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Molecular Mechanisms of DNMT3A-3L-Mediated de novo DNA Methylation on Chromatin
Open accessPreprint — published as 10.1038/s41594-025-01704-4 · Paper page
Abstract
De novo DNA methylation is a fundamental epigenetic process essential for early development. It is mediated by DNA methyltransferase DNMT3A and DNMT3B, in cooperation with catalytically inactive DNMT3L. Abnormal DNA methylation contributes to genomic instability and oncogenesis, yet the mechanisms governing its establishment and regulation remain unclear. Here, we present high-resolution cryo-EM structures of the nucleosome-bound full-length DNMT3A2-3L and its oligomeric assemblies in the nucleosome-free state. Strikingly, DNMT3L C-terminal “Switching Helix” displayed a distinct conformation with a 180° rotational difference compared to its DNMT3B3 counterpart in the presence of nucleosome, preventing direct interactions with the nucleosome acidic patch. Instead, DNMT3L ADD domain promotes nucleosome binding, while DNMT3A PWWP domain inhibits it, indicating multi-layer regulation. Additionally, the novel oligomeric arrangement of DNMT3A2-3L in nucleosome-free states highlights its dynamic assembly and potential allosteric regulation. Furthermore, we identified the critical role of DNMT3L as a sensor of histone modifications, guiding the complex’s chromatin interaction. These findings uncover a previously unknown mechanism by which DNMT3A-3L mediates de novo DNA methylation on chromatin through complex reorganization, histone tail sensing, dynamic DNA search, and nucleosome engagement, providing key insights into epigenetic regulation.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
UCSF ChimeraX : Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,521
Okano, M., Bell, D. W., Haber, D. A., & Li, E. (1999) · Cell · doi:10.1016/s0092-8674(00)81656-6 · Cited by 6,143
Automated electron microscope tomography using robust prediction of specimen movements
Mastronarde, D. N. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.07.007 · Cited by 5,136
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808
The diverse roles of DNA methylation in mammalian development and disease
Greenberg, M., & Bourc’his, D. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0159-6 · Cited by 2,244
Lowary, P. T., & Widom, J. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1494 · Cited by 1,782
DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
Ooi, S. K. T., Qiu, C., Bernstein, E., Li, K., Jia, D., Yang, Z., Erdjument‐Bromage, H., Tempst, P., Lin, S., Allis, C. D., et al. (2007) · Nature · doi:10.1038/nature05987 · Cited by 1,643
DeepEMhancer: a deep learning solution for cryo-EM volume post-processing
Sánchez-García, R., Gómez-Blanco, J., Cuervo, A., Carazo, J. M., Sorzano, C. Ó. S., & Vargas, J. (2021) · Communications Biology · doi:10.1038/s42003-021-02399-1 · Cited by 1,311
Hata, K., Okano, M., Lei, H., & Li, E. (2002) · Development · doi:10.1242/dev.129.8.1983 · Cited by 1,073
Hhal methyltransferase flips its target base out of the DNA helix
Klimašauskas, S., Kumar, S., Roberts, R. J., & Cheng, X. (1994) · Cell · doi:10.1016/0092-8674(94)90342-5 · Cited by 959
Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation
Jia, D., Jurkowska, R. Z., Zhang, X., Jeltsch, A., & Cheng, X. (2007) · Nature · doi:10.1038/nature06146 · Cited by 850
Intragenic DNA methylation prevents spurious transcription initiation
