ArticleCell2014
Structural basis of hAT transposon end recognition by Hermes, an octameric DNA transposase from Musca domestica.
Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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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.
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Who cites it
48 citing papers in PubMed, 74 citations in OpenAlex.
- Characterization of hAT DNA transposon superfamily in the genome of Neotropical fish Apareiodon sp.Molecular genetics and genomics : MGG · 2024Article
- Article
- Multiple horizontal transfer events of a DNA transposon into turtles, fishes, and a frog.Mobile DNA · 2024Article
- Independent evolution of transposase and TIRs facilitated by recombination betweenProceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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
- Structural basis of transposon end recognition explains central features of Tn7 transposition systems.Molecular cell · 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
- Diverse Eukaryotic CGG-Binding Proteins Produced by Independent Domestications of hAT Transposons.Molecular biology and evolution · 2021Article
- APOBEC1 cytosine deaminase activity on single-stranded DNA is suppressed by replication protein A.Nucleic acids research · 2021Article
- Structures of ISCth4 transpososomes reveal the role of asymmetry in copy-out/paste-in DNA transposition.The EMBO journal · 2021Article
- Insertion Specificity of the hATx-6 Transposase ofFrontiers in molecular biosciences · 2021Article
- Structural basis of seamless excision and specific targeting by piggyBac transposase.Nature communications · 2020Article
- Cutting antiparallel DNA strands in a single active site.Nature structural & molecular biology · 2020Article
- Jump ahead with a twist: DNA acrobatics drive transposition forward.Current opinion in structural biology · 2019Review
- Article
- Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts.Nature structural & molecular biology · 2019Article
- Review
- Structural gymnastics of RAG-mediated DNA cleavage in V(D)J recombination.Current opinion in structural biology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 1 country.
Funding
Abstract
Hermes is a member of the hAT transposon superfamily that has active representatives, including McClintock's archetypal Ac mobile genetic element, in many eukaryotic species. The crystal structure of the Hermes transposase-DNA complex reveals that Hermes forms an octameric ring organized as a tetramer of dimers. Although isolated dimers are active in vitro for all the chemical steps of transposition, only octamers are active in vivo. The octamer can provide not only multiple specific DNA-binding domains to recognize repeated subterminal sequences within the transposon ends, which are important for activity, but also multiple nonspecific DNA binding surfaces for target capture. The unusual assembly explains the basis of bipartite DNA recognition at hAT transposon ends, provides a rationale for transposon end asymmetry, and suggests how the avidity provided by multiple sites of interaction could allow a transposase to locate its transposon ends amidst a sea of chromosomal DNA.
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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.