ArticleNucleic acids research2021
Single bacterial resolvases first exploit, then constrain intrinsic dynamics of the Holliday junction to direct recombination.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Real-time visualization of spatial and temporal coordination in resolvase-mediated Holliday junction binding.iScience · 2026Article
- Integration Host Factor Binds DNA Holliday Junctions.International journal of molecular sciences · 2022Article
- Single-Molecule FRET: A Tool to Characterize DNA Nanostructures.Frontiers in molecular biosciences · 2022Review
- Editorial: Single-molecule studies of DNA-protein interactions collection 2021.Nucleic acids research · 2021Article
- Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules.Micromachines · 2021Review
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3 authors.
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Abstract
Homologous recombination forms and resolves an entangled DNA Holliday Junction (HJ) crucial for achieving genetic reshuffling and genome repair. To maintain genomic integrity, specialized resolvase enzymes cleave the entangled DNA into two discrete DNA molecules. However, it is unclear how two similar stacking isomers are distinguished, and how a cognate sequence is found and recognized to achieve accurate recombination. We here use single-molecule fluorescence observation and cluster analysis to examine how prototypic bacterial resolvase RuvC singles out two of the four HJ strands and achieves sequence-specific cleavage. We find that RuvC first exploits, then constrains the dynamics of intrinsic HJ isomer exchange at a sampled branch position to direct cleavage toward the catalytically competent HJ conformation and sequence, thus controlling recombination output at minimal energetic cost. Our model of rapid DNA scanning followed by 'snap-locking' of a cognate sequence is strikingly consistent with the conformational proofreading of other DNA-modifying enzymes.
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