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Journal articles on the topic 'Histone acetylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Chicoine, L. G., R. Richman, R. G. Cook, M. A. Gorovsky, and C. D. Allis. "A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones." Journal of Cell Biology 105, no. 1 (1987): 127–35. http://dx.doi.org/10.1083/jcb.105.1.127.

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A salt-extracted histone acetyltransferase activity from Tetrahymena macronuclei acetylates mostly histone H3 and H4 when free histones are used as substrate. Free histone H4 is acetylated first at position 11 (monoacetylated) or positions 11 and 4 (diacetylated). This activity strongly resembles in vivo, deposition-related acetylation of newly synthesized histones. When acetylase-free mononucleosomes are used as substrate, all four core histones are acetylated by the same extract, and H4 is acetylated first at position 7 (monoacetylated) or positions 7 and 4 (diacetylated). In this respect, t

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2

Cuevas-Bennett, Christian, and Thomas Shenk. "Dynamic Histone H3 Acetylation and Methylation at Human Cytomegalovirus Promoters during Replication in Fibroblasts." Journal of Virology 82, no. 19 (2008): 9525–36. http://dx.doi.org/10.1128/jvi.00946-08.

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ABSTRACT Human cytomegalovirus DNA is packaged in virions without histones but associates with histones upon reaching the nucleus of an infected cell. Since transcription is modulated by the interplay of histone modifications, we used chromatin immunoprecipitation to detect acetylation and methylation of histone H3 at viral promoters at different times during the viral replication cycle. Histone H3 at immediate-early promoters is acetylated at the start of infection, while it is initially methylated at early and late promoters. Acetylation at immediate-early promoters is dynamic, with a high l

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Legartová, Soňa, Stanislav Kozubek, Michal Franek, et al. "Cell differentiation along multiple pathways accompanied by changes in histone acetylation status." Biochemistry and Cell Biology 92, no. 2 (2014): 85–93. http://dx.doi.org/10.1139/bcb-2013-0082.

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Post-translational modification of histones is fundamental to the regulation of basic nuclear processes and subsequent cellular events, including differentiation. In this study, we analyzed acetylated forms of histones H2A, H2B, and H4 during induced differentiation in mouse (mESCs) and human (hESCs) embryonic stem cells and during induced enterocytic differentiation of colon cancer cells in vitro. Endoderm-like differentiation of mESCs induced by retinoic acid and enterocytic differentiation induced by histone deacetylase inhibitor sodium butyrate were accompanied by increased mono-, di-, and

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4

Kring, Friedhelm, and Peter Böger. "Histone Acetylation is not Affected by Chloroacetamides in vitro." Zeitschrift für Naturforschung C 49, no. 5-6 (1994): 309–11. http://dx.doi.org/10.1515/znc-1994-5-605.

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Abstract The effects of chloroacetamides on the acetylation of histone protein in maize (Zea mays) were studied in an in vitro assay. Neither alachlor nor metazachlor showed any influence on both of the investigated acetylating enzymes, the nuclear histone acetyltransferase A and the cytoplasmic histone acetyltransferase B. Furthermore, an effect of these herbicides on deacetylation of histones could be excluded.

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Waterborg, Jakob H., and Tamás Kapros. "Kinetic analysis of histone acetylation turnover and Trichostatin A induced hyper- and hypoacetylation in alfalfa." Biochemistry and Cell Biology 80, no. 3 (2002): 279–93. http://dx.doi.org/10.1139/o02-021.

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Dynamic histone acetylation is a characteristic of chromatin transcription. The first estimates for the rate of acetylation turnover of plants are reported, measured in alfalfa cells by pulse, pulse-chase, and steady-state acetylation labeling. Acetylation turnover half-lives of about 0.5 h were observed by all methods used for histones H3, H4, and H2B. This is consistent with the rate at which changes in gene expression occur in plants. Treatment with histone deacetylase inhibitor Trichostatin A (TSA) induced hyperacetylation at a similar rate. Replacement histone variant H3.2, preferentially

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Demyanenko, Svetlana, and Svetlana Sharifulina. "The Role of Post-Translational Acetylation and Deacetylation of Signaling Proteins and Transcription Factors after Cerebral Ischemia: Facts and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (2021): 7947. http://dx.doi.org/10.3390/ijms22157947.

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Histone deacetylase (HDAC) and histone acetyltransferase (HAT) regulate transcription and the most important functions of cells by acetylating/deacetylating histones and non-histone proteins. These proteins are involved in cell survival and death, replication, DNA repair, the cell cycle, and cell responses to stress and aging. HDAC/HAT balance in cells affects gene expression and cell signaling. There are very few studies on the effects of stroke on non-histone protein acetylation/deacetylation in brain cells. HDAC inhibitors have been shown to be effective in protecting the brain from ischemi

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Deckert, Jutta, and Kevin Struhl. "Histone Acetylation at Promoters Is Differentially Affected by Specific Activators and Repressors." Molecular and Cellular Biology 21, no. 8 (2001): 2726–35. http://dx.doi.org/10.1128/mcb.21.8.2726-2735.2001.