Neri, F., Rapelli, S., Krepelova, A., Incarnato, D., Parlato, C., Basile, G., Maldotti, M., Anselmi, F., & Oliviero, S. (2017) · Nature · doi:10.1038/nature21373 · Cited by 739
5-Methylcytosine in Eukaryotic DNA
Ehrlich, M., & Wang, R. Y. ‐. (1981) · Science · doi:10.1126/science.6262918 · Cited by 736
Genomic profiling of DNA methyltransferases reveals a role for DNMT3B in genic methylation
Baubec, T., Colombo, D. F., Wirbelauer, C., Schmidt, J., Burger, L., Krebs, A. R., Akalin, A., & Schübeler, D. (2015) · Nature · doi:10.1038/nature14176 · Cited by 705
The Dnmt3a PWWP Domain Reads Histone 3 Lysine 36 Trimethylation and Guides DNA Methylation
Dhayalan, A., Rajavelu, A., Rathert, P., Tamas, R., Jurkowska, R. Z., Ragozin, S., & Jeltsch, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.089433 · Cited by 597
GraFix: sample preparation for single-particle electron cryomicroscopy
Kastner, B., Fischer, N., Golas, M. M., Sander, B. O., Dube, P., Boehringer, D., Hartmuth, K., Deckert, J., Hauer, F., Wolf, E., et al. (2007) · Nature Methods · doi:10.1038/nmeth1139 · Cited by 578
DNMT3L Stimulates the DNA Methylation Activity of Dnmt3a and Dnmt3b through a Direct Interaction
Suetake, I., Shinozaki, F., Miyagawa, J., Takeshima, H., & Tajima, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400181200 · Cited by 550
The DNA methyltransferase-like protein DNMT3L stimulates de novo methylation by Dnmt3a
Chedin, F. L., Lieber, M. R., & Hsieh, C. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262443999 · Cited by 540
The histone mark H3K36me2 recruits DNMT3A and shapes the intergenic DNA methylation landscape
Weinberg, D. N., Papillon-Cavanagh, S., Chen, H., Yue, Y., Chen, X., Rajagopalan, K. N., Horth, C., McGuire, J. T., Xu, X., Nikbakht, H., et al. (2019) · Nature · doi:10.1038/s41586-019-1534-3 · Cited by 524
Otani, J., Nankumo, T., Arita, K., Inamoto, S., Ariyoshi, M., & Shirakawa, M. (2009) · EMBO Reports · doi:10.1038/embor.2009.218 · Cited by 435
Zhang, Y., Jurkowska, R. Z., Soeroes, S., Rajavelu, A., Dhayalan, A., Bock, I., Rathert, P., Brandt, O., Reinhardt, R., Fischle, W., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq147 · Cited by 405
DNA methylation loss in late-replicating domains is linked to mitotic cell division
Zhou, W., Dinh, H. Q., Ramjan, Z., Weisenberger, D. J., Nicolet, C. M., Shen, H., Laird, P. W., & Berman, B. P. (2018) · Nature Genetics · doi:10.1038/s41588-018-0073-4 · Cited by 405
Structural insight into autoinhibition and histone H3-induced activation of DNMT3A
Guo, X., Wang, L., Li, J., Ding, Z., Xiao, J., Yin, X., He, S., Shi, P., Dong, L., Li, G., et al. (2015) · Nature · doi:10.1038/nature13899 · Cited by 361
Structural basis for DNMT3A-mediated de novo DNA methylation
Zhang, Z., Lu, R., Wang, P., Yu, Y., Chen, D., Gao, L., Liu, S., Ji, D., Rothbart, S. B., Wang, Y., et al. (2018) · Nature · doi:10.1038/nature25477 · Cited by 354
Gowher, H., Liebert, K., Hermann, A., Xu, G., & Jeltsch, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413412200 · Cited by 327
Chen, T., Tsujimoto, N., & Li, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.9048-9058.2004 · Cited by 284
GraFix: Stabilization of Fragile Macromolecular Complexes for Single Particle Cryo-EM
Stark, H. (2010) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(10)81005-5 · Cited by 246
Chen, Z., Mann, J. R., Hsieh, C., Riggs, A. D., & Chedin, F. L. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20447 · Cited by 231
