![]() ![]() cerevisiae replisome by purified protein factors and the visualization of processive DNA replication at the single-molecule level. We demonstrate here the reconstitution of the S. However, the dynamic behavior of the various replisomal components is largely unexplored due to the challenges associated with averaging over ensembles of molecules that is needed to gain structural and functional insight. Biochemical and structural studies have provided valuable insights into basic enzymatic activities and overall architecture of the eukaryotic replisome. ![]() The commonly accepted model of replication depicts Pol ε stably anchored to CMG but shows Pol δ not physically tethered to the replisome and subsequently replaced for the synthesis of each Okazaki fragment ( Bell and Labib, 2016). On the lagging strand, Pol α-primase generates ~25-nt RNA-DNA primers that Pol δ extends to generate ~150-bp Okazaki fragments ( Bell and Labib, 2016). CMG unwinds DNA by translocating along one of the strands in a 3′ to 5′ direction while forming a complex with Pol ε ( Langston et al., 2014 Sun et al., 2015) to support highly processive synthesis of DNA on the leading strand. Key components include the 11-subunit CMG helicase and three different multi-subunit B-family DNA polymerases: the leading-strand Pol ε, lagging-strand Pol δ, and Pol α-primase ( Bell and Labib, 2016 Burgers and Kunkel, 2017). To robustly synthesize genomic DNA, the eukaryotic replisome requires a large number of interacting protein factors with different enzymatic activities. ![]()
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