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ABSTRACT We analyzed the relationship between histone acetylation and transcriptional regulation at 40 Saccharomyces cerevisiaepromoters that respond to specific activators and repressors. In accord with the general correlation between histone acetylation and transcriptional activity, Gcn4 and the general stress activators (Msn2 and Msn4) cause increased acetylation of histones H3 and H4. Surprisingly, Gal4-dependent activation is associated with a dramatic decrease in histone H4 acetylation, whereas acetylation of histone H3 is unaffected. A specific decrease in H4 acetylation is also observe

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Ito, Takashi, Tsuyoshi Ikehara, Takeya Nakagawa, W. Lee Kraus, and Masami Muramatsu. "p300-Mediated acetylation facilitates the transfer of histone H2A–H2B dimers from nucleosomes to a histone chaperone." Genes & Development 14, no. 15 (2000): 1899–907. http://dx.doi.org/10.1101/gad.14.15.1899.

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We have used a purified recombinant chromatin assembly system, including ACF (Acf-1 + ISWI) and NAP-1, to examine the role of histone acetylation in ATP-dependent chromatin remodeling. The binding of a transcriptional activator (Gal4–VP16) to chromatin assembled using this recombinant assembly system dramatically enhances the acetylation of nucleosomal core histones by the histone acetyltransferase p300. This effect requires both the presence of Gal4-binding sites in the template and the VP16-activation domain. Order-of-addition experiments indicate that prior activator-meditated, ATP-dependen

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Abaturov, O. E., and A. O. Nikulina. "Histones post-translational modifications associated with the development of metabolic dysfunction-associated fatty liver disease. Part 3. Histon acetylation." GASTROENTEROLOGY 59, no. 1 (2025): 56–67. https://doi.org/10.22141/2308-2097.59.1.2025.664.

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Based on the analysis of literature sources from the Pubmed, MEDLINE, The Cochrane Library, Embase databases, the authors of the article highlight general provisions regarding histone acetylation. They emphasize that it is acetylation of the lysine residue that is the key post-translational modification of histones by epigenetic mechanisms of gene expression regulation. To date, at least 2000 human proteins have been identified that can be modified at lysine residues by acetylation. About 1000 proteins in human liver tissue undergo modification by lysine acetylation. Acetylation is mediated by

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10

CraneRobinson, Colyn. "Playing tag: Histone acetylation." Biochemist 29, no. 4 (2007): 9–13. http://dx.doi.org/10.1042/bio02904009.

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Acetylation of the e-amino group of specific lysine residues of core histones – principally but not exclusively in their unstructured N-terminal tails – is a key biochemical modification for establishing the transcriptional competence of genes bound by such histones. High resolution mapping of acetylated core histones by chromatin IPs (ChIPs) has shown them to be preferentially located at the promoters and enhancers of active genes rather than throughout the transcribed regions. Particular distributions of acetylated lysines are part of the nucleosomal ‘histone code’ that defines and to a cons

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11

Jiang, Lihua, Jonell N. Smith, Shannon L. Anderson, Ping Ma, Craig A. Mizzen, and Neil L. Kelleher. "Global Assessment of Combinatorial Post-translational Modification of Core Histones in Yeast Using Contemporary Mass Spectrometry." Journal of Biological Chemistry 282, no. 38 (2007): 27923–34. http://dx.doi.org/10.1074/jbc.m704194200.

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A global view of all core histones in yeast is provided by tandem mass spectrometry of intact histones H2A, H2B, H4, and H3. This allowed detailed characterization of >50 distinct histone forms and their semiquantitative assessment in the deletion mutants gcn5Δ, spt7Δ, ahc1Δ, and rtg2Δ, affecting the chromatin remodeling complexes SAGA, SLIK, and ADA. The “top down” mass spectrometry approach detected dramatic decreases in acetylation on H3 and H2B in gcn5Δ cells versus wild type. For H3 in wild type cells, tandem mass spectrometry revealed a direct correlation between increases of Lys4 tri

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12

Herrera, Julio E., Katherine L. West, R. Louis Schiltz, Yoshihiro Nakatani, and Michael Bustin. "Histone H1 Is a Specific Repressor of Core Histone Acetylation in Chromatin." Molecular and Cellular Biology 20, no. 2 (2000): 523–29. http://dx.doi.org/10.1128/mcb.20.2.523-529.2000.

