ArticleNucleic acids research2023
AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements.
Article in Nucleic acids research, 2023. 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, 7 citations in OpenAlex.
- Insights into the recruitment of the H3K4me3 reader Spp1 by the meiotic double-strand break protein Mer2.Nucleic acids research · 2026Article
- Ulva fasciata litter decomposition fuels microbial restructuring and antibiotic resistance proliferation in mariculture sediment.Antonie van Leeuwenhoek · 2026Article
- Review
- Quantifying complexity in DNA structures with high resolution Atomic Force Microscopy.Nature communications · 2025Article
- Metagenomic Insights into the Diverse Antibiotic Resistome of Non-Migratory Corvidae Species on the Qinghai-Tibetan Plateau.Veterinary sciences · 2025Article
- Probing living cell dynamics and molecular interactions using atomic force microscopy.Biophysical reviews · 2024Review
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
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Abstract
Transposon Tn4430 belongs to a widespread family of bacterial transposons, the Tn3 family, which plays a prevalent role in the dissemination of antibiotic resistance among pathogens. Despite recent data on the structural architecture of the transposition complex, the molecular mechanisms underlying the replicative transposition of these elements are still poorly understood. Here, we use force-distance curve-based atomic force microscopy to probe the binding of the TnpA transposase of Tn4430 to DNA molecules containing one or two transposon ends and to extract the thermodynamic and kinetic parameters of transposition complex assembly. Comparing wild-type TnpA with previously isolated deregulated TnpA mutants supports a stepwise pathway for transposition complex formation and activation during which TnpA first binds as a dimer to a single transposon end and then undergoes a structural transition that enables it to bind the second end cooperatively and to become activated for transposition catalysis, the latter step occurring at a much faster rate for the TnpA mutants. Our study thus provides an unprecedented approach to probe the dynamic of a complex DNA processing machinery at the single-particle level.
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