Sonstiges: |
- Nachgewiesen in: MEDLINE
- Sprachen: English
- Publication Type: Journal Article; Research Support, N.I.H., Extramural
- Language: English
- [Nat Struct Mol Biol] 2020 May; Vol. 27 (5), pp. 461-471. <i>Date of Electronic Publication: </i>2020 Apr 27.
- MeSH Terms: DNA Replication* ; Cell Cycle Proteins / *metabolism ; Checkpoint Kinase 2 / *metabolism ; DNA Helicases / *metabolism ; DNA, Fungal / *biosynthesis ; Saccharomyces cerevisiae / *metabolism ; Saccharomyces cerevisiae Proteins / *metabolism ; Cell Cycle Proteins / genetics ; Checkpoint Kinase 2 / genetics ; DNA Helicases / genetics ; DNA Polymerase II / genetics ; DNA Polymerase II / metabolism ; DNA Polymerase III / genetics ; DNA Polymerase III / metabolism ; DNA Primers ; DNA, Fungal / metabolism ; DNA-Binding Proteins / genetics ; DNA-Binding Proteins / metabolism ; Mutation ; Nuclear Proteins / genetics ; Nuclear Proteins / metabolism ; Nucleosomes / genetics ; Plasmids ; Proliferating Cell Nuclear Antigen / genetics ; Proliferating Cell Nuclear Antigen / metabolism ; Saccharomyces cerevisiae / genetics ; Saccharomyces cerevisiae Proteins / genetics
- References: 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 84, 643–650 (1996). (PMID: 8598050) ; Manosas, M., Spiering, M. M., Ding, F., Croquette, V. & Benkovic, S. J. Collaborative coupling between polymerase and helicase for leading-strand synthesis. Nucleic Acids Res. 40, 6187–6198 (2012). (PMID: 224348863401439) ; Stano, N. M. et al. DNA synthesis provides the driving force to accelerate DNA unwinding by a helicase. Nature 435, 370–373 (2005). (PMID: 159022621563444) ; Yeeles, J. T. P., Janska, A., Early, A. & Diffley, J. F. X. How the eukaryotic replisome achieves rapid and efficient DNA replication. Mol. Cell 65, 105–116 (2017). (PMID: 279894425222725) ; Georgescu, R. E. et al. Mechanism of asymmetric polymerase assembly at the eukaryotic replication fork. Nat. Struct. Mol. Biol. 21, 664–670 (2014). (PMID: 249975984482249) ; Taylor, M. R. G. & Yeeles, J. T. P. The initial response of a eukaryotic replisome to DNA damage. Mol. Cell 70, 1067–1080.e12 (2018). (PMID: 299448886024075) ; Taylor, M. R. G. & Yeeles, J. T. P. Dynamics of replication fork progression following helicase–polymerase uncoupling in eukaryotes. J. Mol. Biol. 431, 2040–2049 (2019). (PMID: 308942926525111) ; Walter, J. & Newport, J. Initiation of eukaryotic DNA replication: origin unwinding and sequential chromatin association of Cdc45, RPA, and DNA polymerase α. Mol Cell 5, 617–627 (2000). (PMID: 10882098) ; Sparks, J. L. et al. The CMG helicase bypasses DNA-protein cross-links to facilitate their repair. Cell 176, 167–181.e21 (2019). (PMID: 30595447) ; Gan, H. et al. Checkpoint Kinase Rad53 Couples Leading- and Lagging-Strand DNA Synthesis under Replication Stress. Mol. Cell 68, 446–455.e3 (2017). (PMID: 290333195802358) ; Katou, Y. et al. S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex. Nature 424, 1078–1083 (2003). (PMID: 12944972) ; Nedelcheva, M. N. et al. Uncoupling of unwinding from DNA synthesis implies regulation of MCM helicase by Tof1/Mrc1/Csm3 checkpoint complex. J. Mol. Biol. 347, 509–521 (2005). (PMID: 15755447) ; Sabatinos, S. A., Green, M. D. & Forsburg, S. L. Continued DNA synthesis in replication checkpoint mutants leads to fork collapse. Mol. Cell. Biol. 32, 4986–4997 (2012). (PMID: 230453963510540) ; Burnham, D. R., Kose, H. B., Hoyle, R. B. & Yardimci, H. The mechanism of DNA unwinding by the eukaryotic replicative helicase. Nat. Commun. 