ArticleNature communications2023
Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Structure-based recasting of a mammalian DNA transpososome as an obligate heterodimer.bioRxiv : the preprint server for biology · 2026Article
- Beyond DNA binding: single C2H2 zinc fingers with adjacent β-strands mediate dimerization in Drosophila transcription factors.Nucleic acids research · 2026Article
- Genome-wide identification and characterization of theFrontiers in plant science · 2026Article
- Activity of the mammalian DNA transposon piggyBat from Myotis lucifugus is restricted by its own transposon ends.Nature communications · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end.
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