References
- Lambert S, Carr AM. Impediments to replication fork movement: stabilisation, reactivation and genome instability. Chromosoma. 2013;122:33–45. doi:10.1007/s00412-013-0398-9. PMID:23446515
- Magdalou I, Lopez BS, Pasero P, et al. The causes of replication stress and their consequences on genome stability and cell fate. Semin Cell DevBiol. 2014;30:154–164. doi:10.1016/j.semcdb.2014.04.035.
- Zeman MK, Cimprich KA. Causes and consequences of replication stress. Nat Cell Biol. 2014;16:2–9. doi:10.1038/ncb2897. PMID:24366029
- Muñoz S, Méndez J. DNA replication stress: from molecular mechanisms to human disease. Chromosoma. 2017;126:1–15. doi:10.1007/s00412-016-0573-x. PMID:26797216
- Friedel AM, Pike BL, Gasser SM. ATR/Mec1: coordinating fork stability and repair. Curr Opin Cell Biol. 2009;21:237–244. doi:10.1016/j.ceb.2009.01.017. PMID:19230642
- Branzei D, Foiani M. Maintaining genome stability at the replication fork. Nat Rev Mol Cell Biol. 2010;11:208–219. doi:10.1038/nrm2852. PMID:20177396
- Ciccia A, Elledge SJ. The DNA damage response: making it safe to play with knives. Mol Cell. 2010;40:179–204. doi:10.1016/j.molcel.2010.09.019. PMID:20965415
- Errico A, Costanzo V. Mechanisms of replication fork protection: a safeguard for genome stability. Crit Rev Biochem Mol Biol. 2012;47:222–235. doi:10.3109/10409238.2012.655374. PMID:22324461
- Cortez D. Preventing replication fork collapse to maintain genome integrity. DNA Repair. 2015;32:149–157. doi:10.1016/j.dnarep.2015.04.026. PMID:25957489
- Yazinski SA, Zou L. Functions, Regulation, and Therapeutic Implications of the ATR Checkpoint Pathway. Ann Rev Genet. 2016;50:155–173. doi:10.1146/annurev-genet-121415-121658. PMID:27617969
- Feng W. Mec1/ATR, the program manager of nucleic acids Inc. Genes. 2017;8:10.
- Byun TS, Pacek M, Yee MC, et al. Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes Dev. 2005;19:1040–1052. doi:10.1101/gad.1301205. PMID:15833913
- Nedelcheva MN, Roguev A, Dolapchiev LB, et al. Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex. J Mol Biol. 2005;347:509–521. doi:10.1016/j.jmb.2005.01.041. PMID:15755447
- Zou L, Elledge SJ. Sensing DNA damage through ATRIP recognition of RPA-ssDNA complexes. Science. 2003;300:1542–1548. doi:10.1126/science.1083430. PMID:12791985
- Navadgi-Patil VM, Burgers PM. Cell-cycle-specific activators of the Mec1/ATR checkpoint kinase. Biochem Soc Trans. 2011;39:600–605. doi:10.1042/BST0390600. PMID:21428947
- Bermejo R, Lai Mong S, Foiani M. Preventing replication stress to maintain genome stability: resolving conflicts between replication and transcription. Molecular Cell. 2012;45:710–718. doi:10.1016/j.molcel.2012.03.001. PMID:22464441
- Iyer D, Rhind N. The Intra-S checkpoint responses to DNA damage. Genes. 2017;8:74. doi:10.3390/genes8020074.
- Tanaka K, Russell P. Mrc1 channels the DNA replication arrest signal to checkpoint kinase Cds1. Nat Cell Biol. 2001;3:966–972. doi:10.1038/ncb1101-966. PMID:11715017
- Alcasabas AA, Osborn AJ, Bachant J, et al. Mrc1 transduces signals of DNA replication stress to activate Rad53. Nat Cell Biol. 2001;3:958–965. doi:10.1038/ncb1101-958. PMID:11715016
- Kumagai A, Dunphy WG. Claspin, a novel protein required for the activation of Chk1 during a DNA replication checkpoint response in Xenopus egg extracts. Mol Cell. 2000;6:839–849. doi:10.1016/S1097-2765(05)00092-4. PMID:11090622
- Yang C-C, Suzuki M, Yamakawa S, et al. Claspin recruits Cdc7 kinase for initiation of DNA replication in human cells. Nat Commun. 2016;7:12135. doi:10.1038/ncomms12135. PMID:27401717
- Matsumoto S, Kanoh Y, Shimmoto M, et al. Checkpoint-independent regulation of origin firing by Mrc1 through interaction with Hsk1 kinase. Mol Cell Biol. 2017;37:e00355–e00316. doi:10.1128/MCB.00355-16.
- Szyjka SJ, Viggiani CJ, Aparicio OM. Mrc1 is required for normal progression of replication forks throughout Chromatin in S. cerevisiae. Mol Cell. 2005;19:691–697. doi:10.1016/j.molcel.2005.06.037.