10, 2159 (2019). (PMID: 310891416517413) ; Graham, J. E., Marians, K. J. & Kowalczykowski, S. C. Independent and stochastic action of DNA polymerases in the replisome. Cell 169, 1201–1213.e17 (2017). (PMID: 286225075548433) ; Pardo, B., Crabbe, L. & Pasero, P. Signaling pathways of replication stress in yeast. FEMS Yeast Res. https://doi.org/10.1093/femsyr/fow101 (2017). ; Byun, T. S., Pacek, M., Yee, M. C., Walter, J. C. & Cimprich, K. A. Functional uncoupling of MCM helicase and DNA polymerase activities activates the ATR-dependent checkpoint. Genes Dev. 19, 1040–1052 (2005). (PMID: 158339131091739) ; Tercero, J. A., Longhese, M. P. & Diffley, J. F. A central role for DNA replication forks in checkpoint activation and response. Mol. Cell 11, 1323–1336 (2003). (PMID: 12769855) ; Lopes, M. et al. The DNA replication checkpoint response stabilizes stalled replication forks. Nature 412, 557–561 (2001). (PMID: 11484058) ; Sogo, J. M., Lopes, M. & Foiani, M. Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects. Science 297, 599–602 (2002). (PMID: 12142537) ; De Piccoli, G. et al. Replisome stability at defective DNA replication forks is independent of S phase checkpoint kinases. Mol. Cell 45, 696–704 (2012). (PMID: 2232599222325992) ; Dungrawala, H. et al. The replication checkpoint prevents two types of fork collapse without regulating replisome stability. Mol. Cell 59, 998–1010 (2015). (PMID: 263653794575883) ; Szyjka, S. J. et al. Rad53 regulates replication fork restart after DNA damage in Saccharomyces cerevisiae. Genes Dev. 22, 1906–1920 (2008). (PMID: 186283972492737) ; Iyer, D. R. & Rhind, N. Replication fork slowing and stalling are distinct, checkpoint-independent consequences of replicating damaged DNA. PLoS Genet. 13, e1006958 (2017). (PMID: 288067265570505) ; Poli, J. et al. dNTP pools determine fork progression and origin usage under replication stress. EMBO J. 31, 883–894 (2012). (PMID: 222341853280562) ; Tercero, J. A. & Diffley, J. F. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412, 553–557 (2001). (PMID: 11484057) ; Devbhandari, S., Jiang, J., Kumar, C., Whitehouse, I. & Remus, D. Chromatin constrains the initiation and elongation of DNA replication. Mol. Cell 65, 131–141 (2017). (PMID: 2798943727989437) ; Bell, S. P. & Labib, K. Chromosome duplication in Saccharomyces cerevisiae. Genetics 203, 1027–1067 (2016). (PMID: 2738402627384026) ; Burgers, P. M. J. & Kunkel, T. A. Eukaryotic DNA replication fork. Annu. Rev. Biochem. 