   PubMed Web of Science ®Google Scholar
• Labib K. How do Cdc7 and cyclin-dependent kinases trigger the initiation of chromosome replication in eukaryotic cells?s Genes Dev 2010; 24:1208-1219; PMID:20551170; http://dx.doi.org/10.1101/gad.1933010
   PubMed Web of Science ®Google Scholar
• Randell J, Fan A, Chan C, Francis L, Heller R, Galani K, Bell S. Mec1 is one of multiple kinases that prime the Mcm2-7 helicase for phosphorylation by Cdc7. Mol Cell 2010; 40:353-363; PMID:21070963; http://dx.doi.org/10.1016/j.molcel.2010.10.017
   PubMed Web of Science ®Google Scholar
• Masai H, Taniyama C, Ogino K, Matsui E, Kakusho N, Matsumoto S, Kim J, Ishii A, Tanaka T, Kobayashi T, et al. Phosphorylation of MCM4 by Cdc7 kinase facilitates its interaction with Cdc45 on the chromatin. J Biol Chem 2006; 281:39249-39261; PMID:17046832; http://dx.doi.org/10.1074/jbc.M608935200
   PubMed Web of Science ®Google Scholar
• Sheu YJ, Stillman B. Cdc7-Dbf4 phosphorylates MCM proteins via a docing site-mediated mechanism to promote S phase progression. Mol Cell 2006; 24:101-113; PMID:17018296; http://dx.doi.org/10.1016/j.molcel.2006.07.033
   PubMed Web of Science ®Google Scholar
• Sheu Y, Kinney J, Lengronne A, Pasero P, Stillman B. Domain within the helicase subunit Mcm4 integrates multiple kinase signals to control DNA replication initiation and fork progression. Proc Natl Acad Sci U S A 2014; 111:E1899-1908; PMID:24740181; http://dx.doi.org/10.1073/pnas.1404063111
   PubMed Web of Science ®Google Scholar
• Sheu Y, Stillman B. The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory activity in Mcm4. Nature 2010; 463:113-117; PMID:20054399; http://dx.doi.org/10.1038/nature08647
   PubMed Web of Science ®Google Scholar
• Lei M, Kawasaki Y, Young M, Kihara M, Sugino A, Tye B. MCM2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis. Genes Dev 1997; 11:3365-3374; PMID:9407029; http://dx.doi.org/10.1101/gad.11.24.3365
   PubMed Web of Science ®Google Scholar
• Bruck I, Kaplan D. Dbf4-Cdc7 phosphorylation of Mcm2 is required for cell growth. J Biol Chem 2009; 284:28823-28831; PMID:19692334; http://dx.doi.org/10.1074/jbc.M109.039123
   PubMed Web of Science ®Google Scholar
• Stead B, Brandl C, Davey M. Phosphorylation of Mcm2 modulates Mcm2-7 activity and affects the cell's response to DNA damage. Nucleic Acids Res 2011; 39:6998-7008; PMID:21596784; http://dx.doi.org/10.1093/nar/gkr371
   PubMed Web of Science ®Google Scholar
• Bruck I, Kaplan DL. The Dbf4-Cdc7 kinase promotes Mcm2-7 ring opening to allow for single-stranded DNA extrusion and helicase assembly. J Biol Chem 2015; 290:1210-1221; PMID:25471369; http://dx.doi.org/10.1074/jbc.M114.608232
   PubMed Web of Science ®Google Scholar
• Bruck I, Kaplan D. Conserved mechanism for coordinating replication fork helicase assembly with phosphorylation of the helicase. Proc Natl Acad Sci U S A 2015; 112:11223-11228; PMID:26305950; http://dx.doi.org/10.1073/pnas.1509608112
   PubMed Web of Science ®Google Scholar
• Samel S, Fernández-Cid A, Sun J, Riera A, Tognetti S, Herrera M, Li H, Speck C. A unique DNA entry gate serves for regulated loading of the eukaryotic replicative helicase MCM2-7 onto DNA. Genes Dev 2014; 28:1653-1666; PMID:25085418; http://dx.doi.org/10.1101/gad.242404.114
