Histone core modifications regulating nucleosome structure and dynamics
Abstract
Post-translational modifications of histones regulate all DNA-templated processes, including replication, transcription and repair. These modifications function as platforms for the recruitment of specific effector proteins, such as transcriptional regulators or chromatin remodellers. Recent data suggest that histone modifications also have a direct effect on nucleosomal architecture. Acetylation, methylation, phosphorylation and citrullination of the histone core may influence chromatin structure by affecting histone-histone and histone-DNA interactions, as well as the binding of histones to chaperones.
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Chromatin condensation status and existing chromatin dynamics influence both UV damage occurrence and repair capacity.
“One of the critical factors that influence both damage occurrence and repair capacity is certainly the chromatin condensation status and existing chromatin dynamics.”
From Focus on UV-Induced DNA Damage and Repair—Disease Relevance and Protective Strategies (2020) · cites this paper as [34]
Methylation (mono-, di-, tri-) and acetylation are the most extensively studied histone modifications, although many more have been observed.
“Methylation (mono-, di- and tri-) and acetylation are the most extensively studied modifications, although many more have been observed (Tessarz and Kouzarides, 2014).”
From The Cellular and Molecular Landscapes of the Developing Human Central Nervous System (2016) · cites this paper as Tessarz and Kouzarides, 2014
Acetylation of histone tails alters chromatin dynamics and generally increases accessibility to transcription factors, leading to activation of gene transcription.
“Acetylation of histone tails alters chromatin dynamics and generally increases accessibility to transcription factors, leading to activation of gene transcription (189) (Fig. 6).”
From Regulation and function of the mammalian tricarboxylic acid cycle (2023) · cites this paper as [189]
Cites
1 retracted
Yeast CAF-1 assembles histone (H3-H4)2 tetramers prior to DNA deposition
Winkler, D. D., Zhou, H., Dar, M. A., Zhang, Z., & Luger, K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks812 · Cited by 82 · see citing works
RetractedChromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works
Self-citationCrystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466 · see citing works
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,419 · see citing works
Perceiving the epigenetic landscape through histone readers
Musselman, C. A., Lalonde, M., Côté, J., & Kutateladze, T. G. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2436 · Cited by 840 · see citing works
Schübeler, D., MacAlpine, D. M., Scalzo, D., Wirbelauer, C., Kooperberg, C. L., van Leeuwen, F., Gottschling, D. E., O’Neill, L. P., Turner, B. M., Delrow, J. J., et al. (2004) · Genes & Development · doi:10.1101/gad.1198204 · Cited by 795 · see citing works
Jin, C., Zang, C., Wei, G., Cui, K., Peng, W., Zhao, K., & Felsenfeld, G. (2009) · Nature Genetics · doi:10.1038/ng.409 · Cited by 776 · see citing works
Nucleosome Assembly by a Complex of CAF-1 and Acetylated Histones H3/H4
Verreault, A., Kaufman, P. D., Kobayashi, R., & Stillman, B. (1996) · Cell · doi:10.1016/s0092-8674(00)81326-4 · Cited by 634 · see citing works
A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Masumoto, H., Hawke, D. H., Kobayashi, R., & Verreault, A. (2005) · Nature · doi:10.1038/nature03714 · Cited by 595 · see citing works
Crystal structure of a nucleosome core particle containing the variant histone H2A.Z.