86, 417–438 (2017). (PMID: 283017435597965) ; Tahirov, T. H., Makarova, K. S., Rogozin, I. B., Pavlov, Y. I. & Koonin, E. V. Evolution of DNA polymerases: an inactivated polymerase-exonuclease module in Pol ε and a chimeric origin of eukaryotic polymerases from two classes of archaeal ancestors. Biol. Direct 4, 11 (2009). (PMID: 192968562669801) ; Dua, R., Levy, D. L. & Campbell, J. L. Analysis of the essential functions of the C-terminal protein/protein interaction domain of Saccharomyces cerevisiae pol ε and its unexpected ability to support growth in the absence of the DNA polymerase domain. J. Biol. Chem. 274, 22283–22288 (1999). (PMID: 10428796) ; Kesti, T., Flick, K., Keranen, S., Syvaoja, J. E. & Wittenberg, C. DNA polymerase ε catalytic domains are dispensable for DNA replication, DNA repair, and cell viability. Mol. Cell 3, 679–685 (1999). (PMID: 10360184) ; Yu, C. et al. A mechanism for preventing asymmetric histone segregation onto replicating DNA strands. Science 361, 1386–1389 (2018). (PMID: 65972486597248) ; Schauer, G. D. & O’Donnell, M. E. Quality control mechanisms exclude incorrect polymerases from the eukaryotic replication fork. Proc. Natl Acad. Sci. USA 114, 675–680 (2017). (PMID: 28069954) ; Baker, T. A., Sekimizu, K., Funnell, B. E. & Kornberg, A. Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome. Cell 45, 53–64 (1986). (PMID: 3006926) ; Dean, F. B. et al. Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication. Proc. Natl Acad. Sci. USA 84, 16–20 (1987). (PMID: 3025851) ; Wold, M. S., Li, J. J. & Kelly, T. J. Initiation of simian virus 40 DNA replication in vitro: large-tumor-antigen- and origin-dependent unwinding of the template. Proc. Natl Acad. Sci. USA 84, 3643–3647 (1987). (PMID: 3035543) ; Goswami, P. et al. Structure of DNA-CMG-Pol epsilon elucidates the roles of the non-catalytic polymerase modules in the eukaryotic replisome. Nat. Commun. 9, 5061 (2018). (PMID: 3049821630498216) ; Langston, L. D. et al. CMG helicase and DNA polymerase epsilon form a functional 15-subunit holoenzyme for eukaryotic leading-strand DNA replication. Proc. Natl Acad. Sci. USA 111, 15390–15395 (2014). (PMID: 25313033) ; Sun, J. et al. The architecture of a eukaryotic replisome. Nat. Struct. Mol. Biol. 22, 976–982 (2015). (PMID: 48498634849863) ; Douglas, M. E., Ali, F. A., Costa, A. & Diffley, J. F. X. The mechanism of eukaryotic CMG helicase activation. Nature 555, 265–268 (2018). (PMID: 294897496847044) ; Georgescu, R. E. et al. Reconstitution of a eukaryotic replisome reveals suppression mechanisms that define leading/lagging strand operation. Elife 4, e04988 (2015). (PMID: 258718474413876) ; Chilkova, O. 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 Res. 35, 6588–6597 (2007). (PMID: 179058132095795) ; Dua, R., Levy, D. L., Li, C. M., Snow, P. M. & Campbell, J. L. In vivo reconstitution of Saccharomyces cerevisiae DNA polymerase ε in insect cells. Purification and characterization. J. Biol. Chem. 277, 7889–7896 (2002). (PMID: 11756442) ; Ganai, R. A., Bylund, G. O. & Johansson, E. Switching between polymerase and exonuclease sites in DNA polymerase epsilon. Nucleic Acids Res. 43, 932–942 (2015). (PMID: 25550436) ; Garbacz, M. A. et al. Evidence that DNA polymerase δ contributes to initiating leading strand DNA replication in Saccharomyces cerevisiae. Nat. Commun. 9, 858 (2018). (PMID: 58291665829166) ; Acar, M., Becskei, A. & van Oudenaarden, A. Enhancement of cellular memory by reducing stochastic transitions. Nature 435, 228–232 (2005). (PMID: 15889097) ; Szyjka, S. J., Viggiani, C. J. & Aparicio, O. M. Mrc1 is required for normal progression of replication forks throughout chromatin in S. cerevisiae. Mol. Cell 19, 691–697 (2005). (PMID: 16137624) ; 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 19, 699–706 (2005). (PMID: 16137625) ; Smolka, M. B., Albuquerque, C. P., Chen, S. H. & Zhou, H. