Chromatin modifications and their function
Open accessAbstract
The surface of nucleosomes is studded with a multiplicity of modifications. At least eight different classes have been characterized to date and many different sites have been identified for each class. Operationally, modifications function either by disrupting chromatin contacts or by affecting the recruitment of nonhistone proteins to chromatin. Their presence on histones can dictate the higher-order chromatin structure in which DNA is packaged and can orchestrate the ordered recruitment of enzyme complexes to manipulate DNA. In this way, histone modifications have the potential to influence many fundamental biological processes, some of which may be epigenetically inherited.
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Combinatorial post-translational modification patterns are interpreted by reader proteins that recruit effector complexes to regulate chromatin accessibility.
“Combinatorial PTM patterns—the so-called “histone code”—are interpreted by reader proteins that recruit effector complexes to regulate chromatin accessibility (Kouzarides, 2007; Campos and Reinberg, 2009).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Kouzarides, 2007
Previous studies investigating the role of HDACi on gene expression changes in HL60 cells are in agreement with the observed gene expression changes.
“This is in agreement with previous studies investigating the role of HDACiongeneexpression changes in HL60 cells (2, 29, 30, 35, 43).”
From Histone Deacetylase (HDAC) Inhibitor Kinetic Rate Constants Correlate with Cellular Histone Acetylation but Not Transcription and Cell Viability (2013) · cites this paper as [2]
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InfluentialING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
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A Topoisomerase IIß-Mediated dsDNA Break Required for Regulated Transcription
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Histone Deimination Antagonizes Arginine Methylation
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“One role for H3K36me is the suppression of inappropriate initiation from cryptic start sites within the coding region (Carrozza et al., 2005; Cuthbert et al., 2004; Joshi and Struhl, 2005; Keogh et al., 2005).”
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An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
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Cotranscriptional Set2 Methylation of Histone H3 Lysine 36 Recruits a Repressive Rpd3 Complex
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The key to development: interpreting the histone code?
Margueron, R., Trojer, P., & Reinberg, D. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.01.005 · Cited by 747 · cited 1× · see citing works
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The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
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Dynamic Regulation of Histone Lysine Methylation by Demethylases
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“A role for this modification has been demonstrated in transcriptional elongation by the histone chaperone FACT (Pavri et al., 2006).”
Vakoc, C. R., Mandat, S. A., Olenchock, B. A., & Blobel, G. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.011 · Cited by 698 · cited 2× · see citing works
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Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2
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Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
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InfluentialHistone Variant H2A.Z Marks the 5′ Ends of Both Active and Inactive Genes in Euchromatin
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SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosisPreprint
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InfluentialA role for Saccharomyces cerevisiae histone H2A in DNA repair
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“Two phosphorylation sites on this histone have a role in doublestrand break repair via nonhomologous end joining: H2AS129 mediated by Mec1 (Downs et al., 2000) and H4S1 mediated by Caesin kinase II (Cheung et al.”
The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
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Methylation of Histone H4 Lysine 20 Controls Recruitment of Crb2 to Sites of DNA Damage
Sanders, S. L., Portoso, M., Mata, J., Bähler, J., Allshire, R. C., & Kouzarides, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.009 · Cited by 545 · cited 8× · see citing works
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“…two nucleosomes flanking the initiation site that are hypoacetylated at certain lysines and are enriched in the H2A variant Hzt1 (Liu et al., 2005; Zhang et al., 2005; Raisner et al., 2005; Millar et al., 2006; Millar and Grunstein, 2006); the initiation site itself is devoid of nucleosomes;…”
Monoubiquitination of Human Histone H2B: The Factors Involved and Their Roles in HOX Gene Regulation
Zhu, B., Zheng, Y., Pham, A.-D., Mandal, S. S., Erdjument‐Bromage, H., Tempst, P., & Reinberg, D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.025 · Cited by 532 · cited 1× · see citing works
“In contrast, H2BK120 ubiquitylation is mediated by human RNF20/RNF40 and UbcH6 and in budding yeast by Rad6/Bre1 and is activatory for transcription (Zhu et al., 2005).”
