The DOI matches its Crossref record; 237 of the 238 references it cites were found in a registry or an index.
Histone post-translational modifications - cause and consequence of genome function
Abstract
Much has been learned since the early 1960s about histone post-translational modifications (PTMs) and how they affect DNA-templated processes at the molecular level. This understanding has been bolstered in the past decade by the identification of new types of histone PTM, the advent of new genome-wide mapping approaches and methods to deposit or remove PTMs in a locally and temporally controlled manner. Now, with the availability of vast amounts of data across various biological systems, the functional role of PTMs in important processes (such as transcription, recombination, replication, DNA repair and the modulation of genomic architecture) is slowly emerging. This Review explores the contribution of histone PTMs to the regulation of genome function by discussing when these modifications play a causative (or instructive) role in DNA-templated processes and when they are deposited as a consequence of such processes, to reinforce and record the event. Important advances in the field showing that histone PTMs can exert both direct and indirect effects on genome function are also presented.
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“These PTMs predominantly occur on the N-terminal histone tails and include acetylation, methylation, phosphorylation, and ubiquitination, forming combinatorial patterns often referred to as the “histone code,” which influences transcription in a context-dependent manner (Millán-Zambrano et al., 2022; Miziak et al., 2024; Jenuwein and Allis, 2001; Lam et al., 2019).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Millán-Zambrano et al., 2022
In the citing paper
“The flexible N-terminal tails of histones protrude from the nucleosome and serve as major sites for post-translational modifications (PTMs), including acetylation, methylation, and phosphorylation (Millán-Zambrano et al., 2022; Le et al., 2023).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Millán-Zambrano et al., 2022
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Cites
Items 201–237 of 237
Laue, K., Rajshekar, S., Courtney, A. J., Lewis, Z., & Goll, M. G. (2019) · Nature Communications · doi:10.1038/s41467-019-09582-3 · Cited by 78
Phosphorylation of histone H3(T118) alters nucleosome dynamics and remodeling
North, J. A., Javaid, S., Ferdinand, M. B., Chatterjee, N., Picking, J. W., Shoffner, M. A., Nakkula, R. J., Bartholomew, B., Ottesen, J. J., Fishel, R. A., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr304 · Cited by 77
Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler‐Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., et al. (2018) · Science Advances · doi:10.1126/sciadv.aat6224 · Cited by 77
In vivo binding of PRDM9 reveals interactions with noncanonical genomic sitesPreprint
Grey, C., Clément, J. A. J., Buard, J., Leblanc, B., Gut, I. G., Gut, M. O., Duret, L., & de Massy, B. (2017) · Genome Research · doi:10.1101/gr.217240.116 · Cited by 76
Jack, A. P. M., Bussemer, S., Hahn, M., Pünzeler, S., Snyder, M., Wells, M. B., Csankovszki, G., Solovei, I. V., Schotta, G., & Hake, S. B. (2013) · PLoS ONE · doi:10.1371/journal.pone.0051765 · Cited by 73
McCarthy, R. L., Kaeding, K. E., Keller, S. H., Zhong, Y., Xu, L., Hsieh, A., Hou, Y., Donahue, G., Becker, J. S., Alberto, O., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00725-7 · Cited by 73
Sitbon, D., Boyarchuk, E., Dingli, F., Loew, D., & Almouzni, G. (2020) · Nature Communications · doi:10.1038/s41467-020-15084-4 · Cited by 71
Bian, Q., Anderson, E. C., Yang, Q., & Meyer, B. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002068117 · Cited by 71
Effects of Histone Tail Domains on the Rate of Transcriptional Elongation through a Nucleosome
Protacio, R. U., Li, G., Lowary, P. T., & Widom, J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.23.8866-8878.2000 · Cited by 67
Rondinelli, B., Schwerer, H., Antonini, E., Gaviraghi, M., Lupi, A., Frenquelli, M., Cittaro, D., Segalla, S., Lemaı̂tre, J.-M., & Tonon, G. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv090 · Cited by 64
A mechanism for epigenetic control of DNA replicationPreprint