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ABSTRACT Although a link between histone acetylation and transcription has been established, it is not clear how acetylases function in the nucleus of the cell and how they access their targets in a chromatin fiber containing H1 and folded into a highly condensed structure. Here we show that the histone acetyltransferase (HAT) p300/CBP-associated factor (PCAF), either alone or in a nuclear complex, can readily acetylate oligonucleosomal substrates. The linker histones, H1 and H5, specifically inhibit the acetylation of mono- and oligonucleosomes and not that of free histones or histone-DNA mix

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13

Adimulam, Theolan, Thilona Arumugam, Ashmika Foolchand, Terisha Ghazi, and Anil A. Chuturgoon. "The Effect of Organoselenium Compounds on Histone Deacetylase Inhibition and Their Potential for Cancer Therapy." International Journal of Molecular Sciences 22, no. 23 (2021): 12952. http://dx.doi.org/10.3390/ijms222312952.

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Genetic and epigenetic changes alter gene expression, contributing to cancer. Epigenetic changes in cancer arise from alterations in DNA and histone modifications that lead to tumour suppressor gene silencing and the activation of oncogenes. The acetylation status of histones and non-histone proteins are determined by the histone deacetylases and histone acetyltransferases that control gene transcription. Organoselenium compounds have become promising contenders in cancer therapeutics. Apart from their anti-oxidative effects, several natural and synthetic organoselenium compounds and metabolit

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14

Hendzel, M. J., and J. R. Davie. "Dynamically acetylated histones of chicken erythrocytes are selectively methylated." Biochemical Journal 273, no. 3 (1991): 753–58. http://dx.doi.org/10.1042/bj2730753.

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The relationship between histone acetylation and methylation in chicken immature erythrocytes was investigated. Previous studies have shown that transcriptionally active/competent gene-enriched chromatin fragments are enriched in newly methylated histones H3 and H4. Moreover, newly methylated histone H4 is hyperacetylated. Here, we show that dynamically acetylated histone H4 is selectively engaged in ongoing methylation. While sodium butyrate (an inhibitor of histone deacetylase) does not inhibit ongoing histone methylation, it does affect the acetylation state of newly methylated histone H4 w

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15

Choi, Jennifer K., and LeAnn J. Howe. "Histone acetylation: truth of consequences?This paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 87, no. 1 (2009): 139–50. http://dx.doi.org/10.1139/o08-112.

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Eukaryotic DNA is packaged into a nucleoprotein structure known as chromatin, which is comprised of DNA, histones, and nonhistone proteins. Chromatin structure is highly dynamic, and can shift from a transcriptionally inactive state to an active form in response to intra- and extracellular signals. A major factor in chromatin architecture is the covalent modification of histones through the addition of chemical moieties, such as acetyl, methyl, ubiquitin, and phosphate groups. The acetylation of the amino-terminal tails of histones is a process that is highly conserved in eukaryotes, and was o

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Endo, Tsutomu, Aoi Imai, Takuma Shimaoka, Kiyoshi Kano, and Kunihiko Naito. "Histone exchange activity and its correlation with histone acetylation status in porcine oocytes." REPRODUCTION 141, no. 4 (2011): 397–405. http://dx.doi.org/10.1530/rep-10-0164.

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In mammalian oocytes, histone H3 and histone H4 (H4) in the chromatin are highly acetylated at the germinal vesicle (GV) stage, and become globally deacetylated after GV breakdown (GVBD). Although nuclear core histones can be exchanged by cytoplasmic free histones in somatic cells, it remains unknown whether this is also the case in mammalian oocytes. In this study, we examined the histone exchange activity in maturing porcine oocytes before and after GVBD, and investigated the correlations between this activity and both the acetylation profile of the H4 N-terminal tail and the global histone

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Johnson, Kristen, Cristina Angelin-Duclos, Sinae Park, and Kathryn L. Calame. "Changes in Histone Acetylation Are Associated with Differences in Accessibility of VH Gene Segments to V-DJ Recombination during B-Cell Ontogeny and Development." Molecular and Cellular Biology 23, no. 7 (2003): 2438–50. http://dx.doi.org/10.1128/mcb.23.7.2438-2450.2003.

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ABSTRACT Although V(D)J recombination is thought to be regulated by changes in the accessibility of chromatin to the recombinase machinery, the mechanisms responsible for establishing “open” chromatin are poorly understood. We performed a detailed study of the acetylation status of histones associated with 11 VH gene segments, their flanking regions, and various intergenic elements during B-cell development and ontogeny, when V(D)J recombination is highly regulated. Histone H4 shows higher and more-regulated acetylation than does histone H3 in the VH locus. In adult pro-B cells, VH gene segmen

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18

Swaminathan, V., A. Hari Kishore, K. K. Febitha, and Tapas K. Kundu. "Human Histone Chaperone Nucleophosmin Enhances Acetylation-Dependent Chromatin Transcription." Molecular and Cellular Biology 25, no. 17 (2005): 7534–45. http://dx.doi.org/10.1128/mcb.25.17.7534-7545.2005.

