ArticleMolecular cell2022
Structural basis of transposon end recognition explains central features of Tn7 transposition systems.
Article in Molecular cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 30 citations in OpenAlex.
- Transposon end recognition and pairing by I-F3 CRISPR-associated transposase.Science advances · 2026Article
- Transposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.Nature communications · 2026Article
- A functional atlas of transposon-encoded products and their integration into host networks.Nature communications · 2026Article
- DNA remodeling couples target recognition to directional transposition in a Tn7-like CAST.bioRxiv : the preprint server for biology · 2026Article
- Asymmetric loading of TnsE regulates Tn7 targeting of DNA replication structures.Nucleic acids research · 2025Article
- A family of Tn7-like transposons evolved to target CRISPR repeats.Mobile DNA · 2025Article
- Emerging trends in genome integration tools for precision engineering of diverse bacterial species.Synthetic biology (Oxford, England) · 2025Review
- Article
- Natural and Engineered Guide RNA-Directed Transposition with CRISPR-Associated Tn7-Like Transposons.Annual review of biochemistry · 2024Review
- Assembly of the Tn7 targeting complex by a regulated stepwise process.Molecular cell · 2024Article
- Activity of zebrafish THAP9 transposase and zebrafish P element-like transposons.bioRxiv : the preprint server for biology · 2024Article
- Genome Engineering by RNA-Guided Transposition forACS synthetic biology · 2024Article
- Transposons and CRISPR: Rewiring Gene Editing.Biochemistry · 2023Article
- CRISPR-based gene editing technology and its application in microbial engineering.Engineering microbiology · 2023Review
- Novel molecular requirements for CRISPR RNA-guided transposition.Nucleic acids research · 2023Article
- IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings.Nature communications · 2023Article
- Insertion sequences related to ISAjo2 target pMicrobial genomics · 2023Article
- Distribution, characterization, and evolution of heavy metal resistance genes and Tn7-like associated heavy metal resistance Gene Island ofFrontiers in microbiology · 2023Article
- Article
- Transposase N-terminal phosphorylation and asymmetric transposon ends inhibit piggyBac transposition in mammalian cells.Nucleic acids research · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Tn7 is a bacterial transposon with relatives containing element-encoded CRISPR-Cas systems mediating RNA-guided transposon insertion. Here, we present the 2.7 Å cryoelectron microscopy structure of prototypic Tn7 transposase TnsB interacting with the transposon end DNA. When TnsB interacts across repeating binding sites, it adopts a beads-on-a-string architecture, where the DNA-binding and catalytic domains are arranged in a tiled and intertwined fashion. The DNA-binding domains form few base-specific contacts leading to a binding preference that requires multiple weakly conserved sites at the appropriate spacing to achieve DNA sequence specificity. TnsB binding imparts differences in the global structure of the protein-bound DNA ends dictated by the spacing or overlap of binding sites explaining functional differences in the left and right ends of the element. We propose a model of the strand-transfer complex in which the terminal TnsB molecule is rearranged so that its catalytic domain is in a position conducive to transposition.
Indexed as
Identifiers
What OpenQuestion holds
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.