Allosteric control of mammalian DNA methyltransferases – a new regulatory paradigm
Jeltsch, A., & Jurkowska, R. Z. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw723 · Cited by 218
DNA methylation in human epigenomes depends on local topology of CpG sites
Lövkvist, C., Dodd, I. B., Sneppen, K., & Haerter, J. O. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw124 · Cited by 180
Roles of H3K4 methylation in biology and disease
Wang, H., & Helin, K. (2024) · Trends in Cell Biology · doi:10.1016/j.tcb.2024.06.001 · Cited by 173
Duymich, C. E., Charlet, J., Yang, X., Jones, P. A., & Liang, G. (2016) · Nature Communications · doi:10.1038/ncomms11453 · Cited by 165
Self-citationVeland, N., Lu, Y., Hardikar, S., Gaddis, S., Zeng, Y., Liu, B., Estecio, M. R., Takata, Y., Lin, K., Tomida, M. W., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky947 · Cited by 150
Histone tails regulate DNA methylation by allosterically activating de novo methyltransferase
Li, B.-Z., Huang, Z., Cui, Q., Song, X., Du, L., Jeltsch, A., Chen, P., Li, G., Li, E., & Xu, G. (2011) · Cell Research · doi:10.1038/cr.2011.92 · Cited by 148
Structure of nucleosome-bound DNA methyltransferases DNMT3A and DNMT3B
Xu, T.-H., Liu, M., Zhou, X. E., Liang, G., Zhao, G., Xu, H. E., Melcher, K., & Jones, P. A. (2020) · Nature · doi:10.1038/s41586-020-2747-1 · Cited by 131
Self-citationDNMT1 reads heterochromatic H4K20me3 to reinforce LINE-1 DNA methylation
Ren, W., Fan, H., Grimm, S. A., Kim, J. J., Li, L., Guo, Y., Petell, C. J., Tan, X.-F., Zhang, Z., Coan, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22665-4 · Cited by 124
The role of DNA methylation in directing the functional organization of the cancer epigenomePreprint
Lay, F. D., Liu, Y., Kelly, T. K., Witt, H. N., Farnham, P., Jones, P. A., & Berman, B. P. (2015) · Genome Research · doi:10.1101/gr.183368.114 · Cited by 111
Self-citationOligomerization and Binding of the Dnmt3a DNA Methyltransferase to Parallel DNA Molecules
Jurkowska, R. Z., Rajavelu, A., Anspach, N., Urbanke, C., Jankevicius, G., Ragozin, S., Nellen, W., & Jeltsch, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.254987 · Cited by 106
Oligomerization of DNMT3A Controls the Mechanism of de Novo DNA Methylation
Holz-Schietinger, C., Matje, D. M., Harrison, M. F., & Reich, N. O. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.284687 · Cited by 81
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Zeng, Y., Ren, R., Kaur, G., Hardikar, S., Ying, Z., Babcock, L., Gupta, E., Zhang, X., Chen, T., & Cheng, X. (2020) · Genes & Development · doi:10.1101/gad.341925.120 · Cited by 81
Dukatz, M., Holzer, K., Choudalakis, M., Emperle, M., Lungu, C., Bashtrykov, P., & Jeltsch, A. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.09.006 · Cited by 78
microRNA-199a-3p, DNMT3A, and aberrant DNA methylation in testicular cancer
Chen, B., Gu, S., Suen, Y. K., Li, L., & Chan, W. (2013) · Epigenetics · doi:10.4161/epi.25799 · Cited by 64
Nguyen, T.-V., Yao, S., Wang, Y., Rolfe, A., Selvaraj, A., Darman, R. B., Ke, J., Warmuth, M., Smith, P. G., Larsen, N., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010126 · Cited by 44
Epigenetic modifiers DNMT3A and BCOR are recurrently mutated in CYLD cutaneous syndrome
Davies, H. R., Hodgson, K., Schwalbe, E. C., Coxhead, J., Sinclair, N., Zou, X., Cockell, S., Husain, A., Nik‐Zainal, S., & Rajan, N. (2019) · Nature Communications · doi:10.1038/s41467-019-12746-w · Cited by 39