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ABSTRACT Histone chaperones are a group of proteins that aid in the dynamic chromatin organization during different cellular processes. Here, we report that the human histone chaperone nucleophosmin interacts with the core histones H3, H2B, and H4 but that this histone interaction is not sufficient to confer the chaperone activity. Significantly, nucleophosmin enhances the acetylation-dependent chromatin transcription and it becomes acetylated both in vitro and in vivo. Acetylation of nucleophosmin and the core histones was found to be essential for the enhancement of chromatin transcription.

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Cote, Joy M., Yin-Ming Kuo, Ryan A. Henry, Hataichanok Scherman, Daniel D. Krzizike, and Andrew J. Andrews. "Two factor authentication: Asf1 mediates crosstalk between H3 K14 and K56 acetylation." Nucleic Acids Research 47, no. 14 (2019): 7380–91. http://dx.doi.org/10.1093/nar/gkz508.

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Abstract The ability of histone chaperone Anti-silencing factor 1 (Asf1) to direct acetylation of lysine 56 of histone H3 (H3K56ac) represents an important regulatory step in genome replication and DNA repair. In Saccharomyces cerevisiae, Asf1 interacts functionally with a second chaperone, Vps75, and the lysine acetyltransferase (KAT) Rtt109. Both Asf1 and Vps75 can increase the specificity of histone acetylation by Rtt109, but neither alter selectivity. However, changes in acetylation selectivity have been observed in histones extracted from cells, which contain a plethora of post-translatio

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20

Friis, R. Magnus N., and Michael C. Schultz. "Untargeted tail acetylation of histones in chromatin: lessons from yeastThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB’s 51st Annual Meeting – Epigenetics and Chromatin Dynamics, and has undergone the Journal’s usual peer review process." Biochemistry and Cell Biology 87, no. 1 (2009): 107–16. http://dx.doi.org/10.1139/o08-097.

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Dynamic acetylation of lysine residues in the amino-terminal tails of the core histones is functionally important for the regulation of diverse DNA-dependent processes in the nucleus, including replication, transcription, and DNA repair. The targeted and untargeted activities of histone lysine acetylases (KATs) and deacetylases (HDACs) both contribute to the dynamics of chromatin acetylation. While the mechanisms and functional consequences of targeted on histone acetylation are well understood, relatively little is known about untargeted histone acetylation. Here, we review the current unders

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Miziak, Paulina, Marzena Baran, Lidia Borkiewicz, Tomasz Trombik, and Andrzej Stepulak. "Acetylation of Histone H3 in Cancer Progression and Prognosis." International Journal of Molecular Sciences 25, no. 20 (2024): 10982. http://dx.doi.org/10.3390/ijms252010982.

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Cancer is a multifactorial disease resulting from both genetic factors and epigenetic changes. Histone acetylation, a post-translational modification, which alters chromatin architecture and regulates gene expression is associated with cancer initiation, development and progression. Aberrations in global histone acetylation levels are observed in various cancer cells and are also associated with patients’ tumor aggressiveness. Therefore, histone acetylation may have prognostic utility and serve as a potential biomarker of cancer progression and patients’ prognosis. The reversible modification

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Wang, Yonggang, Xiao Miao, Yucheng Liu, et al. "Dysregulation of Histone Acetyltransferases and Deacetylases in Cardiovascular Diseases." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/641979.

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Cardiovascular disease (CVD) remains a leading cause of mortality worldwide despite advances in its prevention and management. A comprehensive understanding of factors which contribute to CVD is required in order to develop more effective treatment options. Dysregulation of epigenetic posttranscriptional modifications of histones in chromatin is thought to be associated with the pathology of many disease models, including CVD. Histone acetyltransferases (HATs) and deacetylases (HDACs) are regulators of histone lysine acetylation. Recent studies have implicated a fundamental role of reversible

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Hamam, Hussein, Meraj Khan, and Nades Palaniyar. "Histone Acetylation Promotes Neutrophil Extracellular Trap Formation." Biomolecules 9, no. 1 (2019): 32. http://dx.doi.org/10.3390/biom9010032.

