ArticleNucleic acids research2016
Sequence-dependent nanometer-scale conformational dynamics of individual RecBCD-DNA complexes.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Specific Monitoring the DNA Helicase Function via Anchor-Embedded DNA Probe.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- E. coli RecB Nuclease Domain Regulates RecBCD Helicase Activity but not Single Stranded DNA Translocase Activity.Journal of molecular biology · 2024Article
- Protamine folds DNA into flowers and loop stacks.Biophysical journal · 2023Article
- Kinetic and structural mechanism for DNA unwinding by a non-hexameric helicase.Nature communications · 2021Article
- Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.Journal of molecular biology · 2021Article
- Modelling single-molecule kinetics of helicase translocation using high-resolution nanopore tweezers (SPRNT).Essays in biochemistry · 2021Review
- Protamine loops DNA in multiple steps.Nucleic acids research · 2020Article
- Determining the effects of DNA sequence on Hel308 helicase translocation along single-stranded DNA using nanopore tweezers.Nucleic acids research · 2019Article
- Article
- How Does a Helicase Unwind DNA? Insights from RecBCD Helicase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018Review
- Helicase SPRNTing through the nanopore.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Revealing dynamics of helicase translocation on single-stranded DNA using high-resolution nanopore tweezers.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Shuttling along DNA and directed processing of D-loops by RecQ helicase support quality control of homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Processive DNA Unwinding by RecBCD Helicase in the Absence of Canonical Motor Translocation.Journal of molecular biology · 2016Article
Corrections and comments
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Authors and funding
7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
RecBCD is a multifunctional enzyme that possesses both helicase and nuclease activities. To gain insight into the mechanism of its helicase function, RecBCD unwinding at low adenosine triphosphate (ATP) (2-4 μM) was measured using an optical-trapping assay featuring 1 base-pair (bp) precision. Instead of uniformly sized steps, we observed forward motion convolved with rapid, large-scale (∼4 bp) variations in DNA length. We interpret this motion as conformational dynamics of the RecBCD-DNA complex in an unwinding-competent state, arising, in part, by an enzyme-induced, back-and-forth motion relative to the dsDNA that opens and closes the duplex. Five observations support this interpretation. First, these dynamics were present in the absence of ATP. Second, the onset of the dynamics was coupled to RecBCD entering into an unwinding-competent state that required a sufficiently long 5' strand to engage the RecD helicase. Third, the dynamics were modulated by the GC-content of the dsDNA. Fourth, the dynamics were suppressed by an engineered interstrand cross-link in the dsDNA that prevented unwinding. Finally, these dynamics were suppressed by binding of a specific non-hydrolyzable ATP analog. Collectively, these observations show that during unwinding, RecBCD binds to DNA in a dynamic mode that is modulated by the nucleotide state of the ATP-binding pocket.
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