- Tourriere H, Versini G, Cordon-Preciado V, Alabert C, Pasero P. Mrc1 and Tof1 promote replication fork progression and recovery independently of Rad53. Mol Cell 2005; 19. doi:10.1016/j.molcel.2005.07.028. PMID:16137625
- Hodgson B, Calzada A, Labib K. Mrc1 and Tof1 regulate DNA replication Forks in different ways during Normal S phase. Mol Biol Cell. 2007;18:3894–3902. doi:10.1091/mbc.E07-05-0500. PMID:17652453
- Petermann E, Helleday T, Caldecott KW. Claspin promotes normal replication fork rates in human cells. Mol Biol Cell. 2008;19:2373–2378. doi:10.1091/mbc.E07-10-1035. PMID:18353973
- Yeeles JTP, Janska A, Early A, et al. How the Eukaryotic replisome achieves rapid and efficient DNA replication. Mol Cell. 2017;65:105–116. doi:10.1016/j.molcel.2016.11.017. PMID:27989442
- Katou Y, Kanoh Y, Bando M, et al. S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex. Nature 2003;424:1078–1083. doi:10.1038/nature01900. PMID:12944972
- Lou H, Komata M, Katou Y, et al. Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint. Mol Cell. 2008;32:106–117. doi:10.1016/j.molcel.2008.08.020. PMID:18851837
- Duch A, Felipe-Abrio I, Barroso S, et al. Coordinated control of replication and transcription by a SAPK protects genomic integrity. Nature. 2013;493:116–119. doi:10.1038/nature11675. PMID:23178807
- Zhao H, Russell P. DNA binding domain in the replication checkpoint protein Mrc1 of Schizosaccharomyces pombe. J Biol Chem. 2004;279:53023–53027. doi:10.1074/jbc.M410449200. PMID:15471884
- Sar F, Lindsey-Boltz LA, Subramanian D, et al. Human Claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures. J Biol Chem. 2004;279:39289–39295. doi:10.1074/jbc.M405793200. PMID:15226314
- Tanaka T, Yokoyama M, Matsumoto S, et al. Fission yeast Swi1-Swi3 complex facilitates DNA binding of Mrc1. J Biol Chem. 2010;285:39609–39622. doi:10.1074/jbc.M110.173344. PMID:20924116
- Uno S, Masai H. Efficient expression and purification of human replication fork-stabilizing factor, Claspin, from mammalian cells: DNA-binding activity and novel protein interactions. Genes Cells. 2011;16:842–856. doi:10.1111/j.1365-2443.2011.01535.x. PMID:21790909
- Cho W-H, Kang Y-H, An Y-Y, et al. Human Tim-Tipin complex affects the biochemical properties of the replicative DNA helicase and DNA polymerases. Proc Natl Acad Sci. 2013;110:2523–2527. doi:10.1073/pnas.1222494110.
- Aria V, De Felice M, Di Perna R, et al. The human Tim-Tipin complex interacts directly with DNA polymerase ε and stimulates its synthetic activity. J Biol Chem. 2013;288:12742–12752. doi:10.1074/jbc.M112.398073. PMID:23511638
- Quan Y, Xia Y, Liu L, et al. Cell-cycle-regulated interaction between Mcm10 and double Hexameric Mcm2-7 is required for helicase splitting and activation during S phase. Cell Rep. 2015;13:2576–2586. doi:10.1016/j.celrep.2015.11.018. PMID:26686640
- Hogg M, Osterman P, Bylund GO, et al. Structural basis for processive DNA synthesis by yeast DNA polymerase ϵ. Nat Struct Mol Biol. 2014;21:49–55. doi:10.1038/nsmb.2712. PMID:24292646
- Ganai RA, Osterman P, Johansson E. Yeast DNA polymerase ε catalytic core and holoenzyme have comparable catalytic rates. J Biol Chem. 2015;290:3825–3835. doi:10.1074/jbc.M114.615278. PMID:25538242
- Ganai RA, Zhang X-P, Heyer W-D, et al. Strand displacement synthesis by yeast DNA polymerase ϵ. Nucleic Acids Res. 2016;44:8229–8240. doi:10.1093/nar/gkw556. PMID:27325747
- Dua R, Edwards S, Levy DL, et al. Subunit interactions within the saccharomyces cerevisiae DNA Polymerase ϵ (pol ϵ) complex: DEMONSTRATION OF A DIMERIC pol ϵ. J Biol Chem. 2000;275:28816–28825. doi:10.1074/jbc.M002376200. PMID:10878005
- Niu Y, Xia Y, Wang S, et al. A PRototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns. J Biol Chem. 2013;288:13728–13740. doi:10.1074/jbc.M113.452979. PMID:23530048