Luger, K., Suto, R. K., Clarkson, M. J., & Tremethick, D. J. (2000) · Nature Structural Biology · doi:10.1038/81971 · Cited by 541 · see citing works
Ng, H. H., Feng, Q., Wang, H., Erdjument‐Bromage, H., Tempst, P., Zhang, Y., & Struhl, K. (2002) · Genes & Development · doi:10.1101/gad.1001502 · Cited by 536 · see citing works
Steger, D. J., Lefterova, M. I., Ying, L., Stonestrom, A. J., Schupp, M., Zhuo, D. X., Vakoc, A. L., Kim, J., Chen, J., Lazar, M. A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02076-07 · Cited by 499 · see citing works
Neumann, H., Hancock, S. M., Buning, R., Routh, A. L., Chapman, L., Somers, J., Owen‐Hughes, T., van Noort, J., Rhodes, D., & Chin, J. W. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.027 · Cited by 498 · see citing works
Structural Basis for the Histone Chaperone Activity of Asf1
English, C. M., Adkins, M. W., Carson, J. J., Churchill, M. E. A., & Tyler, J. K. (2006) · Cell · doi:10.1016/j.cell.2006.08.047 · Cited by 449 · see citing works
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447 · see citing works
Citrullination regulates pluripotency and histone H1 binding to chromatin
Christophorou, M. A., Castelo‐Branco, G., Halley‐Stott, R. P., Oliveira, C. S., Loos, R., Radzisheuskaya, A., Mowen, K. A., Bertone, P., Silva, J., Zernicka‐Goetz, M., et al. (2014) · Nature · doi:10.1038/nature12942 · Cited by 409 · see citing works
Self-citationProfile of Histone Lysine Methylation across Transcribed Mammalian Chromatin
Vakoc, C. R., Sachdeva, M. M., Wang, H., & Blobel, G. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01529-06 · Cited by 406 · see citing works
Acetylation in Histone H3 Globular Domain Regulates Gene Expression in Yeast
Xu, F., Zhang, K., & Grunstein, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.03.011 · Cited by 394 · see citing works
High-resolution dynamic mapping of histone-DNA interactions in a nucleosome
Hall, M. A., Shundrovsky, A., Bai, L., Fulbright, R. M., Lis, J. T., & Wang, M. D. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1526 · Cited by 385 · see citing works
Histone chaperones: an escort network regulating histone traffic
de Koning, L., Corpet, A., Haber, J. E., & Almouzni, G. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1318 · Cited by 365 · see citing works
Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4
Natsume, R., Eitoku, M., Akai, Y., Sano, N., Horikoshi, M., & Senda, T. (2007) · Nature · doi:10.1038/nature05613 · Cited by 291 · see citing works
Identification of novel histone post-translational modifications by peptide mass fingerprinting
Zhang, L., Eugeni, E. E., Parthun, M. R., & Freitas, M. A. (2003) · Chromosoma · doi:10.1007/s00412-003-0244-6 · Cited by 274 · see citing works
Tropberger, P., Pott, S., Keller, C., Kamieniarz-Gdula, K., Caron, M. J., Richter, F. M., Li, G., Mittler, G., Liu, E. T., Bühler, M., et al. (2013) · Cell · doi:10.1016/j.cell.2013.01.032 · Cited by 272 · see citing works
Kruger, W. D., Peterson, C. L., Sil, A., et al. (1995) · Genes & Development · doi:10.1101/gad.9.22.2770 · Cited by 246 · see citing works
Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
Tessarz, P., Santos-Rosa, H., Robson, S. C., Sylvestersen, K. B., Nelson, C. J., Nielsen, M. L., & Kouzarides, T. (2014) · Nature · doi:10.1038/nature12819 · Cited by 243 · see citing works
Self-citationAndrews, A. J., Chen, X., Zevin, A. S., Stargell, L. A., & Luger, K. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.037 · Cited by 236 · see citing works
Hyland, E. M., Cosgrove, M. S., Molina, H., Wang, D., Pandey, A., Cottee, R. J., & Boeke, J. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.22.10060-10070.2005 · Cited by 236 · see citing works
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure
Lu, X., Simon, M. D., Chodaparambil, J. V., Hansen, J. C., Shokat, K. M., & Luger, K. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1489 · Cited by 232 · see citing works
The role of FACT in making and breaking nucleosomes
Formosa, T. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.07.009 · Cited by 198 · see citing works
Histone fold modifications control nucleosome unwrapping and disassembly
