ArticleNucleic acids research2013
Structural asymmetry in the Thermus thermophilus RuvC dimer suggests a basis for sequential strand cleavages during Holliday junction resolution.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Real-time visualization of spatial and temporal coordination in resolvase-mediated Holliday junction binding.iScience · 2026Article
- MOC1 cleaves Holliday junctions through a cooperative nick and counter-nick mechanism mediated by metal ions.Nature communications · 2024Article
- Differential requirement for RecFOR pathway components in Thermus thermophilus.Environmental microbiology reports · 2024Article
- Review
- Article
- Structural and Functional Characterization of the Holliday Junction Resolvase RuvC fromMicroorganisms · 2022Article
- Profiles of Natural and Designed Protein-Like Sequences Effectively Bridge Protein Sequence Gaps: Implications in Distant Homology Detection.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Single-molecule insight into stalled replication fork rescue in Escherichia coli.Nucleic acids research · 2021Review
- Single bacterial resolvases first exploit, then constrain intrinsic dynamics of the Holliday junction to direct recombination.Nucleic acids research · 2021Article
- Active-Site Models ofFrontiers in molecular biosciences · 2021Article
- Structural insights into sequence-dependent Holliday junction resolution by the chloroplast resolvase MOC1.Nature communications · 2020Article
- Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase.Scientific reports · 2020Article
- Structural basis of sequence-specific Holliday junction cleavage by MOC1.Nature chemical biology · 2019Article
- DNA Unwinding Is the Primary Determinant of CRISPR-Cas9 Activity.Cell reports · 2018Article
- Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.Nucleic acids research · 2017Article
- Structural insights into dynamics of RecU-HJ complex formation elucidates key role of NTR and stalk region toward formation of reactive state.Nucleic acids research · 2017Article
- Resolution of single and double Holliday junction recombination intermediates by GEN1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure and Metal Binding Properties of a Poxvirus Resolvase.The Journal of biological chemistry · 2016Article
- Holliday junction resolvases.Cold Spring Harbor perspectives in biology · 2014Review
- Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Holliday junction (HJ) resolvases are structure-specific endonucleases that cleave four-way DNA junctions (HJs) generated during DNA recombination and repair. Bacterial RuvC, a prototypical HJ resolvase, functions as homodimer and nicks DNA strands precisely across the junction point. To gain insights into the mechanisms underlying symmetrical strand cleavages by RuvC, we performed crystallographic and biochemical analyses of RuvC from Thermus thermophilus (T.th. RuvC). The crystal structure of T.th. RuvC shows an overall protein fold similar to that of Escherichia coli RuvC, but T.th. RuvC has a more tightly associated dimer interface possibly reflecting its thermostability. The binding mode of a HJ-DNA substrate can be inferred from the shape/charge complementarity between the T.th. RuvC dimer and HJ-DNA, as well as positions of sulfate ions bound on the protein surface. Unexpectedly, the structure of T.th. RuvC homodimer refined at 1.28 Å resolution shows distinct asymmetry near the dimer interface, in the region harboring catalytically important aromatic residues. The observation suggests that the T.th. RuvC homodimer interconverts between two asymmetric conformations, with alternating subunits switched on for DNA strand cleavage. This model provides a structural basis for the 'nick-counter-nick' mechanism in HJ resolution, a mode of HJ processing shared by prokaryotic and eukaryotic HJ resolvases.
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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.