   PubMed Web of Science ®Google Scholar
• Hardy CFJ, Dryga O, Seematter S, Pahl PMB, Sclafani RA. mcm5/cdc46-bob1 bypasses the requirement for the S phase activatorCdc7p. Proc Natl Acad Sci U S A 1997; 94:3151-3155; PMID:9096361; http://dx.doi.org/10.1073/pnas.94.7.3151
   PubMed Web of Science ®Google Scholar
• Itou H, Muramatsu S, Shirakihara Y, Araki H. Crystal structure of the homology domain of the eukaryotic DNA replication proteins Sld3 Treslin Structure 2014; 22:1341-1347; PMID:25126958; http://dx.doi.org/10.1016/j.str.2014.07.001
   PubMed Web of Science ®Google Scholar
• Kamimura Y, Tak YS, Sugino A, Araki H. Sld3, which interacts with Cdc45 (Sld4), functions for chromosomal DNA replication in Saccharomyces cerevisiae. EMBO J 2001; 20:2097-2107; PMID:11296242; http://dx.doi.org/10.1093/emboj/20.8.2097
   PubMed Web of Science ®Google Scholar
• Dhingra N, Bruck I, Smith S, Ning B, Kaplan D. Dpb11 helps control assembly of the Cdc45-Mcm2-7-GINS replication fork helicase. J Biol Chem 2015; 290:7586-7601; PMID:25659432; http://dx.doi.org/10.1074/jbc.M115.640383
   PubMed Web of Science ®Google Scholar
• Bruck I, Kaplan D. The replication initiation protein sld2 regulates helicase assembly. J Biol Chem 2014; 289:1948-1959; PMID:24307213; http://dx.doi.org/10.1074/jbc.M113.532085
   PubMed Web of Science ®Google Scholar
• Bruck I, Kaplan DL. The replication initiation protein Sld3/Treslin orchestrates the assembly of the replication fork helicase during S phase. J Biol Chem 2015; 290(45):27414-24; PMID: 26405041; http://dx.doi.org/10.1074/jbc.M115.688424
   PubMed Web of Science ®Google Scholar
• Ohlenschläger O, Kuhnert A, Schneider A, Haumann S, Bellstedt P, Keller H, Saluz HP, Hortschansky P, Hänel F, Grosse F, et al. The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif. Nucleic Acids Res 2012; 40:8309-8324; http://dx.doi.org/10.1093/nar/gks591
   PubMed Web of Science ®Google Scholar
• Geraghty D, Ding M, Heintz N, Pederson D. Premature structural changes at replication origins in a yeast minichromosome maintenance (MCM) mutant. J Biol Chem 2000; 275:18011-18021; PMID:10751424; http://dx.doi.org/10.1074/jbc.M909787199
   PubMed Web of Science ®Google Scholar
• Fu Y, Yardimci H, Long D, Ho T, Guainazzi A, Bermudez V, Hurwitz J, van Oijen A, Schärer O, Walter J. Selective bypass of a lagging strand roadblock by the eukaryotic replicative DNA helicase. Cell 2011; 146:931-941; PMID:21925316; http://dx.doi.org/10.1016/j.cell.2011.07.045
   PubMed Web of Science ®Google Scholar
• Takahashi TS, Wigley DB, Walter JC. Pumps, paradoxes, and ploughshares: mechanism of the Mcm2-7 DNA helicase. Trends Biochem Sci 2005; 30:437-444; PMID:16002295; http://dx.doi.org/10.1016/j.tibs.2005.06.007
   PubMed Web of Science ®Google Scholar
• Gai D, Chang Y, Chen X. Origin DNA melting and unwinding in DNA replication. Curr Opin Struct Biol 2010; 20:756-762; PMID:20870402; http://dx.doi.org/10.1016/j.sbi.2010.08.009
   PubMed Web of Science ®Google Scholar
• Herrera, MC, Tognetti, S, Riera, A, Zech, J, Clarke P, Fernández-Cid A, Speck C. A reconstituted system reveals how activating and inhibitory interactions control DDK dependent assembly of the eukaryotic replicative helicase. Nucleic Acids Res 2015; 43(21):10238-10250; PMID: 26338774; http://dx.doi.org/10.1093/nar/gkv881