Šimon, M., North, J. A., Shimko, J. C., Forties, R. A., Ferdinand, M. B., Manohar, M., Zhang, M., Fishel, R. A., Ottesen, J. J., & Poirier, M. G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106264108 · Cited by 197 · see citing works
Brown, D. T., Izard, T., & Misteli, T. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1050 · Cited by 193 · see citing works
Structural basis of histone H2A–H2B recognition by the essential chaperone FACT
Hondele, M., Stuwe, T., Hassler, M., Halbach, F., Bowman, A. J., Zhang, E., Nijmeijer, B., Kotthoff, C., Rybin, V., Amlacher, S., et al. (2013) · Nature · doi:10.1038/nature12242 · Cited by 181 · see citing works
Histone H4 Lysine 91 Acetylation
Ye, J., Ai, X., Eugeni, E. E., Zhang, L., Carpenter, L. R., Jelinek, M. A., Freitas, M. A., & Parthun, M. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.031 · Cited by 170 · see citing works
Mechanisms for ATP-dependent chromatin remodelling
Flaus, A., & Owen‐Hughes, T. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00172-6 · Cited by 164 · see citing works
Sir2 Deacetylates Histone H3 Lysine 56 to Regulate Telomeric Heterochromatin Structure in Yeast
Xu, F., Zhang, Q., Zhang, K., Xie, W., & Grunstein, M. R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.021 · Cited by 161 · see citing works
Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription
Cerbo, V. D., Mohn, F., Ryan, D., Montellier, E., Kacem, S., Tropberger, P., Kallis, E., Holzner, M., Hoerner, L., Feldmann, A., et al. (2014) · eLife · doi:10.7554/elife.01632 · Cited by 157 · see citing works
H3R42me2a is a histone modification with positive transcriptional effects
Casadio, F., Lu, X., Pollock, S. B., LeRoy, G., Garcia, B. A., Muir, T. W., Roeder, R. G., & Allis, C. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1312925110 · Cited by 154 · see citing works
Garcia, H., Miecznikowski, J. C., Safina, A. F., Commane, M., Ruusulehto, A., Kilpinen, S. K., Leach, R. W., Attwood, K. M., Yan, L., Degan, S. E., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.06.013 · Cited by 153 · see citing works
Daujat, S., Weiss, T., Mohn, F., Lange, U. C., Ziegler-Birling, C., Zeißler, U., Lappé, M., Schübeler, D., Torres‐Padilla, M., & Schneider, R. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1629 · Cited by 134 · see citing works
Histone Tails and the H3 αN Helix Regulate Nucleosome Mobility and Stability
Ferreira, H. C., Somers, J., Webster, R., Flaus, A., & Owen‐Hughes, T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02229-06 · Cited by 134 · see citing works
Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing
Huang, S., Zhou, H., Katzmann, D., Hochstrasser, M., Atanasova, E., & Zhang, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506176102 · Cited by 130 · see citing works
Structural basis for recognition of H3K56-acetylated histone H3–H4 by the chaperone Rtt106
Su, D., Hu, Q., Li, Q., Thompson, J. R., Cui, G., Fazly, A., Davies, B. A., Botuyan, M. V., Zhang, Z., & Mer, G. (2012) · Nature · doi:10.1038/nature10861 · Cited by 128 · see citing works
Histone H3 Lysine 56 Methylation Regulates DNA Replication through Its Interaction with PCNA
Yu, Y., Song, C., Zhang, Q., DiMaggio, P. A., Garcia, B. A., York, A. G., Carey, M., & Grunstein, M. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.019 · Cited by 126 · see citing works
Chromatin as an expansive canvas for chemical biology
Fierz, B., & Muir, T. W. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.938 · Cited by 121 · see citing works
Characterization of Lysine 56 of Histone H3 as an Acetylation Site in Saccharomyces cerevisiae
Özdemir, A., Spicuglia, S., Lasonder, E., Vermeulen, M., Campsteijn, C., Stunnenberg, H. G., & Logie, C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500181200 · Cited by 119 · see citing works
Bowman, A. J., Ward, R., Mkami, H. E., Owen‐Hughes, T., & Norman, D. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1003 · Cited by 105 · see citing works
Establishment and Maintenance of Alternative Chromatin States at a Multicopy Gene Locus
