ArticleProceedings of the National Academy of Sciences of the United States of America2017
Quality control mechanisms exclude incorrect polymerases from the eukaryotic replication fork.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 59 citations in OpenAlex.
- Reconstituting human and SV40 replisomes with Okazaki fragment maturation reveals synchronized leading- and lagging-strand synthesis.Nature communications · 2026Article
- DNA Polymerase α has pyrimidine dimer translesion activity that is suppressed during normal replication.bioRxiv : the preprint server for biology · 2026Article
- Revised mechanism of hydroxyurea-induced cell cycle arrest and an improved alternative.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Single-molecule characterization of SV40 replisome and novel factors: human FPC and Mcm10.Nucleic acids research · 2024Article
- CAF-1 deposits newly synthesized histones during DNA replication using distinct mechanisms on the leading and lagging strands.Nucleic acids research · 2023Article
- Mechanistic investigation of human maturation of Okazaki fragments reveals slow kinetics.Nature communications · 2022Article
- The Fork Protection Complex: A Regulatory Hub at the Head of the Replisome.Sub-cellular biochemistry · 2022Article
- DNA replication machinery: Insights fromComputational and structural biotechnology journal · 2021Review
- Mechanisms for Maintaining Eukaryotic Replisome Progression in the Presence of DNA Damage.Frontiers in molecular biosciences · 2021Review
- Limiting DNA polymerase delta alters replication dynamics and leads to a dependence on checkpoint activation and recombination-mediated DNA repair.PLoS genetics · 2021Article
- Replisome bypass of a protein-based R-loop block by Pif1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular mechanisms of eukaryotic origin initiation, replication fork progression, and chromatin maintenance.The Biochemical journal · 2020Article
- Structure of the polymerase ε holoenzyme and atomic model of the leading strand replisome.Nature communications · 2020Article
- High density of unrepaired genomic ribonucleotides leads to Topoisomerase 1-mediated severe growth defects in absence of ribonucleotide reductase.Nucleic acids research · 2020Article
- Rad53 limits CMG helicase uncoupling from DNA synthesis at replication forks.Nature structural & molecular biology · 2020Article
- Structure of the processive human Pol δ holoenzyme.Nature communications · 2020Article
- Acute hydroxyurea-induced replication blockade results in replisome components disengagement from nascent DNA without causing fork collapse.Cellular and molecular life sciences : CMLS · 2020Article
- The absence of the catalytic domains of Saccharomyces cerevisiae DNA polymerase ϵ strongly reduces DNA replication fidelity.Nucleic acids research · 2019Article
- DNA polymerase η contributes to genome-wide lagging strand synthesis.Nucleic acids research · 2019Article
- Mechanism of Bidirectional Leading-Strand Synthesis Establishment at Eukaryotic DNA Replication Origins.Molecular cell · 2018Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The eukaryotic genome is primarily replicated by two DNA polymerases, Pol ε and Pol δ, that function on the leading and lagging strands, respectively. Previous studies have established recruitment mechanisms whereby Cdc45-Mcm2-7-GINS (CMG) helicase binds Pol ε and tethers it to the leading strand, and PCNA (proliferating cell nuclear antigen) binds tightly to Pol δ and recruits it to the lagging strand. The current report identifies quality control mechanisms that exclude the improper polymerase from a particular strand. We find that the replication factor C (RFC) clamp loader specifically inhibits Pol ε on the lagging strand, and CMG protects Pol ε against RFC inhibition on the leading strand. Previous studies show that Pol δ is slow and distributive with CMG on the leading strand. However, Saccharomyces cerevisiae Pol δ-PCNA is a rapid and processive enzyme, suggesting that CMG may bind and alter Pol δ activity or position it on the lagging strand. Measurements of polymerase binding to CMG demonstrate Pol ε binds CMG with a K
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