Molecular Architecture of the Mos1 Paired-End Complex: The Structural Basis of DNA Transposition in a Eukaryote
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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 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 [51]
The Results and Discussion (‘The PEC contains a dimeric transposase’; page not available) describe a visualized eukaryotic Mos1 transpososome, supporting that part of the citation. But the structure contains transposon ends positioned as if just cleaved, not a post-catalytic strand-transfer complex. In ‘A model for the target capture complex,’ target DNA is modeled rather than observed, so this paper does not show a sharp deformation of target DNA. (LLM, conf=0.88)
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“(a) CAACTG-----AA-----TTGAA (3) (b) CAACT ---CAAA -----TGAA (2) (c) CAACTG---GA-------TTGAA (4) (d) CAACT-----CGA------TTGAA (1) (e) CAACT—--CAG------TTGAA (1) (f) CAACTG---AAA--------TGAA (1) (g) CAAC-----CGAA--------TGAA (2) C rpsL LacZ-SB CCCTAGAATTCATAATA TATTATGAATTCTAGGG CCCTAGAATTCATAATACAG TATTATGAATTCTAGGG”
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Feng, X., Bednarz, A. L., & Colloms, S. D. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1068 · Cited by 34 · see citing works
“(B) ISY100 transposase is expected to act as a dimer (27); one”
BackgroundSelf-citationBuchmann, J. P., Matsumoto, T., Stein, N., Keller, B., & Wicker, T. (2012) · The Plant Journal · doi:10.1111/j.1365-313x.2012.05007.x · Cited by 33 · see citing works
Morellet, N., Li, X., Wieninger, S. A., Taylor, J. L., Bischerour, J., Moriau, S., Lescop, E., Bardiaux, B., Mathy, N., Assrir, N., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky044 · Cited by 32 · see citing works
“Four transpososomes assembled by DD(D/E) transposases have been structurally characterized: the prokaryotic Tn5 transposase in complex with Tn5 transposon end DNAs (68); the Mu transposase in complex with bacteriophage DNA ends and target DNA (69); the eukaryotic mariner Mos1 transposon (70) and Hermes, a member of th…”
MethodZhang, T., Tan, S., Tang, N., Li, Y., Zhang, C., Sun, J., Guo, Y., Gao, H., Cai, Y., Sun, W. H., et al. (2024) · Cell · doi:10.1016/j.cell.2024.05.007 · Cited by 31 · see citing works
Structural gymnastics of RAG-mediated DNA cleavage in V(D)J recombination
Ru, H., Zhang, P., & Wu, H. (2018) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2018.11.001 · Cited by 30 · see citing works
Engineered Sleeping Beauty transposase redirects transposon integration away from genes
Miskey, C., Kesselring, L., Querques, I., Abrusán, G., Barábas, O., & Ivics, Z. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac092 · Cited by 28 · see citing works
“Structural modeling identifies candidate residues involved in target DNA interactions of the Sleeping Beauty transposase To shortlist amino acids in the SB transposase potentially involved in shaping its integration site selection, we performed a comparative structural analysis of a structural model of the SB TCC comp…”
InfluentialSolution conformations of early intermediates in Mos1 transposition
Cuypers, M. G., Trubitsyna, M., Callow, P., Forsyth, V. T., & Richardson, J. M. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1295 · Cited by 29 · see citing works
“The order and requirements for DNA excision have been established (10,11), and crystal structures have been determined of the transposase C-terminal catalytic domain (11) and the paired-end complex of transposase and cleaved transposon DNA (14).”
BackgroundInfluentialSelf-citationIdentification and evolutionary history of the DD41D transposons in insects
Zhang, H., Shen, Y., Xiong, X., Han, M., & Xiao-gu, Z. (2015) · Genes & Genomics · doi:10.1007/s13258-015-0356-4 · Cited by 28 · see citing works
“2009), the transposase structures of the rosa subfamily and the Lsra subfamily can be predicted based on these templates (van Pouderoyen et al. 1997; Richardson et al. 2009).”