Wittner, M., Hamperl, S., Stöckl, U., Seufert, W., Tschochner, H., Milkereit, P., & Griesenbeck, J. (2011) · Cell · doi:10.1016/j.cell.2011.03.051 · Cited by 90 · see citing works
VanDemark, A. P., Hua, X., McCullough, L. L., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m708682200 · Cited by 88 · see citing works
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 · see citing works
The chaperone–histone partnership: for the greater good of histone traffic and chromatin plasticity
Hondele, M., & Ladurner, A. G. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.10.003 · Cited by 60 · see citing works
Structural characterization of H3K56Q nucleosomes and nucleosomal arrays
Watanabe, S., Resch, M. G., Lilyestrom, W. G., Clark, N., Hansen, J. C., Peterson, C. L., & Luger, K. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2010.01.009 · Cited by 57 · see citing works
Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing
Zunder, R. M., Antczak, A. J., Berger, J. M., & Rine, J. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1119095109 · Cited by 48 · see citing works
Iwasaki, W., Tachiwana, H., Kawaguchi, K., Shibata, T., Kagawa, W., & Kurumizaka, H. (2011) · Biochemistry · doi:10.1021/bi201021h · Cited by 47 · see citing works
Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure
North, J. A., Šimon, M., Ferdinand, M. B., Shoffner, M. A., Picking, J. W., Howard, C. J., Mooney, A. M., van Noort, J., Poirier, M. G., & Ottesen, J. J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku150 · Cited by 46 · see citing works
McCullough, L. L., Rawlins, R., Olsen, A. E., et al. (2011) · Genetics · doi:10.1534/genetics.111.128769 · Cited by 41 · see citing works
Identification of Histone Mutants That Are Defective for Transcription-Coupled Nucleosome Occupancy
Hainer, S. J., & Martens, J. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05195-11 · Cited by 37 · see citing works
Control of eukaryotic transcription elongation.
Winston, F. (2001) · Genome biology · doi:10.1186/gb-2001-2-2-reviews1006 · Cited by 34 · see citing works
Hyland, E. M., Molina, H., Poorey, K., et al. (2011) · Genes & Development · doi:10.1101/gad.2050311 · Cited by 30 · see citing works
Somers, J., & Owen‐Hughes, T. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp114 · Cited by 26 · see citing works
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“Acetylation of histone tails alters chromatin dynamics and generally increases accessibility to transcription factors, leading to activation of gene transcription (189) (Fig.”
BackgroundUnderstanding nucleosome dynamics and their links to gene expression and DNA replication
Lai, W. K. M., & Pugh, B. F. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.47 · Cited by 495 · see citing works
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- Authors
- Tessarz, P., & Kouzarides, T.
- Affiliations
- The Gurdon Institute (GB)
- Corresponding author
- Tessarz, Peter
- Kouzarides, Tony
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2014-10-15
- Volume
- 15
- Issue
- 11
- Pages
- 703-708
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2094998522
- Cited by
- 1,018
- References
- 60
- Citations by year
- 2026: 42 · 2025: 69 · 2024: 93 · 2023: 93 · 2022: 80 · 2021: 108 · 2020: 83 · 2019: 104 · 2018: 92 · 2017: 99 · 2016: 92 · 2015: 63
- FWCI
- 8.01
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust (092096)
- Cancer Research UK (10827, 17001)
- Biotechnology and Biological Sciences Research Council (BB/K017438/1)
- 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, nucleosome structure, nucleosome dynamics, histone acetylation, histone methylation, histone phosphorylation, histone citrullination, chromatin structure, histone-DNA interactions, histone-histone interactions, histone chaperone, chromatin remodeling, transcriptional regulation, DNA replication, DNA repair
- MeSH terms
- Acetylation, Citrulline, DNA, DNA Repair, DNA Replication, Histones, Humans, Methylation, Nucleosomes, Phosphorylation, Protein Processing, Post-Translational, Transcription, Genetic, Molecular Chaperones
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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