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Neutrophils undergo a unique form of cell death to generate neutrophil extracellular traps (NETs). It is well established that citrullination of histones (e.g., CitH3) facilitates chromatin decondensation during NET formation (NETosis), particularly during calcium-induced NETosis that is independent of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase (NOX) activation. However, the importance of other forms of histone modifications in NETosis has not been established. We considered that acetylation of histones would also facilitate NETosis. To test this hypothesis, we induced NOX-dep

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Loyola, Alejandra, Gary LeRoy, Yuh-Hwa Wang, and Danny Reinberg. "Reconstitution of recombinant chromatin establishes a requirement for histone-tail modifications during chromatin assembly and transcription." Genes & Development 15, no. 21 (2001): 2837–51. http://dx.doi.org/10.1101/gad.937401.

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The human ISWI-containing factor RSF (remodeling andspacing factor) was found to mediate nucleosome deposition and, in the presence of ATP, generate regularly spaced nucleosome arrays. Using this system, recombinant chromatin was reconstituted with bacterially produced histones. Acetylation of the histone tails was found to play an important role in establishing regularly spaced nucleosome arrays. Recombinant chromatin lacking histone acetylation was impaired in directing transcription. Histone-tail modifications were found to regulate transcription from the recombinant chromatin. Acetylation

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Bartl, S., J. Taplick, G. Lagger, H. Khier, K. Kuchler, and C. Seiser. "Identification of mouse histone deacetylase 1 as a growth factor-inducible gene." Molecular and Cellular Biology 17, no. 9 (1997): 5033–43. http://dx.doi.org/10.1128/mcb.17.9.5033.

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Reversible acetylation of core histones plays an important role in transcriptional regulation, cell cycle progression, and developmental events. The acetylation state of histones is controlled by the activities of acetylating and deacetylating enzymes. By using differential mRNA display, we have identified a mouse histone deacetylase gene, HD1, as an interleukin-2-inducible gene in murine T cells. Sequence alignments revealed that murine HD1 is highly homologous to the yeast RPD3 pleiotropic transcriptional regulator. Indirect immunofluorescence microscopy proved that mouse HD1 is a nuclear pr

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Weiss, G., H. Talasz, and B. Puschendorf. "Possible role of histone acetylation and histone H1° replacement for the initiation of replication in regenerating rat liver." Biochemical Journal 280, no. 3 (1991): 777–81. http://dx.doi.org/10.1042/bj2800777.

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The role of histone acetylation and DNA synthesis has been investigated extensively in the regenerating rat liver system in the presence and absence of the cyclophosphamide derivative mafosfamide. We demonstrate a mafosfamide-induced inhibition of maximum histone acetyltransferase activity followed by a second elevation of enzyme activity and an accompanying total suppression of DNA synthesis for 7-8 h. The maximum of histone acetyltransferase activity, in parallel with an elevated acetylation in vivo, the consecutive replacement of histone H1(0) amd initiation of replication occur sequentiall

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Barnes, Claire E., David M. English, and Shaun M. Cowley. "Acetylation & Co: an expanding repertoire of histone acylations regulates chromatin and transcription." Essays in Biochemistry 63, no. 1 (2019): 97–107. http://dx.doi.org/10.1042/ebc20180061.

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Abstract Packaging the long and fragile genomes of eukaryotic species into nucleosomes is all well and good, but how do cells gain access to the DNA again after it has been bundled away? The solution, in every species from yeast to man, is to post-translationally modify histones, altering their chemical properties to either relax the chromatin, label it for remodelling or make it more compact still. Histones are subject to a myriad of modifications: acetylation, methylation, phosphorylation, ubiquitination etc. This review focuses on histone acylations, a diverse group of modifications which o

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Harb, Hani, Bilal Alashkar Alhamwe, Nathalie Acevedo, et al. "Epigenetic Modifications in Placenta are Associated with the Child’s Sensitization to Allergens." BioMed Research International 2019 (April 17, 2019): 1–11. http://dx.doi.org/10.1155/2019/1315257.

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Prenatal environmental exposures are considered to contribute to the development of allergic sensitization by epigenetic mechanisms. The role of histone acetylation in the placenta has not been examined yet. We hypothesized that placental histone acetylation at the promoter regions of allergy-related immune regulatory genes is associated with the development of sensitization to allergens in the child. Histones H3 and H4 acetylation at the promoter regions of 6 selected allergy-related immune regulatory genes was assessed by a chromatin immunoprecipitation assay in 173 term placentas collected

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Lee, Yuri, Mi Hee Shin, Min-Kyoung Kim, et al. "Increased Histone Acetylation and Decreased Expression of Specific Histone Deacetylases in Ultraviolet-Irradiated and Intrinsically Aged Human Skin In Vivo." International Journal of Molecular Sciences 22, no. 4 (2021): 2032. http://dx.doi.org/10.3390/ijms22042032.

