ArticleScientific reports2017
Probing the mechanical stability of bridged DNA-H-NS protein complexes by single-molecule AFM pulling.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Biofunctionalized polymer semiconductors toward soft and stretchable transistor-based biosensors.Science advances · 2026Article
- Deciphering Sequence-Specific DNA Binding by H-NS Using Molecular Simulation.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Quantitative characterization of cell physiological state based on dynamical cell mechanics for drug efficacy indication.Journal of pharmaceutical analysis · 2023Article
- Extracting and characterizing protein-free megabase-pair DNA forCell reports methods · 2022Article
- Molecular Basis for Environment Sensing by a Nucleoid-Structuring Bacterial Protein Filament.The journal of physical chemistry letters · 2021Article
- Organization of DNA in Mammalian Mitochondria.International journal of molecular sciences · 2019Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Atomic force microscopy (AFM) has proven to be a powerful tool for the study of DNA-protein interactions due to its ability to image single molecules at the nanoscale. However, the use of AFM in force spectroscopy to study DNA-protein interactions has been limited. Here we developed a high throughput, AFM based, pulling assay to measure the strength and kinetics of protein bridging of DNA molecules. As a model system, we investigated the interactions between DNA and the Histone-like Nucleoid-Structuring protein (H-NS). We confirmed that H-NS both changes DNA rigidity and forms bridges between DNA molecules. This straightforward methodology provides a high-throughput approach with single-molecule resolution which is widely applicable to study cross-substrate interactions such as DNA-bridging proteins.
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