ArticleNature structural & molecular biology2022
Structural basis for DNA targeting by the Tn7 transposon.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 52 citations in OpenAlex.
- Transposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.Nature communications · 2026Article
- DNA remodeling couples target recognition to directional transposition in a Tn7-like CAST.bioRxiv : the preprint server for biology · 2026Article
- Structural basis of RNA-guided DNA integration by type I CRISPR-associated transposases.bioRxiv : the preprint server for biology · 2026Article
- Comparative structural analysis of IS21 transposition complexes using Cryo-EM and AlphaFold3.Mobile DNA · 2025Article
- Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding.Mobile DNA · 2025Article
- Type I-F CRISPR-associated transposons contribute to genomic plasticity inMicrobial genomics · 2025Article
- Graph Attention Neural Networks Reveal TnsC Filament Assembly in a CRISPR-Associated Transposon.bioRxiv : the preprint server for biology · 2025Article
- Insights on the regulation and function of the CRISPR/Cas transposition system located in the pathogenicity island VpaI-7 fromInfection and immunity · 2025Article
- Asymmetric loading of TnsE regulates Tn7 targeting of DNA replication structures.Nucleic acids research · 2025Article
- Telomeric transposons are pervasive in linear bacterial genomes.Science (New York, N.Y.) · 2025Article
- Overview and Prospects of DNA Sequence Visualization.International journal of molecular sciences · 2025Review
- Emerging trends in genome integration tools for precision engineering of diverse bacterial species.Synthetic biology (Oxford, England) · 2025Review
- Article
- Distinct horizontal transfer mechanisms for type I and type V CRISPR-associated transposons.Nature communications · 2024Article
- Natural and Engineered Guide RNA-Directed Transposition with CRISPR-Associated Tn7-Like Transposons.Annual review of biochemistry · 2024Review
- Elucidating the Architectural dynamics of MuB filaments in bacteriophage Mu DNA transposition.Nature communications · 2024Article
- Assembly of the Tn7 targeting complex by a regulated stepwise process.Molecular cell · 2024Article
- Article
- Novel mechanisms of diversity generation in Acinetobacter baumannii resistance islands driven by Tn7-like elements.Nucleic acids research · 2024Article
- Annotation and Comparative Genomics of Prokaryotic Transposable Elements.Methods in molecular biology (Clifton, N.J.) · 2024Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Tn7 transposable elements are unique for their highly specific, and sometimes programmable, target-site selection mechanisms and precise insertions. All the elements in the Tn7 family utilize an AAA+ adaptor (TnsC) to coordinate target-site selection with transpososome assembly and to prevent insertions at sites already containing a Tn7 element. Owing to its multiple functions, TnsC is considered the linchpin in the Tn7 element. Here we present the high-resolution cryo-EM structure of TnsC bound to DNA using a gain-of-function variant of the protein and a DNA substrate that together recapitulate the recruitment to a specific DNA target site. TnsC forms an asymmetric ring on target DNA that segregates target-site selection and interaction with the paired-end complex to opposite faces of the ring. Unlike most AAA+ ATPases, TnsC uses a DNA distortion to find the target site but does not remodel DNA to activate transposition. By recognizing pre-distorted substrates, TnsC creates a built-in regulatory mechanism where ATP hydrolysis abolishes ring formation proximal to an existing element. This work unveils how Tn7 and Tn7-like elements determine the strict spacing between the target and integration sites.
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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.