A single-molecule view of DNA replication: the dynamic nature of multi-protein complexes revealed
Section snippets
References and recommended reading
Papers of particular interest, published within the period of review, have been highlighted as:
• of special interest
•• of outstanding interest
Acknowledgements
AMvO would like to acknowledge funding from the Netherlands Organization for Scientific Research (NWO; Vici 680-47-607) and the European Research Council (ERC Starting 281098).
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Cited by (22)
Bacterial chromosomes and their replication
2023, Molecular Medical Microbiology, Third EditionComparison of Bacterial and Eukaryotic Replisome Components
2022, Encyclopedia of Cell Biology: Volume 1-6, Second EditionA Primase-Induced Conformational Switch Controls the Stability of the Bacterial Replisome
2020, Molecular CellCitation Excerpt :Instead, frequent turnover of the Pol III∗ in the replisome has been observed (Yuan et al., 2016; Beattie et al., 2017; Lewis et al., 2017), suggesting that the helicase acts as the central organizing structure as opposed to the polymerase. An explanation for this surprising level of plasticity can be found in the network of weak interactions that enable polymerases from solution to eventually replace those at the fork (Geertsema and van Oijen, 2013; Lewis et al., 2017). However, this explanation seems at odds with the putatively strong and stable interaction between multimeric τ in the CLC (Pritchard et al., 2000; Park et al., 2010) and DnaB (Kim et al., 1996; Gao and McHenry, 2001a).
Bacterial replisomes
2018, Current Opinion in Structural BiologyCitation Excerpt :A more recent in vitro single-molecule study showed that leading-strand and lagging-strand DNA synthesis by the E. coli replisome can indeed be carried out in a decoupled and stochastic way, in which both polymerases and helicase work independently [36•]. Considering the exchange of active polymerases at replication forks, perhaps new Pol III* can be utilized to synthesize new OFs at, or even behind, the replication fork, as happens with the T7 replisome [27,28•] (Figure 2b). Excess Pol III* can wait or scan for a new primer and start to synthesize an OF once a new primer is available.
Simultaneous Real-Time Imaging of Leading and Lagging Strand Synthesis Reveals the Coordination Dynamics of Single Replisomes
2016, Molecular CellCitation Excerpt :In the absence of competition, polymerases can continually sample all these sites at the replication fork providing multiple points of contact, ensuring a stable attachment. However, under conditions of competition, the relatively low affinity of the individual interactions within the replisome allows polymerases from solution to quickly outcompete those at the fork, driving polymerase exchange and release (Åberg et al., 2016; Geertsema and van Oijen, 2013). Based on our observations, we envision a spectrum of exchange frequencies and coordination mechanisms among replication systems.
Binding affinities among DNA helicase-primase, DNA polymerase, and replication intermediates in the replisome of bacteriophage T7
2016, Journal of Biological Chemistry