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Histone deacetylases (HDACs) are conserved enzymes that remove acetyl groups from lysine side chains in histones and other proteins and play a crucial role in epigenetic regulation. Previously, we showed that histone acetylation is implicated in ultraviolet (UV)-induced inflammation and matrix impairment. To elucidate the histone acetylation status and specific HDACs involved in skin aging, we examined the changes in histone acetylation, global HDAC activity, and the expression of HDACs and sirtuins (SIRTs) in intrinsically aged and photoaged human skin as well as in UV-irradiated human skin i

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Zhu, Liqian, Xinyi Jiang, Xiaotian Fu, Yanhua Qi, and Guoqiang Zhu. "The Involvement of Histone H3 Acetylation in Bovine Herpesvirus 1 Replication in MDBK Cells." Viruses 10, no. 10 (2018): 525. http://dx.doi.org/10.3390/v10100525.

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During bovine herpesvirus 1 (BoHV-1) productive infection in cell cultures, partial of intranuclear viral DNA is present in nucleosomes, and viral protein VP22 associates with histones and decreases histone H4 acetylation, indicating the involvement of histone H4 acetylation in virus replication. In this study, we demonstrated that BoHV-1 infection at the late stage (at 24 h after infection) dramatically decreased histone H3 acetylation [at residues K9 (H3K9ac) and K18 (H3K18ac)], which was supported by the pronounced depletion of histone acetyltransferases (HATs) including CBP/P300 (CREB bind

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Bertos, Nicholas R., Audrey H. Wang, and Xiang-Jiao Yang. "Class II histone deacetylases: Structure, function, and regulation." Biochemistry and Cell Biology 79, no. 3 (2001): 243–52. http://dx.doi.org/10.1139/o01-032.

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Acetylation of histones, as well as non-histone proteins, plays important roles in regulating various cellular processes. Dynamic control of protein acetylation levels in vivo occurs through the opposing actions of histone acetyltransferases and histone deacetylases (HDACs). In the past few years, distinct classes of HDACs have been identified in mammalian cells. Class I members, such as HDAC1, HDAC2, HDAC3, and HDAC8, are well-known enzymatic transcriptional corepressors homologous to yeast Rpd3. Class II members, including HDAC4, HDAC5, HDAC6, HDAC7, and HDAC9, possess domains similar to the

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Ge, Zhongqi, Devi Nair, Xiaoyan Guan, Neha Rastogi, Michael A. Freitas, and Mark R. Parthun. "Sites of Acetylation on Newly Synthesized Histone H4 Are Required for Chromatin Assembly and DNA Damage Response Signaling." Molecular and Cellular Biology 33, no. 16 (2013): 3286–98. http://dx.doi.org/10.1128/mcb.00460-13.

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The best-characterized acetylation of newly synthesized histone H4 is the diacetylation of the NH2-terminal tail on lysines 5 and 12. Despite its evolutionary conservation, this pattern of modification has not been shown to be essential for either viability or chromatin assembly in any model organism. We demonstrate that mutations in histone H4 lysines 5 and 12 in yeast confer hypersensitivity to replication stress and DNA-damaging agents when combined with mutations in histone H4 lysine 91, which has also been found to be a site of acetylation on soluble histone H4. In addition, these mutatio

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Calestagne-Morelli, Alison, and Juan Ausió. "Long-range histone acetylation: biological significance, structural implications, and mechanismsThis paper is one of a selection of papers published in this Special Issue, entitled 27th International West Coast Chromatin and Chromosome Conference, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 84, no. 4 (2006): 518–27. http://dx.doi.org/10.1139/o06-067.

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Genomic characterization of various euchromatic regions in higher eukaryotes has revealed that domain-wide hyperacetylation (over several kb) occurs at a range of loci, including individual genes, gene family clusters, compound clusters, and more general clusters of unrelated genes. Patterns of long-range histone hyperacetylation are strictly conserved within each unique cellular system studied and they reflect biological variability in gene regulation. Domain-wide histone acetylation consists generally of nonuniform peaks of enriched hyperacetylation of specific core histones, histone isoform

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Drury, Georgina E., Adam A. Dowle, David A. Ashford, Wanda M. Waterworth, Jerry Thomas, and Christopher E. West. "Dynamics of plant histone modifications in response to DNA damage." Biochemical Journal 445, no. 3 (2012): 393–401. http://dx.doi.org/10.1042/bj20111956.

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DNA damage detection and repair take place in the context of chromatin, and histone proteins play important roles in these events. Post-translational modifications of histone proteins are involved in repair and DNA damage signalling processes in response to genotoxic stresses. In particular, acetylation of histones H3 and H4 plays an important role in the mammalian and yeast DNA damage response and survival under genotoxic stress. However, the role of post-translational modifications to histones during the plant DNA damage response is currently poorly understood. Several different acetylated H

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Zhao, Youshan, Feng Xu, Juan Guo, Sida Zhao, Chunkang Chang, and Xiao Li. "Dysregulation of ANKRD11 Influenced Hematopoisis By Histone Acetylation-Mediated Gene Expression in Myelodysplastic Syndrome." Blood 128, no. 22 (2016): 4292. http://dx.doi.org/10.1182/blood.v128.22.4292.4292.

