ArticleNature communications2019
RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Target RNA-triggered CRISPR-Cas12a2 preferentially cleaves collateral DNA over RNA.Nucleic acids research · 2026Article
- Target RNA-triggered CRISPR-Cas12a2 Preferentially Cleaves Collateral DNA over RNA.bioRxiv : the preprint server for biology · 2026Article
- Real-time visualization of spatial and temporal coordination in resolvase-mediated Holliday junction binding.iScience · 2026Article
- Chloroplast-to-apoplast relocalization of MOC1 strengthens plant vascular immunity.Horticulture research · 2026Article
- Genome-wide screen reveals a universal role of ATP in ciprofloxacin tolerance among genetically distinctmLife · 2026Article
- DNA 'Breathing' Recombination Cloning: A Mismatch-Tolerant, Temperature-Dependent Homologous Recombination Cloning Method.International journal of molecular sciences · 2026Article
- Degradation and stable maintenance of adeno-associated virus inverted terminal repeats in E. coli.Nucleic acids research · 2025Article
- Holliday junction resolvase RuvC targets biofilm eDNA and confers plant resistance to vascular pathogens.Nature plants · 2024Article
- Review
- Vector enabled CRISPR gene editing - A revolutionary strategy for targeting the diversity of brain pathologies.Coordination chemistry reviews · 2023Article
- Atomistic Picture of Opening-Closing Dynamics of DNA Holliday Junction Obtained by Molecular Simulations.Journal of chemical information and modeling · 2023Article
- Quinolone Antibiotics: Resistance and Therapy.Infection and drug resistance · 2023Review
- Article
- Interrogating the substrate specificity landscape of UvrC reveals novel insights into its non-canonical function.Biophysical journal · 2022Article
- Transcriptomics and Functional Analysis of Copper Stress Response in the Sulfate-Reducing BacteriumInternational journal of molecular sciences · 2022Article
- Kinetic analysis of Cas12a and Cas13a RNA-Guided nucleases for development of improved CRISPR-Based diagnostics.iScience · 2021Article
- Single bacterial resolvases first exploit, then constrain intrinsic dynamics of the Holliday junction to direct recombination.Nucleic acids research · 2021Article
- Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1.Nature communications · 2020Article
- MD simulations reveal the basis for dynamic assembly of Hfq-RNA complexes.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Holliday junctions (HJs) are four-way DNA structures that occur in DNA repair by homologous recombination. Specialized nucleases, termed resolvases, remove (i.e., resolve) HJs. The bacterial protein RuvC is a canonical resolvase that introduces two symmetric cuts into the HJ. For complete resolution of the HJ, the two cuts need to be tightly coordinated. They are also specific for cognate DNA sequences. Using a combination of structural biology, biochemistry, and a computational approach, here we show that correct positioning of the substrate for cleavage requires conformational changes within the bound DNA. These changes involve rare high-energy states with protein-assisted base flipping that are readily accessible for the cognate DNA sequence but not for non-cognate sequences. These conformational changes and the relief of protein-induced structural tension of the DNA facilitate coordination between the two cuts. The unique DNA cleavage mechanism of RuvC demonstrates the importance of high-energy conformational states in nucleic acid readouts.
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