ArticleJournal of molecular biology2014
Control of RecBCD enzyme activity by DNA binding- and Chi hotspot-dependent conformational changes.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- The RecBCD complex interacts directly with the DNA sliding clamp in Escherichia coli.Nucleic acids research · 2026Article
- Chi hotspot control of RecBCD enzyme requires a RecB tether-RecC groove crosspoint interaction.Genetics · 2026Article
- The Nuclease Domain of E. coli RecBCD Helicase Regulates DNA Binding and Base Pair Melting.Journal of molecular biology · 2026Article
- Article
- Chi hotspot Control of RecBCD Helicase-nuclease: Enzymatic Tests Support the Intramolecular Signal-transduction Model.Journal of molecular biology · 2024Article
- RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023Review
- Article
- Single-molecule studies of helicases and translocases in prokaryotic genome-maintenance pathways.DNA repair · 2021Review
- Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.Journal of molecular biology · 2021Article
- Chi hotspot control of RecBCD helicase-nuclease by long-range intramolecular signaling.Scientific reports · 2020Article
- Small-molecule sensitization of RecBCD helicase-nuclease to a Chi hotspot-activated state.Nucleic acids research · 2020Article
- The Roles of Bacterial DNA Double-Strand Break Repair Proteins in Chromosomal DNA Replication.FEMS microbiology reviews · 2020Review
- The positioning of Chi sites allows the RecBCD pathway to suppress some genomic rearrangements.Nucleic acids research · 2019Article
- The RecB helicase-nuclease tether mediates Chi hotspot control of RecBCD enzyme.Nucleic acids research · 2019Article
- Article
- Physical basis for long-distance communication along meiotic chromosomes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- How Does a Helicase Unwind DNA? Insights from RecBCD Helicase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018Review
- ATP hydrolysis provides functions that promote rejection of pairings between different copies of long repeated sequences.Nucleic acids research · 2017Article
- A non-catalytic role of RecBCD in homology directed gap repair and translesion synthesis.Nucleic acids research · 2017Article
- Global analysis of double-strand break processing reveals in vivo properties of the helicase-nuclease complex AddAB.PLoS genetics · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Faithful repair of DNA double-strand breaks by homologous recombination is crucial to maintain functional genomes. The major Escherichia coli pathway of DNA break repair requires RecBCD enzyme, a complex protein machine with multiple activities. Upon encountering a Chi recombination hotspot (5' GCTGGTGG 3') during DNA unwinding, RecBCD's unwinding, nuclease, and RecA-loading activities change dramatically, but the physical basis for these changes is unknown. Here, we identify, during RecBCD's DNA unwinding, two Chi-stimulated conformational changes involving RecC. One produced a marked, long-lasting, Chi-dependent increase in protease sensitivity of a small patch, near the Chi recognition domain, on the solvent-exposed RecC surface. The other change was identified by crosslinking of an artificial amino acid inserted in this RecC patch to RecB. Small-angle X-ray scattering analysis confirmed a major conformational change upon binding of DNA to the enzyme and is consistent with these two changes. We propose that, upon DNA binding, the RecB nuclease domain swings from one side of RecC to the other; when RecBCD encounters Chi, the nuclease domain returns to its initial position determined by crystallography, where it nicks DNA exiting from RecC and loads RecA onto the newly generated 3'-ended single-stranded DNA during continued unwinding; a crevice between RecB and RecC increasingly narrows during these steps. This model provides a physical basis for the intramolecular "signal transduction" from Chi to RecC to RecD to RecB inferred previously from genetic and enzymatic analyses, and it accounts for the enzymatic changes that accompany Chi's stimulation of recombination.
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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.