ArticleNature communications2021
Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A conundrum resolved: regulation and activation of UvrD-family DNA helicases/translocases.Trends in biochemical sciences · 2026Review
- Mechanistic models of asymmetric hand-over-hand translocation and nucleosome navigation by CMG helicase.Nature communications · 2025Article
- Unwinding process of DNA/RNA quadruplexes by proteins under label-free nanopore monitoring.Nucleic acids research · 2025Article
- Structural basis for dimerization and activation of UvrD-family helicases.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structure-based discovery of first inhibitors targeting the helicase activity of human PIF1.Nucleic acids research · 2024Article
- Structural Basis for Dimerization and Activation of UvrD-family Helicases.bioRxiv : the preprint server for biology · 2024Article
- Continuous millisecond conformational cycle of a DEAH box helicase reveals control of domain motions by atomic-scale transitions.Communications biology · 2023Article
- Brownian Motion in Optical Tweezers, a Comparison between MD Simulations and Experimental Data in the Ballistic Regime.Polymers · 2023Article
- Rapid single-molecule characterisation of enzymes involved in nucleic-acid metabolism.Nucleic acids research · 2023Article
- Mechanical regulation of the helicase activity of Zika virus NS3.Biophysical journal · 2022Article
- Quantitative and kinetic single-molecule analysis of DNA unwinding byBiophysics and physicobiology · 2022Article
- Monitoring helicase-catalyzed unwinding of multiple duplexes simultaneously.Methods in enzymology · 2022Article
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Authors and funding
7 authors.
Funding
Abstract
UvrD, a model for non-hexameric Superfamily 1 helicases, utilizes ATP hydrolysis to translocate stepwise along single-stranded DNA and unwind the duplex. Previous estimates of its step size have been indirect, and a consensus on its stepping mechanism is lacking. To dissect the mechanism underlying DNA unwinding, we use optical tweezers to measure directly the stepping behavior of UvrD as it processes a DNA hairpin and show that UvrD exhibits a variable step size averaging ~3 base pairs. Analyzing stepping kinetics across ATP reveals the type and number of catalytic events that occur with different step sizes. These single-molecule data reveal a mechanism in which UvrD moves one base pair at a time but sequesters the nascent single strands, releasing them non-uniformly after a variable number of catalytic cycles. Molecular dynamics simulations point to a structural basis for this behavior, identifying the protein-DNA interactions responsible for strand sequestration. Based on structural and sequence alignment data, we propose that this stepping mechanism may be conserved among other non-hexameric helicases.
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