The Mu transpososome structure sheds light on DDE recombinase evolution

Montaño, Sherwin P.; Pigli, Ying Z.; Rice, Phoebe A.

doi:10.1038/nature11602

Cited by 138Bacterial Genetics and BiotechnologyDNA Repair MechanismsEnzyme Structure and Function

The Mu transpososome structure sheds light on DDE recombinase evolution

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Montaño, Sherwin P., Pigli, Ying Z., Rice, Phoebe A.·2012·Nature

DOI 10.1038/nature11602PMC PMC3536463

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Abstract

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 and prokaryotic and eukaryotic transpososomes have been visualized as post-catalytic strand transfer complexes, all showing sharp deformations of target DNA.
“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]
The Methods (Overview; page not specified) describe a final strand-transfer complex of Mu, and Overall Architecture (Target DNA; page not specified) reports that its target DNA bends by about 140°. Convergent and divergent evolution also describes bent target DNA in the PFV intasome, but says Mos1 was crystallized without target DNA and bending in Tn5 was inferred by modeling. The paper therefore does not support the claim that all the complexes mentioned were visualized as post-catalytic complexes displaying sharply deformed target DNA, or its reference to several retroviral species. (LLM, conf=0.88)
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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
Publisher: Springer Science and Business Media LLC
Published: 2012-11
Volume: 491
Issue: 7424
Pages: 413-417
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature11602
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
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
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
Physical Sciences › Materials Science › Materials Chemistry › 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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The Mu transpososome structure sheds light on DDE recombinase evolution

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