The DOI matches its Crossref record; 38 of the 39 references it cites were found in a registry or an index.
Molecular Architecture of the Mos1 Paired-End Complex: The Structural Basis of DNA Transposition in a Eukaryote
Open accessAbstract
A key step in cut-and-paste DNA transposition is the pairing of transposon ends before the element is excised and inserted at a new site in its host genome. Crystallographic analyses of the paired-end complex (PEC) formed from precleaved transposon ends and the transposase of the eukaryotic element Mos1 reveals two parallel ends bound to a dimeric enzyme. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Two additional DNA duplexes in the crystal indicate likely binding sites for flanking DNA. Biochemical data provide support for a model of the target capture complex and identify Arg186 to be critical for target binding. Mixing experiments indicate that a transposase dimer initiates first-strand cleavage and suggest a pathway for PEC formation.
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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 [51]
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Citations
Cites
Transposable elements and the epigenetic regulation of the genome
Slotkin, R. K., & Martienssen, R. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2072 · Cited by 2,044
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Junk DNA as an evolutionary force
Biémont, C., & Vieira, C. P. (2006) · Nature · doi:10.1038/443521a · Cited by 736
Making and Breaking Nucleic Acids: Two-Mg2+-Ion Catalysis and Substrate Specificity
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RAG1 Core and V(D)J Recombination Signal Sequences Were Derived from Transib Transposons
Kapitonov, V. V., & Jurka, J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030181 · Cited by 521
Mammalian mutagenesis using a highly mobile somatic Sleeping Beauty transposon system
Dupuy, A. J., Akagi, K., Largaespada, D. A., Copeland, N. G., & Jenkins, N. A. (2005) · Nature · doi:10.1038/nature03691 · Cited by 482
Resident aliens: the Tc1/ mariner superfamily of transposable elements
Plasterk, R. H. A., Izsvák, Z., & Ivics, Z. (1999) · Trends in Genetics · doi:10.1016/s0168-9525(99)01777-1 · Cited by 472
A purified mariner transposase is sufficient to mediate transposition in vitro.
Lampe, D. J., Churchill, M. E. A., & Robertson, H. M. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00930.x · Cited by 457
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Sorted by citations
Bacterial insertion sequences: their genomic impact and diversity
Siguier, P., Gourbeyre, E., & Chandler, M. (2014) · FEMS Microbiology Reviews · doi:10.1111/1574-6976.12067 · Cited by 773
“Other ISs such as the IS630 family, related to the eukaryote mariner/Tc superfamily, employ a mechanism in which the initial H2O-catalysed cleavage of the nontransferred strand occurs with a small offset of 2 bases into the IS prior to cleavage of the transferred strand (Feng & Colloms, 2007) as do their eukaryotic co…”
BackgroundNucleases: diversity of structure, function and mechanism
Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692
Retroviral intasome assembly and inhibition of DNA strand transfer
Hare, S., Gupta, S. S., Valkov, E., Engelman, A., & Cherepanov, P. (2010) · Nature · doi:10.1038/nature08784 · Cited by 678
Craigie, R., & Bushman, F. D. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006890 · Cited by 327
“The intertwined nature of protein–protein and protein–DNA contacts is reminiscent of the structures of Tn5 and Mos1 transpososomes (Davies et al. 2000; Richardson et al. 2009).”
BackgroundThe mechanism of retroviral integration from X-ray structures of its key intermediates
Maertens, G. N., Hare, S., & Cherepanov, P. (2010) · Nature · doi:10.1038/nature09517 · Cited by 296
“The reservoir contained 20% (6)-2-methyl-2,4-pentanediol (MPD), 40 mM MgCl2 and 50 mM sodium cacodylate, pH 5.”
Background
Metadata
- Authors
- Richardson, J. M., Colloms, S. D., Finnegan, D. J., & Walkinshaw, M. D.
- Affiliations
- University of Edinburgh (GB)
- Corresponding author
- Richardson, Julia M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-09
- Volume
- 138
- Issue
- 6
- Pages
- 1096-1108
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3977044
- OpenAlex
- W2026862785
- Cited by
- 145
- References
- 39
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 5 · 2023: 7 · 2022: 4 · 2021: 7 · 2020: 6 · 2019: 6 · 2018: 7 · 2017: 8 · 2016: 10 · 2015: 17 · 2014: 14 · 2013: 12 · 2012: 11
- FWCI
- 4.70
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- Funders
- Wellcome Trust (085176)
- Chinese Academy of Agricultural Sciences
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- DNA transposition, cut-and-paste transposition, crystal structure
- MeSH terms
- Animals, DNA Transposable Elements, DNA-Binding Proteins, Drosophila, Models, Molecular, X-Ray Diffraction, Protein Structure, Tertiary, Crystallography, X-Ray, Transposases, Catalytic Domain
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