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Metamorphism of catalytic domain controls transposition in Tn3 family transposases
Open accessPreprint — published as 10.1038/s41467-022-33871-z · Paper page
Abstract
Transposons account for a remarkable diversity of mobile genetic elements that play the role of genome architects in all domains of life. Tn3 is a family of widespread and among first identified bacterial transposons notorious for their contribution to dissemination of antibiotic resistance. Transposition within this family is mediated by a large TnpA transposase facilitating both transposition and target immunity. The structural framework for understanding the mechanism of the TnpA transposition is however absent. Here, we describe the cryo-EM structures of TnpA from Tn4430 in apo form and paired with transposon ends. We show that TnpA has a unique architecture and exhibits a family-specific regulation mechanism involving metamorphic refolding of the RNase H-like catalytic domain. The TnpA structure, constrained by a double dimerization interface, creates a unique topology that suggests a specific role for target DNA in transpososome assembly, activation, and target immunity.
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Metadata
- Authors
- Shkumatov, A. V., Aryanpour, N., Oger, C. A., Goossens, G., Hallet, B. F., & Efremov, R. G.
- Affiliations
- Vrije Universiteit Brussel (BE)
- UCLouvain (BE)
- Corresponding author
- Hallet, Bernard F.
- Efremov, Rouslan G.
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2022-02-24
- Volume
- 13
- Issue
- 1
- Pages
- 6155-6155
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9579193
- OpenAlex
- W4306721683
- Cited by
- 34
- References
- 1
- Citations by year
- 2026: 13 · 2025: 11 · 2024: 3 · 2023: 6 · 2022: 1
- FWCI
- 3.32
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Digital Access to Libraries (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Université Catholique de Louvain
- Netherlands Centre for Electron Nanoscopy
- European Synchrotron Radiation Facility
- Universiteit Leiden
- Fonds Wetenschappelijk Onderzoek (G054617N, G0H5916N)
- Vlaams Instituut voor Biotechnologie
- Fonds Spéciaux de Recherche
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- Tn3 transposon, DNA strand transfer, DNA cleavage, transposon ends, dimer interface, antibiotic resistance dissemination, cryo-EM structure
- MeSH terms
- DNA Transposable Elements, Escherichia coli, Ribonuclease H, Transposases
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