ArticleProtein science : a publication of the Protein Society2014
NMR structural analysis of Sleeping Beauty transposase binding to DNA.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Exploring transposable elements: new horizons in cancer diagnostics and therapeutics.Mobile DNA · 2025Review
- DNA binding and transposition activity of the Sleeping Beauty transposase: role of structural stability of the primary DNA-binding domain.Nucleic acids research · 2025Article
- A novel hyperactive variant of theMolecular therapy. Nucleic acids · 2024Article
- Contemporary Transposon Tools: A Review and Guide through Mechanisms and Applications ofInternational journal of molecular sciences · 2021Review
- Jumping Ahead withViruses · 2021Review
- NMR solution structure of the RED subdomain of the Sleeping Beauty transposase.Protein science : a publication of the Protein Society · 2017Article
- Regulated complex assembly safeguards the fidelity of Sleeping Beauty transposition.Nucleic acids research · 2017Article
- DNA Transposition at Work.Chemical reviews · 2016Review
- Structural Determinants of Sleeping Beauty Transposase Activity.Molecular therapy : the journal of the American Society of Gene Therapy · 2016Article
- Sleeping Beauty transposase structure allows rational design of hyperactive variants for genetic engineering.Nature communications · 2016Article
- Structural role of the flanking DNA in mariner transposon excision.Nucleic acids research · 2015Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The Sleeping Beauty (SB) transposon is the most widely used DNA transposon in genetic applications and is the only DNA transposon thus far in clinical trials for human gene therapy. In the absence of atomic level structural information, the development of SB transposon relied primarily on the biochemical and genetic homology data. While these studies were successful and have yielded hyperactive transposases, structural information is needed to gain a mechanistic understanding of transposase activity and guides to further improvement. We have initiated a structural study of SB transposase using Nuclear Magnetic Resonance (NMR) and Circular Dichroism (CD) spectroscopy to investigate the properties of the DNA-binding domain of SB transposase in solution. We show that at physiologic salt concentrations, the SB DNA-binding domain remains mostly unstructured but its N-terminal PAI subdomain forms a compact, three-helical structure with a helix-turn-helix motif at higher concentrations of NaCl. Furthermore, we show that the full-length SB DNA-binding domain associates differently with inner and outer binding sites of the transposon DNA. We also show that the PAI subdomain of SB DNA-binding domain has a dominant role in transposase's attachment to the inverted terminal repeats of the transposon DNA. Overall, our data validate several earlier predictions and provide new insights on how SB transposase recognizes transposon 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.