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc. Natl Acad. Sci. USA 104, 10364–10369 (2007). (PMID: 17563356) ; Alcasabas, A. A. et al. Mrc1 transduces signals of DNA replication stress to activate Rad53. Nat. Cell Biol. 3, 958–965 (2001). (PMID: 11715016) ; Osborn, A. J. & Elledge, S. J. Mrc1 is a replication fork component whose phosphorylation in response to DNA replication stress activates Rad53. Genes Dev. 17, 1755–1767 (2003). (PMID: 12865299196183) ; Can, G., Kauerhof, A. C., Macak, D. & Zegerman, P. Helicase subunit Cdc45 targets the checkpoint kinase Rad53 to both replication initiation and elongation complexes after fork stalling. Mol. Cell 73, 562–573.e3 (2019). (PMID: 305954396375734) ; Langston, L. D. et al. Mcm10 promotes rapid isomerization of CMG-DNA for replisome bypass of lagging strand DNA blocks. Elife 6, e29118 (2017). (PMID: 288690375599239) ; Looke, M., Maloney, M. F. & Bell, S. P. Mcm10 regulates DNA replication elongation by stimulating the CMG replicative helicase. Genes Dev. 31, 291–305 (2017). (PMID: 282705175358725) ; Burgers, P. M. Saccharomyces cerevisiae replication factor C. II. Formation and activity of complexes with the proliferating cell nuclear antigen and with DNA polymerases δ and ε. J. Biol. Chem. 266, 22698–22706 (1991). (PMID: 1682322) ; Toledo, L. I. et al. ATR prohibits replication catastrophe by preventing global exhaustion of RPA. Cell 155, 1088–1103 (2013). (PMID: 24267891) ; Gomez-Gonzalez, B., Patel, H., Early, A. & Diffley, J. F. X. Rpd3L contributes to the DNA damage sensitivity of Saccharomyces cerevisiae checkpoint mutants. Genetics 211, 503–513 (2019). (PMID: 30559326) ; Ilves, I., Tamberg, N. & Botchan, M. R. Checkpoint kinase 2 (Chk2) inhibits the activity of the Cdc45/MCM2-7/GINS (CMG) replicative helicase complex. Proc. Natl Acad. Sci. USA 109, 13163–13170 (2012). (PMID: 22853956) ; Gilbert, C. S., Green, C. M. & Lowndes, N. F. Budding yeast Rad9 is an ATP-dependent Rad53 activating machine. Mol. Cell 8, 129–136 (2001). (PMID: 11511366) ; Gros, J., Devbhandari, S. & Remus, D. Origin plasticity during budding yeast DNA replication in vitro. EMBO J. 33, 621–636 (2014). (PMID: 245669883989655)
- Grant Information: P30 CA008748 United States CA NCI NIH HHS; R01 GM107239 United States GM NIGMS NIH HHS
- Substance Nomenclature: 0 (CDC45 protein, S cerevisiae) ; 0 (Cell Cycle Proteins) ; 0 (DNA Primers) ; 0 (DNA, Fungal) ; 0 (DNA-Binding Proteins) ; 0 (Nuclear Proteins) ; 0 (Nucleosomes) ; 0 (POL30 protein, S cerevisiae) ; 0 (Proliferating Cell Nuclear Antigen) ; 0 (Saccharomyces cerevisiae Proteins) ; EC 2.7.1.11 (Checkpoint Kinase 2) ; EC 2.7.12.1 (RAD53 protein, S cerevisiae) ; EC 2.7.7.7 (DNA Polymerase II) ; EC 2.7.7.7 (DNA Polymerase III) ; EC 3.6.4.- (DNA Helicases)
- Entry Date(s): Date Created: 20200429 Date Completed: 20201001 Latest Revision: 20210331
- Update Code: 20240513
- PubMed Central ID: PMC7225081
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