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Abstract Background and Object In addition to histone deacetylation, the importance of histone over-acetylation induced oncogene transcription in initiation and progression of myelodysplastic syndrome (MDS) has been proposed recently. Our previous whole-exome sequencing identified a new somatic mutation, ANKRD11, an important factor in histone acetylation regulation. Its roles in MDS pathophysiology need to be clarified. Methods The next generation target sequencing (Including ANKRD11) was carried out in 320 patients with MDS using the MiSeq Benchtop Sequencer. ANKRD11 mRNA expression in bone

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Tamburini, Beth A., and Jessica K. Tyler. "Localized Histone Acetylation and Deacetylation Triggered by the Homologous Recombination Pathway of Double-Strand DNA Repair." Molecular and Cellular Biology 25, no. 12 (2005): 4903–13. http://dx.doi.org/10.1128/mcb.25.12.4903-4913.2005.

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ABSTRACT Many recent studies have demonstrated recruitment of chromatin-modifying enzymes to double-strand breaks. Instead, we wanted to examine chromatin modifications during the repair of these double-strand breaks. We show that homologous recombination triggers the acetylation of N-terminal lysines on histones H3 and H4 flanking a double-strand break, followed by deacetylation of H3 and H4. Consistent with a requirement for acetylation and deacetylation during homologous recombination, Saccharomyces cerevisiae with substitutions of the acetylatable lysines of histone H4, deleted for the N-t

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Vermeulen, Michiel, Michael J. Carrozza, Edwin Lasonder, Jerry L. Workman, Colin Logie, and Hendrik G. Stunnenberg. "In Vitro Targeting Reveals Intrinsic Histone Tail Specificity of the Sin3/Histone Deacetylase and N-CoR/SMRT Corepressor Complexes." Molecular and Cellular Biology 24, no. 6 (2004): 2364–72. http://dx.doi.org/10.1128/mcb.24.6.2364-2372.2004.

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ABSTRACT The histone code is among others established via differential acetylation catalyzed by histone acetyltransferases (HATs) and histone deacetylases (HDACs). To unambiguously determine the histone tail specificity of HDAC-containing complexes, we have established an in vitro system consisting of nucleosomal templates reconstituted with hyperacetylated histones or recombinant histones followed by acetylation with native SAGA or NuA4. Selective targeting of the mammalian Sin3/HDAC and N-CoR/SMRT corepressor complexes by using specific chimeric repressors created a near physiological settin

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Alam, Shah, Antonia Piazzesi, Mariam Abd El Fatah, Maren Raucamp, and Gerhild van Echten-Deckert. "Neurodegeneration Caused by S1P-Lyase Deficiency Involves Calcium-Dependent Tau Pathology and Abnormal Histone Acetylation." Cells 9, no. 10 (2020): 2189. http://dx.doi.org/10.3390/cells9102189.

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We have shown that sphingosine 1-phosphate (S1P) generated by sphingosine kinase 2 (SK2) is toxic in neurons lacking S1P-lyase (SGPL1), the enzyme that catalyzes its irreversible cleavage. Interestingly, patients harboring mutations in the gene encoding this enzyme (SGPL1) often present with neurological pathologies. Studies in a mouse model with a developmental neural-specific ablation of SGPL1 (SGPL1fl/fl/Nes) confirmed the importance of S1P metabolism for the presynaptic architecture and neuronal autophagy, known to be essential for brain health. We now investigated in SGPL1-deficient murin

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Romhányi, Dóra, Kornélia Szabó, Lajos Kemény, and Gergely Groma. "Histone and Histone Acetylation-Related Alterations of Gene Expression in Uninvolved Psoriatic Skin and Their Effects on Cell Proliferation, Differentiation, and Immune Responses." International Journal of Molecular Sciences 24, no. 19 (2023): 14551. http://dx.doi.org/10.3390/ijms241914551.

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Psoriasis is a chronic immune-mediated skin disease in which the symptom-free, uninvolved skin carries alterations in gene expression, serving as a basis for lesion formation. Histones and histone acetylation-related processes are key regulators of gene expression, controlling cell proliferation and immune responses. Dysregulation of these processes is likely to play an important role in the pathogenesis of psoriasis. To gain a complete overview of these potential alterations, we performed a meta-analysis of a psoriatic uninvolved skin dataset containing differentially expressed transcripts fr

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Topalidou, Irini, Manolis Papamichos-Chronakis, and George Thireos. "Post-TATA Binding Protein Recruitment Clearance of Gcn5-Dependent Histone Acetylation within Promoter Nucleosomes." Molecular and Cellular Biology 23, no. 21 (2003): 7809–17. http://dx.doi.org/10.1128/mcb.23.21.7809-7817.2003.

