ArticleNucleic acids research2015
Structural basis for DNA strand separation by a hexameric replicative helicase.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Viro3D: a comprehensive database of virus protein structure predictions.Molecular systems biology · 2025Article
- Assembly and breakage of head-to-head double hexamer reveals mpox virus E5-catalyzed DNA unwinding initiation.Nature communications · 2025Article
- Article
- Determining translocation orientations of nucleic acid helicases.Methods (San Diego, Calif.) · 2022Review
- Unwinding of a DNA replication fork by a hexameric viral helicase.Nature communications · 2021Article
- Ring-shaped replicative helicase encircles double-stranded DNA during unwinding.Nucleic acids research · 2019Article
- Structural and functional analysis of the nucleotide and DNA binding activities of the human PIF1 helicase.Nucleic acids research · 2019Article
- Structural Study of Heterogeneous Biological Samples by Cryoelectron Microscopy and Image Processing.BioMed research international · 2017Review
- Domain Organization of Vaccinia Virus Helicase-Primase D5.Journal of virology · 2016Article
- Structural Based Analyses of the JC Virus T-Antigen F258L Mutant Provides Evidence for DNA Dependent Conformational Changes in the C-Termini of Polyomavirus Origin Binding Domains.PLoS pathogens · 2016Article
- Structural Mechanisms of Hexameric Helicase Loading, Assembly, and Unwinding.F1000Research · 2016Review
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Hexameric helicases are processive DNA unwinding machines but how they engage with a replication fork during unwinding is unknown. Using electron microscopy and single particle analysis we determined structures of the intact hexameric helicase E1 from papillomavirus and two complexes of E1 bound to a DNA replication fork end-labelled with protein tags. By labelling a DNA replication fork with streptavidin (dsDNA end) and Fab (5' ssDNA) we located the positions of these labels on the helicase surface, showing that at least 10 bp of dsDNA enter the E1 helicase via a side tunnel. In the currently accepted 'steric exclusion' model for dsDNA unwinding, the active 3' ssDNA strand is pulled through a central tunnel of the helicase motor domain as the dsDNA strands are wedged apart outside the protein assembly. Our structural observations together with nuclease footprinting assays indicate otherwise: strand separation is taking place inside E1 in a chamber above the helicase domain and the 5' passive ssDNA strands exits the assembly through a separate tunnel opposite to the dsDNA entry point. Our data therefore suggest an alternative to the current general model for DNA unwinding by hexameric helicases.
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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.