ReviewNucleus (Austin, Tex.)2016
Reconstitution of a eukaryotic replisome reveals the mechanism of asymmetric distribution of DNA polymerases.
Review in Nucleus (Austin, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Analyzing DNA Replication Fork Stability and Collapse Using Chromatin Fiber Analysis and the R-ODD-BLOBS Program.Computational and structural biotechnology journal · 2026Article
- Modelling DNA replication fork stability and collapse using chromatin fiber analysis and the R-ODD-BLOBS program.bioRxiv : the preprint server for biology · 2025Article
- Reconstitution and Coupling of DNA Replication and Segregation in a Biomimetic System.Chembiochem : a European journal of chemical biology · 2019Article
- A recurrent cancer-associated substitution in DNA polymerase ε produces a hyperactive enzyme.Nature communications · 2019Article
- Arranging eukaryotic nuclear DNA polymerases for replication: Specific interactions with accessory proteins arrange Pols α, δ, and ϵ in the replisome for leading-strand and lagging-strand DNA replication.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
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Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Eukaryotes require 3 DNA polymerases for normal replisome operations, DNA polymerases (Pol) α, delta and epsilon. Recent biochemical and structural studies support the asymmetric use of these polymerases on the leading and lagging strands. Pol epsilon interacts with the 11-subunit CMG helicase, forming a 15-protein leading strand complex that acts processively in leading strand synthesis in vitro, but Pol epsilon is inactive on the lagging strand. The opposite results are observed for Pol delta with CMG. Pol delta is highly active on the lagging strand in vitro, but has only feeble activity with CMG on the leading strand. Pol α also functions with CMG to prime both strands, and is even capable of extending both strands with CMG present. However, extensive DNA synthesis by Pol α is sharply curtailed by the presence of either Pol epsilon or Pol delta, which limits the role of the low fidelity Pol α to the initial priming of synthesis.
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Registered trials
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