ArticleeLife2015
Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
The trial behind it
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
31 citing papers in PubMed, 43 citations in OpenAlex.
- In vitro reconstitution of chromatin replication recapitulates symmetric histone recycling.Nature communications · 2026Article
- Direct visualisation of post-replication gap formation at the bacterial RRS.bioRxiv : the preprint server for biology · 2026Article
- ATP is dispensable for E. coli DNA replication and eukaryotic helicase activity.Nature communications · 2026Article
- Torsion is a dynamic regulator of DNA replication stalling and reactivation.Nature communications · 2025Article
- Structural basis of multitasking by the apicoplast DNA polymerase from Plasmodium falciparum.Nucleic acids research · 2025Article
- Open architecture of archaea MCM and dsDNA complexes resolved using monodispersed streptavidin affinity CryoEM.Nature communications · 2024Article
- DNA Polymerase Locks Replication Fork Under Stress.bioRxiv : the preprint server for biology · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Synergism between CMG helicase and leading strand DNA polymerase at replication fork.Nature communications · 2023Article
- Mechanism of strand displacement DNA synthesis by the coordinated activities of human mitochondrial DNA polymerase and SSB.Nucleic acids research · 2023Article
- Unravelling How Single-Stranded DNA Binding Protein Coordinates DNA Metabolism Using Single-Molecule Approaches.International journal of molecular sciences · 2023Review
- The N-terminal domain of human mitochondrial helicase Twinkle has DNA-binding activity crucial for supporting processive DNA synthesis by polymerase γ.The Journal of biological chemistry · 2023Article
- DNA Polymerase-Parental DNA Interaction Is Essential for Helicase-Polymerase Coupling during Bacteriophage T7 DNA Replication.International journal of molecular sciences · 2022Article
- Biochemical methods to monitor loading and activation of hexameric helicases.Methods in enzymology · 2022Article
- Quantitative methods to study helicase, DNA polymerase, and exonuclease coupling during DNA replication.Methods in enzymology · 2022Article
- Mechanisms of hexameric helicases.Critical reviews in biochemistry and molecular biology · 2021Review
- Review
- Single-Molecule Insights Into the Dynamics of Replicative Helicases.Frontiers in molecular biosciences · 2021Review
- Different mechanisms for translocation by monomeric and hexameric helicases.Current opinion in structural biology · 2020Review
- Excessive excision of correct nucleotides during DNA synthesis explained by replication hurdles.The EMBO journal · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Leading strand DNA synthesis requires functional coupling between replicative helicase and DNA polymerase (DNAP) enzymes, but the structural and mechanistic basis of coupling is poorly understood. This study defines the precise positions of T7 helicase and T7 DNAP at the replication fork junction with single-base resolution to create a structural model that explains the mutual stimulation of activities. Our 2-aminopurine studies show that helicase and polymerase both participate in DNA melting, but each enzyme melts the junction base pair partially. When combined, the junction base pair is melted cooperatively provided the helicase is located one nucleotide ahead of the primer-end. The synergistic shift in equilibrium of junction base pair melting by combined enzymes explains the cooperativity, wherein helicase stimulates the polymerase by promoting dNTP binding (decreasing dNTP Km), polymerase stimulates the helicase by increasing the unwinding rate-constant (kcat), consequently the combined enzymes unwind DNA with kinetic parameters resembling enzymes translocating on single-stranded DNA.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.