ArticleJournal of molecular biology2016
Processive DNA Unwinding by RecBCD Helicase in the Absence of Canonical Motor Translocation.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 15 citations in OpenAlex.
- The Nuclease Domain of E. coli RecBCD Helicase Regulates DNA Binding and Base Pair Melting.Journal of molecular biology · 2026Article
- Communication between DNA and nucleotide binding sites facilitates stepping by the RecBCD helicase.Nucleic acids research · 2024Article
- E. coli RecB Nuclease Domain Regulates RecBCD Helicase Activity but not Single Stranded DNA Translocase Activity.Journal of molecular biology · 2024Article
- Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.Journal of molecular biology · 2021Article
- Probing E. coli SSB protein-DNA topology by reversing DNA backbone polarity.Biophysical journal · 2021Article
- Article
- How Does a Helicase Unwind DNA? Insights from RecBCD Helicase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018Review
- Conformational selection and induced fit as a useful framework for molecular motor mechanisms.Biophysical chemistry · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Escherichia coli RecBCD is a DNA helicase/nuclease that functions in double-stranded DNA break repair. RecBCD possesses two motors (RecB, a 3' to 5' translocase, and RecD, a 5' to 3' translocase). Current DNA unwinding models propose that motor translocation is tightly coupled to base pair melting. However, some biochemical evidence suggests that DNA melting of multiple base pairs may occur separately from single-stranded DNA translocation. To test this hypothesis, we designed DNA substrates containing reverse backbone polarity linkages that prevent ssDNA translocation of the canonical RecB and RecD motors. Surprisingly, we find that RecBCD can processively unwind DNA for at least 80bp beyond the reverse polarity linkages. This ability requires an ATPase active RecB motor, the RecB "arm" domain, and also the RecB nuclease domain, but not its nuclease activity. These results indicate that RecBCD can unwind duplex DNA processively in the absence of ssDNA translocation by the canonical motors and that the nuclease domain regulates the helicase activity of RecBCD.
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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.