   PubMed Web of Science ®Google Scholar
• Solomon N, Wright M, Chang S, Buckley A, Dumas L, Gaber R. Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle genes in Saccharomyces cerevisiae. Yeast 1992; 8:273-289; PMID:1514326; http://dx.doi.org/10.1002/yea.320080405
   PubMed Web of Science ®Google Scholar
• Merchant A, Kawasaki Y, Chen Y, Lei M, Tye BK. A lesion in the DNA replication initiation factor Mcm10 induces pausing of elongation forks through chromosomal replication origins in S. cerevisiae. Mol Cell Biol 1997; 17:3261-3271; PMID:9154825; http://dx.doi.org/10.1128/MCB.17.6.3261
   PubMed Web of Science ®Google Scholar
• Thu Y, Bielinsky A. Enigmatic rles of Mcm10 in DNA replication. Trends Biochem Sci 2013; 38:184-194; PMID:23332289; http://dx.doi.org/10.1016/j.tibs.2012.12.003
   PubMed Web of Science ®Google Scholar
• Wohlschlegel J, Dhar S, Prokhorova T, Dutta, A, Walter J. Xenopus Mcm10 binds to origins of DNA replication after Mcm2-7 and stimulates origin binding of Cdc45. Mol Cell 2002; 9:233-240; PMID:11864598; http://dx.doi.org/10.1016/S1097-2765(02)00456-2
   PubMed Web of Science ®Google Scholar
• Gregan J, Lindner K, Brimage L, Franklin R, Namdar M, Hart E, Aves S, Kearsey S. Fission yeast Cdc23/Mcm10 functions after pre-replicative complex formation to promote Cdc45 chromatin binding. Mol Biol Cell 2003; 14:3876-3887; PMID:12972571; http://dx.doi.org/10.1091/mbc.E03-02-0090
   PubMed Web of Science ®Google Scholar
• Sawyer S, Cheng I, Chai W, Tye B. Mcm10 and Cdc45 cooperate in origin activation in Saccharomyces cerevisiae. J Mol Biol 2004; 340:195-202; PMID:15201046; http://dx.doi.org/10.1016/j.jmb.2004.04.066
   PubMed Web of Science ®Google Scholar
• Im JS, Ki SH, Farina A, Jung DS, Hurwitz J, Leea JK. Assembly of the Cdc45-Mcm2-7-GINS complex in human cells requires the Ctf4/And-1, RecQL4, and Mcm10 proteins. Proc Natl Acad Sci U S A 2009; 106:15628-15632; PMID:19805216; http://dx.doi.org/10.1073/pnas.0908039106
   PubMed Web of Science ®Google Scholar
• Watase G, Takisawa H, Kanemaki M. Mcm10 plays a role in functioning of the eukaryotic replicative DNA helicase, Cdc45-Mcm-GINS. Curr Biol 2012; 22:343-349; PMID:22285032; http://dx.doi.org/10.1016/j.cub.2012.01.023
   PubMed Web of Science ®Google Scholar
• 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 J 2012; 31:2195-2206; PMID:22433841; http://dx.doi.org/10.1038/emboj.2012.69
   PubMed Web of Science ®Google Scholar
• Kanke M, Kodama Y, Takahashi T, Nakagawa T, Masukata H. Mcm10 plays an essential role in origin DNA unwinding after loading of the CMG components. EMBO J 2012; 31:2182-2194; PMID:22433840; http://dx.doi.org/10.1038/emboj.2012.68
   PubMed Web of Science ®Google Scholar
• Ricke R, Bielinsky A. A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-α in budding yeast. J Biol Chem 2006; 281:18414-18425; PMID:16675460; http://dx.doi.org/10.1074/jbc.M513551200
   PubMed Web of Science ®Google Scholar
• Ricke RM, Bielinsky AK. Mcm10 regulates the stability and chromatin association of DNA polymerase-α. Mol Cell 2004; 16:173-185; PMID:15494305; http://dx.doi.org/10.1016/j.molcel.2004.09.017
   PubMed Web of Science ®Google Scholar