ArticleNucleic acids research2019
The RecB helicase-nuclease tether mediates Chi hotspot control of RecBCD enzyme.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Chi hotspot control of RecBCD enzyme requires a RecB tether-RecC groove crosspoint interaction.Genetics · 2026Article
- Article
- Cyanobacterial Argonautes and Cas4 family nucleases cooperate to interfere with invading DNA.Molecular cell · 2025Article
- Functional insights into Solo-Cas4 inmicroLife · 2025Article
- Trans-complementation by the RecB nuclease domain of RecBCD enzyme reveals new insight into RecA loading upon χ recognition.Nucleic acids research · 2024Article
- Chi hotspot Control of RecBCD Helicase-nuclease: Enzymatic Tests Support the Intramolecular Signal-transduction Model.Journal of molecular biology · 2024Article
- E. coli RecB Nuclease Domain Regulates RecBCD Helicase Activity but not Single Stranded DNA Translocase Activity.Journal of molecular biology · 2024Article
- RecBCD enzyme: mechanistic insights from mutants of a complex helicase-nuclease.Microbiology and molecular biology reviews : MMBR · 2023Review
- Article
- RecA and RecB: probing complexes of DNA repair proteins with mitomycin C in liveJournal of the Royal Society, Interface · 2022Article
- 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
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
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Authors and funding
2 authors.
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Abstract
In bacteria, repair of DNA double-strand breaks uses a highly conserved helicase-nuclease complex to unwind DNA from a broken end and cut it at specific DNA sequences called Chi. In Escherichia coli the RecBCD enzyme also loads the DNA strand-exchange protein RecA onto the newly formed end, resulting in a recombination hotspot at Chi. Chi hotspots regulate multiple RecBCD activities by altering RecBCD's conformation, which is proposed to include the swinging of the RecB nuclease domain on the 19-amino-acid tether connecting the helicase and nuclease domains. Here, we altered the tether and tested multiple RecBCD activities, genetically in cells and enzymatically in cell-free extracts. Randomizing the amino-acid sequence or lengthening it had little effect. However, shortening it by as little as two residues or making substitutions of ≥10 proline or ≥9 glycine residues dramatically lowered Chi-dependent activities. These results indicate that proper control of RecBCD by Chi requires that the tether be long enough and appropriately flexible. We discuss a model in which the swing-time of the nuclease domain determines the position of Chi-dependent and Chi-independent cuts and Chi hotspot activity.
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