ArticleMolecular cell2024
Assembly of the Tn7 targeting complex by a regulated stepwise process.
Article in Molecular cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Transposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.Nature communications · 2026Article
- Structure of the Type I-F3 CAST holo integration complex reveals licensing mechanisms during RNA-guided DNA integration.bioRxiv : the preprint server for biology · 2026Article
- DNA remodeling couples target recognition to directional transposition in a Tn7-like CAST.bioRxiv : the preprint server for biology · 2026Article
- Escherichia coli proteins uL29 and ACP stabilize the Tn7-encoded TnsD and its DNA binding.Mobile DNA · 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
- Structural basis of TnsC oligomerization and transposase recruitment in type I-B CRISPR-associated transposons.Nucleic acids research · 2025Article
- Controlling and controlled elements: highlights of the year in mobile DNA research.Mobile DNA · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The Tn7 family of transposons is notable for its highly regulated integration mechanisms, including programmable RNA-guided transposition. The targeting pathways rely on dedicated target selection proteins from the TniQ family and the AAA+ adaptor TnsC to recruit and activate the transposase at specific target sites. Here, we report the cryoelectron microscopy (cryo-EM) structures of TnsC bound to the TniQ domain of TnsD from prototypical Tn7 and unveil key regulatory steps stemming from unique behaviors of ATP- versus ADP-bound TnsC. We show that TnsD recruits ADP-bound dimers of TnsC and acts as an exchange factor to release one protomer with exchange to ATP. This loading process explains how TnsC assembles a heptameric ring unidirectionally from the target site. This unique loading process results in functionally distinct TnsC protomers within the ring, providing a checkpoint for target immunity and explaining how insertions at programmed sites precisely occur in a specific orientation across Tn7 elements.
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Registered trials
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.