ArticleBiophysical journal2021
Direct unfolding of RuvA-HJ complex at the single-molecule level.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 5 citations in OpenAlex.
- Measuring the biomechanical properties of cell-derived fibronectin fibrils.Biomechanics and modeling in mechanobiology · 2025Article
- Search and processing of Holliday junctions within long DNA by junction-resolving enzymes.Nature communications · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
The repair of double-stranded DNA breaks via homologous recombination involves a four-way cross-strand intermediate known as Holliday junction (HJ), which is recognized, processed, and resolved by a specific set of proteins. RuvA, a prokaryotic HJ-binding protein, is known to stabilize the square-planar conformation of the HJ, which is otherwise a short-lived intermediate. Despite much progress being made regarding the molecular mechanism of RuvA-HJ interactions, the mechanochemical aspect of this protein-HJ complex is yet to be investigated. Here, we employed an optical-tweezers-based, single-molecule manipulation assay to detect the formation of RuvA-HJ complex and determined its mechanical and thermodynamic properties in a manner that would be impossible with traditional ensemble techniques. We found that the binding of RuvA increases the unfolding force (F
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