Joshi, A., & Struhl, K. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.11.021 · Cited by 531 · cited 1× · see citing works
“One role for H3K36me is the suppression of inappropriate initiation from cryptic start sites within the coding region (Carrozza et al., 2005; Cuthbert et al., 2004; Joshi and Struhl, 2005; Keogh et al., 2005).”
Wang, H., Zhai, L., Xu, J., Joo, H.-Y., Jackson, S., Erdjument‐Bromage, H., Tempst, P., Xiong, Y., & Zhang, Y. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.035 · Cited by 520 · cited 2× · see citing works
“Ubiquitylation of H2AK119 is mediated by the Bmi/Ring1A protein found in the human polycomb complex and is associated with transcriptional repression (Wang et al., 2006).”
Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-dependent acetylation
Pray-Grant, M. G., Daniel, J. A., Schieltz, D. M., Yates, J. R., & Grant, P. A. (2005) · Nature · doi:10.1038/nature03242 · Cited by 516 · cited 2× · see citing works
“…to chromatin, but in these instances the enzymatic activity resides within the methyl-binding protein: JMJD2A is a histone lysine demethylase that binds via a tudor domain and CHD1 is an ATPase that binds via a chromodomain (Huang et al., 2006; Pray-Grant et al., 2005; Sims et al., 2005).”
Bannister, A. J., & Kouzarides, T. (2005) · Nature · doi:10.1038/nature04048 · Cited by 503 · cited 2× · see citing works
“Converting citrulline to arginine has not been described, although citrulline is cyclic on the pS2 promoter, so reversal may be possible (Bannister and Kouzarides, 2005).”
Self-citationTudor, MBT and chromo domains gauge the degree of lysine methylation
Kim, J., Daniel, J. A., Espejo, A. B., Lake, A., Krishna, M., Li, X., Zhang, Y., & Bedford, M. T. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400625 · Cited by 493 · cited 1× · see citing works
“The JMJD2A lysine demethylase has been demonstrated to bind H3K20me (Huang et al., 2006; Kim et al., 2006) via a tudor domain.”
Single-Nucleosome Mapping of Histone Modifications in S. cerevisiae
Liu, C. L., Kaplan, T., Kim, M., Buratowski, S., Schreiber, S. L., Friedman, N., & Rando, O. J. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0030328 · Cited by 491 · cited 4× · see citing works
“Most of the information we have has come from global analyses in budding yeast (Liu et al., 2005; Pokholok et al., 2005).”
InfluentialRole of Protein Methylation in Regulation of Transcription
Lee, D. Y., Teyssier, C., Strahl, B. D., & Stallcup, M. R. (2005) · Endocrine Reviews · doi:10.1210/er.2004-0008 · Cited by 454 · cited 3× · see citing works
“Like lysine methylation, arginine methylation can be either activatory or repressive for Cell 128, 693–705, February 23, 2007 ª2007 Elsevier Inc. 699 transcription, and the enzymes (protein arginine methyltransferases, PRMT’s) are recruited to promoters by transcription factors (Lee et al., 2005b).”
Recognition of Histone H3 Lysine-4 Methylation by the Double Tudor Domain of JMJD2A
Huang, Y., Fang, J., Bedford, M. T., Zhang, Y., & Xu, R.-M. (2006) · Science · doi:10.1126/science.1125162 · Cited by 446 · cited 3× · see citing works
“…to chromatin, but in these instances the enzymatic activity resides within the methyl-binding protein: JMJD2A is a histone lysine demethylase that binds via a tudor domain and CHD1 is an ATPase that binds via a chromodomain (Huang et al., 2006; Pray-Grant et al., 2005; Sims et al., 2005).”
Yeast Rtt109 Promotes Genome Stability by Acetylating Histone H3 on Lysine 56
Driscoll, R., Hudson, A., & Jackson, S. P. (2007) · Science · doi:10.1126/science.1135862 · Cited by 439 · cited 2× · see citing works
“A yeast protein SPT10 may be mediating acetylation of H3K56 at the promoters of histone genes to regulate gene expression (Xu et al., 2005), whereas the Rtt109 acetyltransferase mediates this modification more globally (Han et al., 2007; Driscoll et al., 2007; Schneider et al., 2006).”