Bouazoune, K., Miranda, T. B., Jones, P. A., & Kingston, R. E. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp524 · Cited by 36
Self-citationGretarsson, K. H., Abini-Agbomson, S., Gloor, S. L., Weinberg, D. N., McCuiston, J. L., Kumary, V. U. S., Hickman, A. R., Sahu, V., Lee, R., Xu, X., et al. (2024) · Science Advances · doi:10.1126/sciadv.adp0975 · Cited by 27
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Choi, W.-Y., Li, C., Chen, Y., Wang, Y., & Cheng, Y. (2025) · Nature · doi:10.1038/s41586-025-08782-w · Cited by 26
Bröhm, A., Schoch, T., Dukatz, M., Graf, N., Dorscht, F., Mantai, E., Adam, S., Bashtrykov, P., & Jeltsch, A. (2022) · Communications Biology · doi:10.1038/s42003-022-03119-z · Cited by 25
Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction
Chen, X., Guo, Y., Zhao, T., Lu, J., Fang, J., Wang, Y., Wang, G. G., & Song, J. (2024) · Nature Communications · doi:10.1038/s41467-024-50526-3 · Cited by 25
Structural basis for the allosteric regulation and dynamic assembly of DNMT3B
Lu, J., Fang, J., Zhu, H., Liang, K. L., Khudaverdyan, N., & Song, J. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad972 · Cited by 23
UHRF1 ubiquitin ligase activity supports the maintenance of low-density CpG methylation
Tiedemann, R. L., Hrit, J. A., Du, Q., Wiseman, A. K., Eden, H. E., Dickson, B. M., Kong, X., Chomiak, A. A., Vaughan, R. M., Tibben, B. M., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1105 · Cited by 21
Self-citationStructure-guided functional suppression of AML-associated DNMT3A hotspot mutations
Lu, J., Guo, Y., Yin, J., Chen, J., Wang, Y., Wang, G. G., & Song, J. (2024) · Nature Communications · doi:10.1038/s41467-024-47398-y · Cited by 20
Multimerization of the Dnmt3a DNA Methyltransferase and Its Functional Implications
Jeltsch, A., & Jurkowska, R. Z. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-386931-9.00016-7 · Cited by 19
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Wapenaar, H., Clifford, G., Rolls, W., Pasquier, M., Burdett, H., Zhang, Y., Deák, G., Zou, J., Spanos, C., Taylor, M. R. D., et al. (2024) · EMBO Reports · doi:10.1038/s44319-024-00306-3 · Cited by 18
Chadda, R., Kaushik, V., Ahmad, I. M., Deveryshetty, J., Holehouse, A. S., Sigurdsson, S. T., Biswas, G., Levy, Y., Bothner, B. B., Cooley, R. B., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae584 · Cited by 12
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Metadata
- Authors
- Yan, Y., Zhou, X. E., Thomas, S. L., Liu, M., Lai, G.-Q., Worden, E. J., Jones, P. A., & Xu, T.-H.
- Affiliations
- Saint Louis University (US)
- Van Andel Institute (US)
- Corresponding author
- Jones, Peter A
- Xu, Ting-Hai
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Publisher
- openRxiv
- Published
- 2025-06-13
- Volume
- 33
- Issue
- 1
- Pages
- 171-183
- ISSN
- 1545-9985 (ISSN-L)
- PMC
- PMC13049598
- OpenAlex
- W4415731750
- Cited by
- 14
- References
- 58
- Citations by year
- 2026: 14
- FWCI
- 4.18
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion)
- Funders
- the Doisy Fund of the Edward A. Doisy Department of Biochemistry and Molecular Biology at Saint Louis University School of Medicine
- National Institutes of Health (R35CA209859, R35GM147261, R50CA243878)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- DNMT3A, DNMT3L, de novo methylation, DNA methyltransferases, nucleosome binding, H3K36 methylation, PWWP domain, protein oligomerization, allosteric regulation, cryo-EM structure
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