InfluentialTc1-like transposable elements in plant genomes
Liu, Y., & Yang, G. (2014) · Mobile DNA · doi:10.1186/1759-8753-5-17 · Cited by 27 · see citing works
“The pocket formed by these residues contains the metal ions needed in the DNA cleavage reaction during transposition [24].”
Reconstitution of a functional IS608 single-strand transpososome: role of non-canonical base pairing
He, S., Hickman, A. B., Dyda, F., Johnson, N. P., Chandler, M., & Ton‐Hoang, B. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr566 · Cited by 26 · see citing works
A bend, flip and trap mechanism for transposon integration
Morris, E. R., Grey, H., McKenzie, G., Jones, A. C., & Richardson, J. M. (2016) · eLife · doi:10.7554/elife.15537 · Cited by 26 · see citing works
“The transposase subunits adopt a crossed (or trans) arrangement with IR DNA in the Mos1 STC, similar to the pre- and post-TS cleavage Mos1 PECs (Dornan et al., 2015; Richardson et al., 2009):”
BackgroundResultInfluentialSelf-citationCrosstalk between transposase subunits during cleavage of the mariner transposon
Bouuaert, C. C., Walker, N., Liu, D., & Chalmers, R. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku172 · Cited by 25 · see citing works
“In the Mos1 post-cleavage intermediate, the DNAbinding and catalytic domains of a given subunit are engaged with opposite ends of the transposon (Figure 7B, C and (4)).”
BackgroundInfluentialSeparate structural and functional domains of Tn4430 transposase contribute to target immunity
Lambin, M., Nicolas, É., Oger, C. A., Nguyen, N., Prozzi, D., & Hallet, B. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.07967.x · Cited by 25 · see citing works
“In Tc1/mariner transposases, the DNA binding domain is directly connected to the C-terminal catalytic domain through a short linker of ~ 13 aa (Watkins et al., 2004; Richardson et al., 2009).”
BackgroundKošek, D., Grabundžija, I., Lei, H., Bilić, I., Wang, H., Jin, Y., Peaslee, G. F., Hickman, A. B., & Dyda, F. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.028 · Cited by 20 · see citing works
Structural role of the flanking DNA in mariner transposon excision
Dornan, J., Grey, H., & Richardson, J. M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv096 · Cited by 24 · see citing works
“We proposed that these duplexes could occupy the putative binding sites for flanking DNA (4) served.”
Self-citationCryo-EM structure of mouse RAG1/2 PRC complex (DNA1)
Chen, X., Cui, Y., Zhou, Z. H., Yang, W., & Gellert, M. F. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6oen/pdb · Cited by 24 · see citing works
Hsmar1 Transposition Is Sensitive to the Topology of the Transposon Donor and the Target
Bouuaert, C. C., & Chalmers, R. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053690 · Cited by 23 · see citing works
“Furthermore, the Mos1 post-cleavage pairedends-complex structure suggests that the mariner transpososome may also bind the target [41].”
BackgroundJumping Ahead with Sleeping Beauty: Mechanistic Insights into Cut-and-Paste Transposition
Ochmann, M. T., & Ivics, Z. (2021) · Viruses · doi:10.3390/v13010076 · Cited by 20 · see citing works
“Based on the structure of the Mos1 synaptic complex [37], it is likely that the catalytic DDE domains are acting in”
BackgroundInfluentialStructure, Activity, and Function of SETMAR Protein Lysine Methyltransferase
Tellier, M. (2021) · Life · doi:10.3390/life11121342 · Cited by 20 · see citing works
“Of note, phosphorylation of the equivalent residue in another transposase, Ser170 in Mos1, is performed by the cAMP-dependent protein kinase (PKA) and prevents the active transport of the transposase to the nucleus and also interferes with the formation of the paired-end complex (a transposase dimer bound to two ITRs)…”
BackgroundNMR structural analysis of Sleeping Beauty transposase binding to DNA
Carpentier, C. E., Schreifels, J. M., Aronovich, E. L., Carlson, D. F., Hackett, P. B., & Nesmelova, I. V. (2013) · Protein Science · doi:10.1002/pro.2386 · Cited by 18 · see citing works
Košek, D., Hickman, A. B., Ghirlando, R., He, S., & Dyda, F. (2020) · The EMBO Journal · doi:10.15252/embj.2020105666 · Cited by 18 · see citing works
“This is reflected in the rotational symmetry relating the two bound TIRs seen in available trans-pososome structures (Davies et al , 2000; Richardson et al , 2009; Montan˜o et al , 2012; Liu et al , 2019).”