Sansam, C. G., Pietrzak, K., Majchrzycka, B., Kerlin, M. A., Chen, J., Rankin, S., & Sansam, C. L. (2018) · Genes & Development · doi:10.1101/gad.306464.117 · Cited by 63
Feng, Y., Wang, Y., Wang, X., He, X., Chen, Y., Naseri, A., Pederson, T., Zheng, J., Zhang, S., Xiao, X., et al. (2020) · Genome biology · doi:10.1186/s13059-020-02201-1 · Cited by 62
Wu, R., Wang, Z., Zhang, H., Gan, H., & Zhang, Z. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw848 · Cited by 61
Three Distinct Patterns of Histone H3Y41 Phosphorylation Mark Active Genes
Dawson, M. A., Foster, S. D., Bannister, A. J., Robson, S. C., Hannah, R., Wang, X., Xhemalçe, B., Wood, A. D., Green, A. R., Göttgens, B., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.08.016 · Cited by 60
Self-citationCross-talk between Lysine-Modifying Enzymes Controls Site-Specific DNA Amplifications
Mishra, S., Rechem, C. V., Pal, S., Clarke, T. L., Chakraborty, D., Mahan, S. D., Black, J. C., Murphy, S. E., Lawrence, M. S., Daniels, D. L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.018 · Cited by 60
Bhattacharyya, T., Walker, M., Powers, N. R., Brunton, C., Fine, A. D., Petkov, P. M., & Handel, M. A. (2019) · Current Biology · doi:10.1016/j.cub.2019.02.007 · Cited by 55
Enhancer-associated H3K4 methylation safeguards in vitro germline competence
Bleckwehl, T., Crispatzu, G., Schaaf, K., Respuela, P., Bartusel, M., Benson, L. J., Clark, S. J., Dorighi, K. M., Barral, A., Laugsch, M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26065-6 · Cited by 54
Lim, H.-J., Dimova, N. V., Tan, M.-K. M., Sigoillot, F. D., King, R. W., & Shi, Y. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00689-13 · Cited by 53
Oikawa, M., Simeone, A., Hörmanseder, E., Teperek, M., Gaggioli, V., O’Doherty, A., Falk, E., Sporniak, M., D’Santos, C. S., Franklin, V. N. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17238-w · Cited by 53
Kaiser, V., & Semple, C. (2017) · Genome Biology · doi:10.1186/s13059-018-1483-4 · Cited by 52
Huang, Y., Sicar, S., Ramirez-Prado, J. S., Manza-Mianza, D., Antunez-Sanchez, J., Brik-Chaouche, R., Rodriguez-Granados, N. R., An, J., Bergounioux, C., Mahfouz, M. M., et al. (2021) · Genome Research · doi:10.1101/gr.273771.120 · Cited by 52
Anderson, E. C., Frankino, P. A., Higuchi‐Sanabria, R., Yang, Q., Bian, Q., Podshivalova, K., Shin, A., Kenyon, C. J., Dillin, A. G., & Meyer, B. J. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.08.004 · Cited by 51
Sperm-inherited H3K27me3 impacts offspring transcription and development in C. elegans
Kaneshiro, K. R., Rechtsteiner, A., & Strome, S. (2019) · Nature Communications · doi:10.1038/s41467-019-09141-w · Cited by 50
Gehre, M., Bunina, D., Sidoli, S., Lübke, M. J., Diaz, N. S., Trovato, M., Garcia, B. A., Zaugg, J. B., & Noh, K. (2020) · Nature Genetics · doi:10.1038/s41588-020-0586-5 · Cited by 50
Collective regulation of chromatin modifications predicts replication timing during cell cycle
Rechem, C. V., Ji, F., Chakraborty, D., Black, J. C., Sadreyev, R. I., & Whetstine, J. R. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109799 · Cited by 48
Meers, M. P., Henriques, T., Lavender, C. A., McKay, D. J., Strahl, B. D., Duronio, R. J., Adelman, K., & Matera, A. G. (2017) · eLife · doi:10.7554/elife.23249 · Cited by 44
Kreher, J., Takasaki, T., Cockrum, C., Sidoli, S., Garcia, B. A., Jensen, O. N., & Strome, S. (2018) · Genetics · doi:10.1534/genetics.118.301353 · Cited by 42
Dissecting the role of H3K64me3 in mouse pericentromeric heterochromatin
Lange, U. C., Siebert, S., Wossidlo, M., Weiss, T., Ziegler-Birling, C., Walter, J., Torres‐Padilla, M., Daujat, S., & Schneider, R. (2013) · Nature Communications · doi:10.1038/ncomms3233 · Cited by 37
Self-citationRat PRDM9 shapes recombination landscapes, duration of meiosis, gametogenesis, and age of fertility
Mihola, O., Landa, V., Pratto, F., Brick, K., Kobets, T., Kusari, F., Gasic, S., Smagulova, F. O., Grey, C., Flachs, P., et al. (2021) · BMC Biology · doi:10.1186/s12915-021-01017-0 · Cited by 28
A chemical field guide to histone nonenzymatic modifications
Faulkner, S., Maksimovic, I., & David, Y. (2021) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2021.05.002 · Cited by 19
Cross-talk between Lysine-Modifying Enzymes Controls Site-Specific DNA Amplifications
