ArticleThe EMBO journal2021
Structures of ISCth4 transpososomes reveal the role of asymmetry in copy-out/paste-in DNA transposition.
Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Gamma-Mobile-Trio systems are mobile elements rich in bacterial defensive and offensive tools.Nature microbiology · 2024Article
- Local Genomic Surveillance of InvasiveInternational journal of molecular sciences · 2024Article
- A metagenomics pipeline reveals insertion sequence-driven evolution of the microbiota.Cell host & microbe · 2024Article
- A metagenomics pipeline reveals insertion sequence-driven evolution of the microbiota.bioRxiv : the preprint server for biology · 2024Article
- Transposition mechanism of ISAntimicrobial agents and chemotherapy · 2024Article
- Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.Nature communications · 2023Article
- Targeted IS-element sequencing uncovers transposition dynamics during selective pressure in enterococci.PLoS pathogens · 2023Article
- IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings.Nature communications · 2023Article
- A unique eukaryotic lineage of composite-like DNA transposons encoding a DDD/E transposase and a His-Me finger homing endonuclease.Mobile DNA · 2022Article
- Structural insight into Tn3 family transposition mechanism.Nature communications · 2022Article
- The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5'-transposon end.Molecular cell · 2021Article
- Structures of ISCth4 transpososomes reveal the role of asymmetry in copy-out/paste-in DNA transposition.The EMBO journal · 2021Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Copy-out/paste-in transposition is a major bacterial DNA mobility pathway. It contributes significantly to the emergence of antibiotic resistance, often by upregulating expression of downstream genes upon integration. Unlike other transposition pathways, it requires both asymmetric and symmetric strand transfer steps. Here, we report the first structural study of a copy-out/paste-in transposase and demonstrate its ability to catalyze all pathway steps in vitro. X-ray structures of ISCth4 transposase, a member of the IS256 family of insertion sequences, bound to DNA substrates corresponding to three sequential steps in the reaction reveal an unusual asymmetric dimeric transpososome. During transposition, an array of N-terminal domains binds a single transposon end while the catalytic domain moves to accommodate the varying substrates. These conformational changes control the path of DNA flanking the transposon end and the generation of DNA-binding sites. Our results explain the asymmetric outcome of the initial strand transfer and show how DNA binding is modulated by the asymmetric transposase to allow the capture of a second transposon end and to integrate a circular intermediate.
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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 Socratic graph.