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The Mu transpososome structure sheds light on DDE recombinase evolution
Open accessAbstract
Studies of bacteriophage Mu transposition paved the way for understanding retroviral integration and V(D)J recombination as well as many other DNA transposition reactions. Here we report the structure of the Mu transpososome--Mu transposase (MuA) in complex with bacteriophage DNA ends and target DNA--determined from data that extend anisotropically to 5.2 Å, 5.2 Å and 3.7 Å resolution, in conjunction with previously determined structures of individual domains. The highly intertwined structure illustrates why chemical activity depends on formation of the synaptic complex, and reveals that individual domains have different roles when bound to different sites. The structure also provides explanations for the increased stability of the final product complex and for its preferential recognition by the ATP-dependent unfoldase ClpX. Although MuA and many other recombinases share a structurally conserved 'DDE' catalytic domain, comparisons among the limited set of available complex structures indicate that some conserved features, such as catalysis in trans and target DNA bending, arose through convergent evolution because they are important for function.
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“Intasomes from several retroviral species as well as prokaryotic and eukaryotic transpososomes have been visualised as post-catalytic strand transfer complexes, all of which display sharp deformations of target DNA29,30,32,33,37,51–54.”
From Structure and function of retroviral integrase (2022) · cites this paper as [52]
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Metadata
- Authors
- Montaño, S. P., Pigli, Y. Z., & Rice, P. A.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Rice, Phoebe A.
- ORCID
- Rice, Phoebe A.
- Venue
- Nature
- Published
- 2012-11
- Volume
- 491
- Issue
- 7424
- Pages
- 413-417
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3536463
- OpenAlex
- W2034741116
- Cited by
- 137
- References
- 65
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 4 · 2023: 12 · 2022: 7 · 2021: 13 · 2020: 9 · 2019: 9 · 2018: 6 · 2017: 12 · 2016: 8 · 2015: 24 · 2014: 13 · 2013: 11 · 2012: 1
- FWCI
- 9.40
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- National Institute of General Medical Sciences (GM086826, R01GM086826)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- bacteriophage Mu, transpososome, DNA transposition, synaptic complex, transposon ends, target DNA, convergent evolution, protein-DNA complex structure
- MeSH terms
- DNA, Viral, Models, Molecular, Bacteriophage mu, Protein Binding, Protein Structure, Tertiary, Evolution, Molecular, Transposases, Recombinases
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