ArticleNature2012
The μ transpososome structure sheds light on DDE recombinase evolution.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 141 citations in OpenAlex.
- Transposon end recognition and pairing by I-F3 CRISPR-associated transposase.Science advances · 2026Article
- Core nucleosomes are refractory to lentiviral DNA integration.Nature communications · 2026Article
- Structure-based recasting of a mammalian DNA transpososome as an obligate heterodimer.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
- 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
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- Activity of the mammalian DNA transposon piggyBat from Myotis lucifugus is restricted by its own transposon ends.Nature communications · 2025Article
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- Natural and Engineered Guide RNA-Directed Transposition with CRISPR-Associated Tn7-Like Transposons.Annual review of biochemistry · 2024Review
- Article
- Structure reveals why genome folding is necessary for site-specific integration of foreign DNA into CRISPR arrays.Nature structural & molecular biology · 2023Article
- Article
- Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.Nature communications · 2023Article
- 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
- Non-specific and specific DNA binding modes of bacterial histone, HU, separately regulate distinct physiological processes through different mechanisms.Molecular microbiology · 2023Article
- Insertion sequences related to ISAjo2 target pMicrobial genomics · 2023Article
- Tn5 DNA Transposase in Multi-Omics Research.Methods and protocols · 2023Review
- Article
39 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Studies of bacteriophage Mu transposition paved the way for understanding retroviral integration and V(D)J recombination as well as many other DNA transposition reactions. Here we report the structure of the Mu transpososome--Mu transposase (MuA) in complex with bacteriophage DNA ends and target DNA--determined from data that extend anisotropically to 5.2 Å, 5.2 Å and 3.7 Å resolution, in conjunction with previously determined structures of individual domains. The highly intertwined structure illustrates why chemical activity depends on formation of the synaptic complex, and reveals that individual domains have different roles when bound to different sites. The structure also provides explanations for the increased stability of the final product complex and for its preferential recognition by the ATP-dependent unfoldase ClpX. Although MuA and many other recombinases share a structurally conserved 'DDE' catalytic domain, comparisons among the limited set of available complex structures indicate that some conserved features, such as catalysis in trans and target DNA bending, arose through convergent evolution because they are important for function.
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