Sims, R. J., Chen, C.-F., Santos-Rosa, H., Kouzarides, T., Patel, S. S., & Reinberg, D. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500395200 · Cited by 423 · cited 2× · see citing works
“…to chromatin, but in these instances the enzymatic activity resides within the methyl-binding protein: JMJD2A is a histone lysine demethylase that binds via a tudor domain and CHD1 is an ATPase that binds via a chromodomain (Huang et al., 2006; Pray-Grant et al., 2005; Sims et al., 2005).”
Self-citationRtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication
Han, J., Zhou, H., Horazdovsky, B. F., Zhang, K., Xu, R.-M., & Zhang, Z. (2007) · Science · doi:10.1126/science.1133234 · Cited by 421 · cited 3× · see citing works
“A yeast protein SPT10 may be mediating acetylation of H3K56 at the promoters of histone genes to regulate gene expression (Xu et al., 2005), whereas the Rtt109 acetyltransferase mediates this modification more globally (Han et al., 2007; Driscoll et al., 2007; Schneider et al., 2006).”
Structural Insights into Histone Demethylation by JMJD2 Family Members
Chen, Z., Zang, J., Whetstine, J. R., Hong, X., Davrazou, F., Kutateladze, T. G., Simpson, M., Mao, Q., Pan, C., Dai, S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.04.024 · Cited by 396 · cited 5× · see citing works
“Thirdly, the catalytic activity of an enzyme could be compromised by modification of its substrate recognition site; for example, isomerization of H3P38 affects methylation of H3K36 by Set2 (Nelson et al., 2006).”
InfluentialAcetylation 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 · cited 2× · see citing works
“A yeast protein SPT10 may be mediating acetylation of H3K56 at the promoters of histone genes to regulate gene expression (Xu et al., 2005), whereas the Rtt109 acetyltransferase mediates this modification more globally (Han et al., 2007; Driscoll et al., 2007; Schneider et al., 2006).”
Tethering RITS to a Nascent Transcript Initiates RNAi- and Heterochromatin-Dependent Gene Silencing
Bühler, M., Verdel, A., & Moazed, D. (2006) · Cell · doi:10.1016/j.cell.2006.04.025 · Cited by 382 · cited 1× · see citing works
“Small RNAs may emanate from many loci in the genome and once transmitted to the next generation, these RNAs may deliver chromatin-modifying complexes to specific genes or to specific locations, thus generating the pattern of chromatin that we observe (Verdel et al., 2004; Buhler et al., 2006).”
Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cellsPreprint
Fodor, B. D., Kubicek, S., Yonezawa, M., O’Sullivan, R. J., Sengupta, R., Perez-Burgos, L., Opravil, S., Mechtler, K., Schotta, G., & Jenuwein, T. (2006) · Genes & Development · doi:10.1101/gad.388206 · Cited by 376 · cited 2× · see citing works
“H3K9 can also be demethylated by JHDM2A (Yamane et al., 2006), JMJD2A/JHDM3A (Tsukada et al., 2006; Whetstine et al., 2006), JMJD2B (Fodor et al., 2006), JMJD2C/GASC1 (Cloos et al., 2006), and JMJD2D (Shin and Janknecht, 2006).”
Dai, J., Sultan, S., Taylor, S. S., & Higgins, J. M. G. (2005) · Genes & Development · doi:10.1101/gad.1267105 · Cited by 374 · cited 2× · see citing works
“The study of such pathways is less detailed, but examples include H3K4me disrupting the binding of the NuRD complex and H3T3ph preventing the binding of the INHAT complex.”
Nathan, D., Ingvarsdottir, K., Sterner, D. E., Bylebyl, G. R., Dokmanovic, M., Dorsey, J. A., Whelan, K. A., Krsmanovic, M. L., Lane, W. S., Meluh, P. B., et al. (2006) · Genes & Development · doi:10.1101/gad.1404206 · Cited by 345 · cited 12× · see citing works
“In contrast, H2BK120 ubiquitylation is mediated by human RNF20/RNF40 and UbcH6 and in budding yeast by Rad6/Bre1 and is activatory for transcription (Zhu et al., 2005).”