DNA–PK facilitates piggyBac transposition by promoting paired-end complex formation
Jin, Y., Chen, Y., Zhao, S., Guan, K., Zhuang, Y., Zhou, W., Wu, X., & Xu, T. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612980114 · Cited by 18 · see citing works
“A paired-end complex (PEC) is first formed by aligning both ends of the transposon, which is then excised and inserted into new loci (1, 2).”
BackgroundDemattei, M.-V., Hedhili, S., Sinzelle, L., Bressac, C., Casteret, S., Moiré, N., Cambefort, J., Thomas, X., Pollet, N., Gantet, P., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023693 · Cited by 17 · see citing works
“Moreover, it is located in a non structured segment and contains a proline at the first position [17,32].”
InfluentialJump ahead with a twist: DNA acrobatics drive transposition forward
Arinkin, V., Smyshlyaev, G., & Barábas, O. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.08.006 · Cited by 17 · see citing works
Retroviral integrase: Structure, mechanism, and inhibition
Passos, D. O., Li, M., Craigie, R., & Lyumkis, D. (2021) · The Enzymes · doi:10.1016/bs.enz.2021.06.007 · Cited by 18 · see citing works
“Richardson JM, Colloms SD, Finnegan DJ, Walkinshaw MD, Molecular Architecture of the Mos1 Paired-End Complex: The Structural Basis of DNA Transposition in a Eukaryote, Cell.”
BackgroundTransposable Elements for Insect Transformation
Handler, A. M., & O’Brochta, D. A. (2011) · Elsevier eBooks · doi:10.1016/b978-0-12-384747-8.10004-2 · Cited by 17 · see citing works
B-to-A transition in target DNA during retroviral integration
Jozwik, I. K., Li, W., Zhang, D., Wong, D., Grawenhoff, J., Ballandras-Colas, A., Aiyer, S., Cherepanov, P., Engelman, A., & Lyumkis, D. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac644 · Cited by 16 · see citing works
Transposase–Transposase Interactions in MOS1 Complexes: A Biochemical Approach
Carpentier, G., Jaillet, J., Pflieger, A., Adet, J., Renault, S., & Augé‐Gouillou, C. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.11.032 · Cited by 16 · see citing works
Regulation of Mariner Transposition: The Peculiar Case of Mos1
Jaillet, J., Genty, M., Cambefort, J., Rouault, J.-D., & Augé‐Gouillou, C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043365 · Cited by 15 · see citing works
Chen, W., Mandali, S., Hancock, S. P., Kumar, P., Collazo, M., Cascio, D., & Johnson, R. C. (2018) · eLife · doi:10.7554/elife.39611 · Cited by 15 · see citing works
“For example, each subunit of the Mos1 Mariner-family transposase dimer binds to one transposon terminus and additional separate DNA binding domains associate with two subterminal binding sites on the other transposon end within the active complex (Richardson et al., 2009).”
