ArticleProceedings of the National Academy of Sciences of the United States of America2012
Alteration of χ recognition by RecBCD reveals a regulated molecular latch and suggests a channel-bypass mechanism for biological control.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Trans-complementation by the RecB nuclease domain of RecBCD enzyme reveals new insight into RecA loading upon χ recognition.Nucleic acids research · 2024Article
- Article
- Insight into the biochemical mechanism of DNA helicases provided by bulk-phase and single-molecule assays.Methods (San Diego, Calif.) · 2022Review
- Bloom helicase mediates formation of large single-stranded DNA loops during DNA end processing.Nature communications · 2022Article
- Heterogeneity in E. coli RecBCD Helicase-DNA Binding and Base Pair Melting.Journal of molecular biology · 2021Article
- Homologous Recombination under the Single-Molecule Fluorescence Microscope.International journal of molecular sciences · 2019Review
- RecBCD Enzyme "Chi Recognition" Mutants Recognize Chi Recombination Hotspots in the Right DNA Context.Genetics · 2016Article
- Chi hotspots trigger a conformational change in the helicase-like domain of AddAB to activate homologous recombination.Nucleic acids research · 2016Article
- An Overview of the Molecular Mechanisms of Recombinational DNA Repair.Cold Spring Harbor perspectives in biology · 2015Review
- Control of RecBCD enzyme activity by DNA binding- and Chi hotspot-dependent conformational changes.Journal of molecular biology · 2014Article
- End resection at double-strand breaks: mechanism and regulation.Cold Spring Harbor perspectives in biology · 2014Review
- Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites.Nature · 2014Article
- Structural features of Chi recognition in AddAB with implications for RecBCD.Cell cycle (Georgetown, Tex.) · 2014Article
- On the mechanism of recombination hotspot scanning during double-stranded DNA break resection.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- End-resection at DNA double-strand breaks in the three domains of life.Biochemical Society transactions · 2013Review
- Bacterial DNA repair: recent insights into the mechanism of RecBCD, AddAB and AdnAB.Nature reviews. Microbiology · 2013Review
- Molecular determinants responsible for recognition of the single-stranded DNA regulatory sequence, χ, by RecBCD enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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6 authors.
Funding
Abstract
The RecBCD enzyme is a complex heterotrimeric helicase/nuclease that initiates recombination at double-stranded DNA breaks. In Escherichia coli, its activities are regulated by the octameric recombination hotspot, χ (5'-GCTGGTGG), which is read as a single-stranded DNA sequence while the enzyme is unwinding DNA at over ∼1,000 bp/s. Previous studies implicated the RecC subunit as the "χ-scanning element" in this process. Site-directed mutagenesis and phenotypic analyses identified residues in RecC responsible for χ recognition [Handa N, et al., (2012) Proc Natl Acad Sci USA, 10.1073/pnas.1206076109]. The genetic analyses revealed two classes of mutants. Here we use ensemble and single-molecule criteria to biochemically establish that one class of mutants (type 1) has lost the capacity to recognize χ (lost-recognition), whereas the second class (type 2) has a lowered specificity for recognition (relaxed-specificity). The relaxed-specificity mutants still recognize canonical χ, but they have gained the capacity to precociously recognize single-nucleotide variants of χ. Based on the RecBCD structure, these mutant classes define an α-helix responsible for χ recognition that is allosterically coupled to a structural latch. When opened, we propose that the latch permits access to an alternative exit channel for the single-stranded DNA downstream of χ, thereby avoiding degradation by the nuclease domain. These findings provide a unique perspective into the mechanism by which recognition of a single-stranded DNA sequence switches the translocating RecBCD from a destructive nuclease to a constructive component of recombinational DNA repair.
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