InfluentialMolecular regulation of H3K4 trimethylation by ASH2L, a shared subunit of MLL complexes
Steward, M., Lee, J., O’Donovan, A., Wyatt, M., Bernstein, B., & Shilatifard, A. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1131 · Cited by 325 · cited 2× · see citing works
“…are found may specify a preference for nucleosomal verses free histones (Lee et al., 2005a); proteins that associate with the enzyme may affect its selection of residue to modify (Metzger et al., 2005) or the degree of methylation (mono-, di-, or tri-) at a specific site (Steward et al., 2006).”
Proline Isomerization of Histone H3 Regulates Lysine Methylation and Gene Expression
Nelson, C. J., Santos-Rosa, H., & Kouzarides, T. (2006) · Cell · doi:10.1016/j.cell.2006.07.026 · Cited by 320 · cited 5× · see citing works
“Thirdly, the catalytic activity of an enzyme could be compromised by modification of its substrate recognition site; for example, isomerization of H3P38 affects methylation of H3K36 by Set2 (Nelson et al., 2006).”
InfluentialSelf-citationCelic, I., Masumoto, H., Griffith, W. P., Meluh, P. B., Cotter, R. J., Boeke, J. D., & Verreault, A. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.023 · Cited by 291 · cited 1× · see citing works
“However, in the presence of DNA damage the deacetylases for H3K56, Hst3, and Hst4 (two paralogs of Sir2) are downregulated and the modification persists (Celic et al., 2006; Maas et al., 2006).”
Genome-wide patterns of histone modifications in yeast
Millar, C. B., & Grunstein, M. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1986 · Cited by 286 · cited 2× · see citing works
“Certain common features have come to light regarding the composition and enrichment of modifications on actively transcribed genes: acetylation is enriched at specific sites in the promoter and 50 end of the coding regions; within the promoter there are two nucleosomes flanking the initiation site that are hypoacetyla…”
Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3.
Macdonald, N., Welburn, J., Noble, M., Nguyen, A., Yaffe, M., Clynes, D., Moggs, J., Orphanides, G., Thomson, S., Edmunds, J. W., et al. (2005) · Molecules and Cells · doi:10.1016/j.molcel.2005.08.032 · Cited by 282 · cited 1× · see citing works
“Concomitant with this phosphorylation is the appearance on chromatin of a phosphor-binding protein 14-3-3 (Macdonald et al., 2005).”
Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeastPreprint
Millar, C. B., Xu, F., Zhang, K., & Grunstein, M. R. (2006) · Genes & Development · doi:10.1101/gad.1395506 · Cited by 276 · cited 2× · see citing works
“…that are hypoacetylated at certain lysines and are enriched in the H2A variant Hzt1 (Liu et al., 2005; Zhang et al., 2005; Raisner et al., 2005; Millar et al., 2006; Millar and Grunstein, 2006); the initiation site itself is devoid of nucleosomes; lysine trimethylation is enriched in the…”
Chromatin regulates origin activity in Drosophila follicle cells
Aggarwal, B. D., & Calvi, B. R. (2004) · Nature · doi:10.1038/nature02694 · Cited by 275 · cited 1× · see citing works
“In Drosophila, the HB01 homolog, Chameau, is found to increase the firing of replication origins (Aggarwal and Calvi, 2004).”
Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex
Ruthenburg, A. J., Wang, W., Graybosch, D. M., Li, H., Allis, C. D., Patel, D. J., & Verdine, G. L. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1119 · Cited by 261 · cited 2× · see citing works
“provides an adaptor function, augmenting the recognition of H3K4me (Ruthenburg et al., 2006).”
Ahn, S.-H., Cheung, W. L., Hsu, J.-Y., Diaz, R. L., Smith, M. M., & Allis, C. D. (2005) · Cell · doi:10.1016/j.cell.2004.11.016 · Cited by 259 · cited 2× · see citing works
“Phosphorylation of H4S1 regulates sporulation (Krishnamoorthy et al., 2006), and phosphorylation of H2BS10 regulates peroxide-induced apoptosis (Ahn et al., 2005).”
Molecular recognition of histone H3 by the WD40 protein WDR5
Couture, J., Collazo, E., & Trievel, R. C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1116 · Cited by 256 · cited 1× · see citing works
“However, structural analysis of this interaction does not support a purely methyl-recognitionbased interaction but suggests that this protein binds most avidly to the residues preceding H3K4 and in particular to H3R2 (Couture et al., 2006).”
DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2APreprint
Bergink, S., Salomons, F. A., Hoogstraten, D., Groothuis, T. A., de Waard, H., Wu, J., Li, Y., Citterio, E., Houtsmuller, A. B., Neefjes, J., et al. (2006) · Genes & Development · doi:10.1101/gad.373706 · Cited by 247 · cited 1× · see citing works
“Monoubiquitylation of H2A is also implicated in UV-induced repair (Bergink et al., 2006).”
Activated Signal Transduction Kinases Frequently Occupy Target Genes
Pokholok, D., Zeitlinger, J., Hannett, N. M., Reynolds, D. B., & Young, R. A. (2006) · Science · doi:10.1126/science.1127677 · Cited by 244 · cited 1× · see citing works
“Recently, a global ChIP on CHIP analysis of many kinases in budding yeast has shown that they are present on the chromatin of specific genes (Pokholok et al., 2006).”
Cell Cycle and Checkpoint Regulation of Histone H3 K56 Acetylation by Hst3 and Hst4
Maas, N. L., Miller, K. M., DeFazio, L. G., & Toczyski, D. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.006 · Cited by 237 · cited 1× · see citing works
“However, in the presence of DNA damage the deacetylases for H3K56, Hst3, and Hst4 (two paralogs of Sir2) are downregulated and the modification persists (Celic et al., 2006; Maas et al., 2006).”
Rtt109 Is Required for Proper H3K56 Acetylation
Schneider, J., Bajwa, P., Johnson, F. C., Bhaumik, S. R., & Shilatifard, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600265200 · Cited by 209 · cited 3× · see citing works
“A yeast protein SPT10 may be mediating acetylation of H3K56 at the promoters of histone genes to regulate gene expression (Xu et al., 2005), whereas the Rtt109 acetyltransferase mediates this modification more globally (Han et al., 2007; Driscoll et al., 2007; Schneider et al., 2006).”
Maček, B., Waanders, L. F., Olsen, J. V., & Mann, M. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t500042-mcp200 · Cited by 198 · cited 2× · see citing works
“New methodology that uses a top-down proteomics approach (identify protein first and digest subsequently) gives promise that we may, in the future, look at the intact modification pattern of different histones in a given nucleosome ( Macek et al., 2006 ).”
Regulation of Replication Licensing by Acetyltransferase Hbo1
Iizuka, M., Matsui, T., Takisawa, H., & Smith, M. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.3.1098-1108.2006 · Cited by 198 · cited 1× · see citing works
“In a separate study HB01 is shown to augment the assembly of the pre-replicative complex and the recruitment of MCMs to chromatin (Iizuka et al., 2006).”
Fillingham, J., Keogh, M., & Krogan, N. J. (2006) · Biochemistry and Cell Biology · doi:10.1139/o06-072 · Cited by 190 · cited 1× · see citing works
“One of the earliest recognized responses to DNA damage is the phosphorylation of the histone variant g-H2AX in mammalian cells (Fillingham et al., 2006).”
Emre, N. C. T., Ingvarsdottir, K., Wyce, A., Wood, A., Krogan, N. J., Henry, K. W., Li, K., Marmorstein, R., Greenblatt, J., Shilatifard, A., et al. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.007 · Cited by 178 · cited 1× · see citing works
“The Ubp10 deubiquitylase functions in transcriptional silencing at heterochromatic sites in budding yeast (Emre et al., 2005; Gardner et al., 2005).”
Gardner, R. G., Nelson, Z. W., & Gottschling, D. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.14.6123-6139.2005 · Cited by 165 · cited 1× · see citing works
“The Ubp10 deubiquitylase functions in transcriptional silencing at heterochromatic sites in budding yeast (Emre et al., 2005; Gardner et al., 2005).”
Structural Basis for Histone and Phosphohistone Binding by the GCN5 Histone Acetyltransferase
Clements, A. M., Poux, A. N., Lo, W., Pillus, L., Berger, S. L., & Marmorstein, R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00288-0 · Cited by 156 · cited 6× · see citing works
“A role for H3S10 phosphorylation has been demonstrated for the activation of NFKB-regulated genes and also ‘‘immediate early’’ genes such as c-fos and c-jun.”