BackgroundZhang, Y., Corbett, E., Wu, S., & Schatz, D. G. (2020) · The EMBO Journal · doi:10.15252/embj.2020105857 · Cited by 14 · see citing works
“While multiple STC structures have been reported for DDE transposases/ integrases (Richardson et al , 2009; Montano & Rice, 2011; Morris et al , 2016; Ballandras-Colas et al , 2017; Passos et al , 2017; Arinkin et al , 2019; Ghanim et al , 2019) including recently for RAG (Chen et al , 2020b), no…”
Biochemical Characterization and Comparison of Two Closely Related Active mariner Transposases
Trubitsyna, M., Morris, E. R., Finnegan, D., & Richardson, J. M. (2014) · Biochemistry · doi:10.1021/bi401193w · Cited by 13 · see citing works
Self-citationA model for the molecular organisation of the IS911 transpososome
Rousseau, P., Tardin, C., Tolou, N., Salomé, L., & Chandler, M. (2010) · Mobile DNA · doi:10.1186/1759-8753-1-16 · Cited by 13 · see citing works
“In spite of its key importance, the composition and organisation of such assemblies have been examined for only a handful of transposable elements [2,11] and with varying degrees of detail.”
BackgroundMethodInfluentialSantana, M. F., Silva, J. C. F., Mizubuti, E. S. G., Ara�jo, E. F., & de Queiroz, M. V. (2014) · BMC Microbiology · doi:10.1186/s12866-014-0256-9 · Cited by 13 · see citing works
Mechanistic insights into transposon cleavage and integration by TnsB of ShCAST system
Zeng, T., Yin, J., Liu, Z., Li, Z., Zhang, Y., Lv, Y., Lü, M., Luo, M., Chen, M., & Xiao, Y. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112698 · Cited by 12 · see citing works
Modeling the HIV-1 Intasome: A Prototype View of the Target of Integrase Inhibitors
Yin, Z., & Craigie, R. (2010) · Viruses · doi:10.3390/v2122777 · Cited by 12 · see citing works
“Prior to the determination of the PFV intasome structure, the structures of the Tn5 transposase [12] and Mos 1 [13] transposase were the only structures of an integrase or transposase in complex with DNA and they provided the best available scaffold for modeling the active site of the HIV-1 intasome.”
BackgroundA single active site in the mariner transposase cleaves DNA strands of opposite polarity
Bouuaert, C. C., & Chalmers, R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx826 · Cited by 12 · see citing works
“The residue lies within the second helix-turn-helix motif of the transposase, which is important for the recognition of the transposon end (30,38,39).”
BackgroundStructural Basis of Mos1 Transposase Inhibition by the Anti-retroviral Drug Raltegravir
Wolkowicz, U. M., Morris, E. R., Robson, M. I., Trubitsyna, M., & Richardson, J. M. (2014) · ACS Chemical Biology · doi:10.1021/cb400791u · Cited by 12 · see citing works
Self-citationBouchet, N., Jaillet, J., Gabant, G., Brillet, B., Briseño-Roa, L., Cadène, M., & Augé‐Gouillou, C. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt874 · Cited by 12 · see citing works
“The crystal structure of the Mos1 synaptic complex locates the S170 residue of one monomer in a structure called the ‘clamp loop’ (residues 162–189), which locks the PEC by interacting with the linker region (residues 113–125) of the second monomer (22).”
BackgroundThe Tn3-family of Replicative Transposons
Nicolas, É., Lambin, M., Dandoy, D., Galloy, C., Nguyen, N., Oger, C. A., & Hallet, B. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch32 · Cited by 12 · see citing works
Mechanisms of DNA Transposition
Hickman, A. B., & Dyda, F. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch25 · Cited by 13 · see citing works
Synergistic Coding of Carbon Dioxide and a Human Sweat Odorant in the Mosquito BrainPreprint
Shankar, S., Tauxe, G. M., Spikol, E. D., Li, M., Akbari, O. S., Giraldo, D., & McMeniman, C. J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.02.365916 · Cited by 13 · see citing works
Bouuaert, C. C., Tellier, M., & Chalmers, R. (2014) · Mobile Genetic Elements · doi:10.4161/mge.28807 · Cited by 11 · see citing works
“In the crystal structure of the Mos1 post-cleavage transpososome the WVPHEL motif is seen to occupy a central position in the dimer interface.(17) An unstructured “clamp-loop” feature emerges from the catalytic core of one transposase subunit, crosses the dimer interface, and interacts with the transposon end and the…”
BackgroundInfluentialIS21 family transposase cleaved donor complex traps two right-handed superhelical crossings
Spínola‐Amilibia, M., Araújo‐Bazán, L., de la Gándara, Á., Berger, J. M., & Arias‐Palomo, E. (2023) · Nature Communications · doi:10.1038/s41467-023-38071-x · Cited by 10 · see citing works
“To minimize the heterogeneity we elected to use only the pre-cleavedrightendforthestructuralstudies(SupplementaryTable1),an approach widely used for other transposases 50,51,53,54 .”