Mishra, S., Rechem, C. V., Pal, S., Clarke, T. L., Chakraborty, D., Mahan, S. D., Black, J. C., Murphy, S. E., Lawrence, M. S., Daniels, D. L., et al. (2018) · Cell · doi:10.1016/j.cell.2018.11.018 · Cited by 16
Lineage specific trimethylation of H3 on lysine 4 during C. elegans early embryogenesis
Wang, S., Fisher, K., & Poulin, G. B. (2011) · Developmental Biology · doi:10.1016/j.ydbio.2011.04.010 · Cited by 13
Enhancer-associated H3K4 methylation safeguards in vitro germline competence
Bleckwehl, T., Crispatzu, G., Schaaf, K., Respuela, P., Bartusel, M., Benson, L. J., Clark, S. J., Dorighi, K. M., Barral, A., Laugsch, M., et al. (2020) · Kölner Universitäts PublikationsServer (Universität zu Köln) · doi:10.17863/cam.76317 · Cited by 8
Nhp2 is a reader of H2AQ105me and part of a network integrating metabolism with rRNA synthesis
Mawer, J. S. P., Massen, J., Reichert, C., Grabenhorst, N., Mylonas, C., & Tessarz, P. (2021) · EMBO Reports · doi:10.15252/embr.202152435 · Cited by 8
Feng, Y., Wang, Y., Wang, X., He, X., Chen, Y., Naseri, A., Pederson, T., Zheng, J., Zhang, S., Xiao, X., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.15.204719 · Cited by 7
HELLS and PRDM9 form a Pioneer Complex to Open Chromatin at Meiotic Recombination HotspotsPreprint
Spruce, C. A., Dlamini, S., Ananda, G., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/764183 · Cited by 4
Bhattacharyya, T., Walker, M., Powers, N. R., Brunton, C., Fine, A. D., Petkov, P. M., & Handel, M. A. (2021) · Current Biology · doi:10.1016/j.cub.2021.03.002 · Cited by 2
Research works printed but not linked: 3
- Xhemalce B., Dawson M. A. & Bannister A. J. In Epigenetic Regulation and Epigenomics (ed. Meyers, R. A.) 657–703 (Wiley–Blackwell, 2012).
- Meers, M. P., Janssens, D. H. & Henikoff, S. Multifactorial chromatin regulatory landscapes at single cell resolution. Preprint at bioRxiv https://doi.org/10.1101/2021.07.08.451691v1.full (2021). · DOI
- Altemose, N. et al. DiMeLo-seq: a long-read, single-molecule method for mapping protein-DNA interactions genome-wide. Preprint at bioRxiv https://doi.org/10.1101/2021.07.06.451383v1 (2021). · DOI
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Chen, J., Huang, Z., Chen, Y., Tian, H., Chai, P., Shen, Y., Yao, Y., Xu, S., Ge, S., & Jia, R. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02082-x · Cited by 545
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Signaling pathways and targeted therapies for psoriasis
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Epigenetic regulation in cardiovascular disease: mechanisms and advances in clinical trials
Shi, Y., Zhang, H., Huang, S., Yin, L., Wang, F., Luo, P., & Huang, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01055-2 · Cited by 377
Epigenetics-targeted drugs: current paradigms and future challenges
Dai, W., Qiao, X., Fang, Y., Guo, R., Bai, P., Liu, S., Li, T., Jiang, Y., Wei, S., Na, Z., et al. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02039-0 · Cited by 405
Metadata
- Authors
- Millán-Zambrano, G., Burton, A., Bannister, A. J., & Schneider, R.
- Affiliations
- Consejo Superior de Investigaciones Científicas (ES)
- Helmholtz Munich (DE)
- University of Cambridge (GB)
- Corresponding author
- Bannister, Andrew J.
- Schneider, Robert
- Venue
- Nature Reviews Genetics
- Published
- 2022-03-25
- Volume
- 23
- Issue
- 9
- Pages
- 563-580
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- OpenAlex
- W4220743473
- Semantic Scholar
- 4a452bb0c38ba013f3a90217102ab8f7caf3fdaf
- Cited by
- 1,116
- References
- 238
- Citations by year
- 2026: 241 · 2025: 335 · 2024: 333 · 2023: 170 · 2022: 37
- FWCI
- 23.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- Site cant be reached (submittedVersion)
- PuSH - Publication Server of Helmholtz Zentrum München (submittedVersion)
- Funders
- Wellcome Trust (WT203144)
- Cancer Research UK (C6946/A24843, 27321, RG96894)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- histone modifications, genome function, transcription, DNA recombination, DNA replication, DNA repair, chromatin structure, genome-wide mapping
- MeSH terms
- DNA, DNA Repair, DNA Replication, Histones, Protein Processing, Post-Translational
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