InfluentialPhosphorylation of Histone H4 Serine 1 during DNA Damage Requires Casein Kinase II in S. cerevisiae
Cheung, W. L., Turner, F. B., Krishnamoorthy, T., Wolner, B. S., Ahn, S.-H., Foley, M., Dorsey, J. A., Peterson, C. L., Berger, S. L., & Allis, C. D. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.049 · Cited by 154 · cited 1× · see citing works
“Two phosphorylation sites on this histone have a role in doublestrand break repair via nonhomologous end joining: H2AS129 mediated by Mec1 (Downs et al., 2000) and H4S1 mediated by Caesin kinase II (Cheung et al., 2005).”
Diversity within the JMJD2 histone demethylase family
Shin, S., & Janknecht, R. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.12.147 · Cited by 142 · cited 1× · see citing works
“H3K9 can also be demethylated by JHDM2A (Yamane et al., 2006), JMJD2A/JHDM3A (Tsukada et al., 2006; Whetstine et al., 2006), JMJD2B (Fodor et al., 2006), JMJD2C/GASC1 (Cloos et al., 2006), and JMJD2D (Shin and Janknecht, 2006).”
Du, L.-L., Nakamura, T., & Russell, P. R. (2006) · Genes & Development · doi:10.1101/gad.1422606 · Cited by 141 · cited 2× · see citing works
“This phosphor-binding domain may recognize the DNA-damage-induced phosphorylation site and then stabilize itself on chromatin via the recognition of H4K20me ( Du et al., 2006 ).”
Krishnamoorthy, T., Chen, X., Govin, J., Cheung, W. L., Dorsey, J. A., Schindler, K., Winter, E., Allis, C. D., Guacci, V., Khochbin, S., et al. (2006) · Genes & Development · doi:10.1101/gad.1457006 · Cited by 120 · cited 3× · see citing works
“Phosphorylation of H4S1 regulates sporulation (Krishnamoorthy et al., 2006), and phosphorylation of H2BS10 regulates peroxide-induced apoptosis (Ahn et al., 2005).”
Qin, S., & Parthun, M. R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.9.3649-3658.2006 · Cited by 72 · cited 1× · see citing works
“This enzyme is recruited to sites of DNA repair and acetylates H4K12 (Qin and Parthun, 2006).”
Hidaka, Y., Hagiwara, T., & Yamada, M. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.06.035 · Cited by 53 · cited 1× · see citing works
“In vitro analysis of the PADI4 enzyme suggests that the reversal of monomethyl arginine to citrulline is not carried out by the recombinant enzyme when methylated peptides are used as substrates, suggesting that a cofactor may be necessary in vivo (Hidaka et al., 2005).”
Centromere DNA, proteins and kinetochore assembly in vertebrate cells
Fukagawa, T. (2004) · Chromosome Research · doi:10.1023/b:chro.0000036590.96208.83 · Cited by 31 · cited 9× · see citing works
“The dogma, that H3K9 methylation and HP1 recruitment are always repressive, has recently been challenged by the finding that H3K9me3 and the g isoform of HP1 are enriched in the coding region of active genes (Vakoc et al., 2005).”
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Classification of Intrinsically Disordered Regions and Proteins
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The NIH Roadmap Epigenomics Mapping Consortium
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Self-citationWriting, erasing and reading histone lysine methylations
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- Authors
- Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Kouzarides, Tony
- ORCID
- Kouzarides, Tony
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2007-02
- Volume
- 128
- Issue
- 4
- Pages
- 693-705
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2096083625
- Cited by
- 10,883
- References
- 91
- Citations by year
- 2026: 260 · 2025: 374 · 2024: 387 · 2023: 414 · 2022: 472 · 2021: 616 · 2020: 561 · 2019: 578 · 2018: 530 · 2017: 624 · 2016: 679 · 2015: 664 · 2014: 733 · 2013: 686 · 2012: 796
- FWCI
- 45.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- 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, chromatin modification, nucleosome, chromatin structure, epigenetic inheritance, chromatin remodeling
- MeSH terms
- Animals, DNA, Enzymes, Histones, Humans, Nucleosomes, Protein Processing, Post-Translational, Chromatin Assembly and Disassembly, Epigenesis, Genetic
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