InfluentialEsnault, C., Chénais, B., Casse, N., Delorme, N., Louarn, G., & Pilard, J. (2013) · ChemPhysChem · doi:10.1002/cphc.201200885 · Cited by 11 · see citing works
Target Capture during Mos1 Transposition
Pflieger, A., Jaillet, J., Petit, A., Augé‐Gouillou, C., & Renault, S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.523894 · Cited by 11 · see citing works
“This model predicts that the Arg(186) MOS1 residue will bind to the target through the target TA dinucleotide, supporting subsequent integration (9).”
BackgroundInfluentialStructural Basis for the Inverted Repeat Preferences of mariner Transposases
Trubitsyna, M., Grey, H., Houston, D. R., Finnegan, D., & Richardson, J. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.636704 · Cited by 10 · see citing works
“Comparison of the crystal structure of the Mos1 IRL PEC reported here with our previous IRR PEC structure (18) provides a molecular explanation for this difference in binding affinity, as subtle differences in the interactions of the central region of IR and the linker between the two HTH regions of transposase are re…”
BackgroundMethodInfluentialSelf-citationGenome-wide comparison of Asian and African rice reveals high recent activity of DNA transposons
Roffler, S., & Wicker, T. (2015) · Mobile DNA · doi:10.1186/s13100-015-0040-x · Cited by 10 · see citing works
“When DNA transposons excise, they leave a double-strand break (DSB) with small 3′ overhangs which are derived from the TIRs of the element [22] (Additional file 1: Figure S1).”
BackgroundBlundell‐Hunter, G., Tellier, M., & Chalmers, R. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky794 · Cited by 9 · see citing works
“Next, the Hsmar1 transposase has a low affinity for non-specific DNA and two helix-turn-helix domains for sequence-specific binding (22,32,51).”
Tu, Z. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384747-8.10003-0 · Cited by 6 · see citing works
Structural Determinants of Sleeping Beauty Transposase Activity
Abrusán, G., Yant, S. R., Szilágyi, A., Marsh, J. A., Mátés, L., Izsvák, Z., Barábas, O., & Ivics, Z. (2016) · Molecular Therapy · doi:10.1038/mt.2016.110 · Cited by 8 · see citing works
“…similar structure in the Protein Data Bank (PDB, http:/www.rcsb.org) to the predicted structure (supplementary SB.pdb file) is the Mos1 transposase, 29 which was also the highest ranking template used by I-TASSER (see Supplementary Figure S1b,c for structural alignments between the Mos1…”
Mariner and the ITm Superfamily of Transposons
Tellier, M., Bouuaert, C. C., & Chalmers, R. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch34 · Cited by 8 · see citing works
Shankar, S., Giraldo, D., Tauxe, G. M., Spikol, E. D., Li, M., Akbari, O. S., Wohl, M. P., & McMeniman, C. J. (2025) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkae307 · Cited by 6 · see citing works
“BLAST searches were used to map splinkerette fragments derived from each Mos1 mariner cassette to coordinate locations in the genome at canonical TA dinucleotides (Richardson et al .”
Harshey, R. M. (2015) · ASM Press eBooks · doi:10.1128/9781555819217.ch31 · Cited by 7 · see citing works
Tellier, M., & Chalmers, R. (2020) · Mobile DNA · doi:10.1186/s13100-020-0200-5 · Cited by 7 · see citing works
- 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 › Agricultural and Biological Sciences › Plant Science › 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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