ArticleNature structural & molecular biology2024
Structural basis for processive daughter-strand synthesis and proofreading by the human leading-strand DNA polymerase Pol ε.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Structural and single-molecule insights into the core human mitochondrial DNA replisome.The Biochemical journal · 2026Review
- Deficiency in POLE Exonuclease Causes Synthetic Lethality in Highly Aneuploid Cancer Cells.Cancer research · 2026Article
- Interpreting the effects of DNA polymerase variants at the structural level.Molecular oncology · 2026Article
- Understanding single stranded DNA gaps: from formation to fate.The Biochemical journal · 2026Review
- A thumb-domain insertion balances processivity and fidelity in DNA polymerase ε.Nucleic acids research · 2026Article
- Cryo-EM maps of human DNA polymerase ε should be reevaluated in light of its unexpected behavior in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Reply to Roske and Yeeles: Mismatch correction by a replicative polymerase constrained on DNA by a ring.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Comparative Study for the Incorporation of 8-oxo-dATP in DNA by Human DNA Polymerases.International journal of molecular sciences · 2026Article
- ATM immunohistochemistry as an effective screening method for POLE variants among endometrial carcinomas lacking mismatch repair deficiency and p53 abnormalities.The journal of pathology. Clinical research · 2026Article
- Article
- The genetic and biochemical basis of human leading strand synthesis.Nature communications · 2025Article
- Evidence for a functional interaction between yeast Pol ε and PCNA in vivo.Nucleic acids research · 2025Article
- Coordinated transfer of DNA between Pol θ and Pol δ resets microhomology choice during double-strand break repair.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis of multitasking by the apicoplast DNA polymerase from Plasmodium falciparum.Nucleic acids research · 2025Article
- Traditional and New Views on MSI-H/dMMR Endometrial Cancer.Biomolecules · 2025Review
- The human primosome requires replication protein A when copying DNA with inverted repeats.Nucleic acids research · 2025Article
- The proofreading mechanism of the human leading-strand DNA polymerase ε holoenzyme.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Replicative DNA polymerase epsilon and delta holoenzymes show wide-ranging inhibition at G-quadruplexes in the human genome.Nucleic acids research · 2025Article
- A conserved thumb domain insertion in DNA polymerase epsilon supports processive DNA synthesis.Nucleic acids research · 2025Article
- Advances in Immunotherapy for Endometrial Cancer: Insights into MMR Status and Tumor Microenvironment.Cancers · 2024Review
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
During chromosome replication, the nascent leading strand is synthesized by DNA polymerase epsilon (Pol ε), which associates with the sliding clamp processivity factor proliferating cell nuclear antigen (PCNA) to form a processive holoenzyme. For high-fidelity DNA synthesis, Pol ε relies on nucleotide selectivity and its proofreading ability to detect and excise a misincorporated nucleotide. Here, we present cryo-electron microscopy (cryo-EM) structures of human Pol ε in complex with PCNA, DNA and an incoming nucleotide, revealing how Pol ε associates with PCNA through its PCNA-interacting peptide box and additional unique features of its catalytic domain. Furthermore, by solving a series of cryo-EM structures of Pol ε at a mismatch-containing DNA, we elucidate how Pol ε senses and edits a misincorporated nucleotide. Our structures delineate steps along an intramolecular switching mechanism between polymerase and exonuclease activities, providing the basis for a proofreading mechanism in B-family replicative polymerases.
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