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ABSTRACT Transcriptional activation of eukaryotic genes often requires the function of histone acetyltransferases (HATs), which is expected to result in the hyperacetylation of histones within promoter nucleosomes. In this study we show that, in Saccharomyces cerevisiae, the steady-state levels of Gcn5-dependent histone acetylation within a number of transcriptionally active promoters are inversely related to the rate of transcription. High acetylation levels were measured only when transcription was attenuated either by TATA element mutations or in a strain carrying a temperature-sensitive pr

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Waterborg, Jakob H. "Dynamics of histone acetylation in vivo. A function for acetylation turnover?" Biochemistry and Cell Biology 80, no. 3 (2002): 363–78. http://dx.doi.org/10.1139/o02-080.

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Histone acetylation, discovered more than 40 years ago, is a reversible modification of lysines within the amino-terminal domain of core histones. Amino-terminal histone domains contribute to the compaction of genes into repressed chromatin fibers. It is thought that their acetylation causes localized relaxation of chromatin as a necessary but not sufficient condition for processes that repackage DNA such as transcription, replication, repair, recombination, and sperm formation. While increased histone acetylation enhances gene transcription and loss of acetylation represses and silences genes

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Tao, Dan, Jun Lu, Hui Sun, et al. "Trichostatin A Extends the Lifespan of Drosophila melanogaster by Elevating hsp22 Expression." Acta Biochimica et Biophysica Sinica 36, no. 9 (2004): 618–22. http://dx.doi.org/10.1093/abbs/36.9.618.

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Abstract The level of acetylation of histones in nucleosomes is related to the longevity of yeast and animals. However, the mechanisms by which acetylation and deacetylation affect longevity remain unclear. In present study, we investigated the influence of histone acetylation modification on the expression of hsp22 gene and the lifespan in Drosophila melanogaster using histone deacetylase (HDAC) inhibitor Trichostatin A (TSA). The results showed that TSA could extend the lifespan of Drosophila melanogaster. Furthermore, TSA significantly promoted the hsp22 gene transcription, and affected the

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Gómez, Eliana B., Joaquín M. Espinosa, and Susan L. Forsburg. "Schizosaccharomyces pombe mst2+ Encodes a MYST Family Histone Acetyltransferase That Negatively Regulates Telomere Silencing." Molecular and Cellular Biology 25, no. 20 (2005): 8887–903. http://dx.doi.org/10.1128/mcb.25.20.8887-8903.2005.

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ABSTRACT Histone acetylation and deacetylation are associated with transcriptional activity and the formation of constitutively silent heterochromatin. Increasingly, histone acetylation is also implicated in other chromosome transactions, including replication and segregation. We have cloned the only Schizosaccharomyces pombe MYST family histone acetyltransferase genes, mst1 + and mst2 +. Mst1p, but not Mst2p, is essential for viability. Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. Δmst2 genetically interacts with mutants that affect heterochroma

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Lin, R., J. W. Leone, R. G. Cook, and C. D. Allis. "Antibodies specific to acetylated histones document the existence of deposition- and transcription-related histone acetylation in Tetrahymena." Journal of Cell Biology 108, no. 5 (1989): 1577–88. http://dx.doi.org/10.1083/jcb.108.5.1577.

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In this study, we have constructed synthetic peptides which are identical to hyperacetylated amino termini of two Tetrahymena core histones (tetra-acetylated H4 and penta-acetylated hv1) and used them to generate polyclonal antibodies specific for acetylated forms (mono-, di-, tri-, etc.) of these histones. Neither of these antisera recognizes histone that is unacetylated. Immunoblotting analyses demonstrate that both transcription-related and deposition-related acetate groups on H4 are recognized by both antisera. In addition, the antiserum raised against penta-acetylated hv1 also recognizes

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Fang, Lei, Danqi Chen, Clinton Yu, et al. "Mechanisms Underlying Acrolein-Mediated Inhibition of Chromatin Assembly." Molecular and Cellular Biology 36, no. 23 (2016): 2995–3008. http://dx.doi.org/10.1128/mcb.00448-16.

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Acrolein is a major component of cigarette smoke and cooking fumes. Previously, we reported that acrolein compromises chromatin assembly; however, underlying mechanisms have not been defined. Here, we report that acrolein reacts with lysine residues, including lysines 5 and 12, sites important for chromatin assembly, on histone H4 in vitro and in vivo . Acrolein-modified histones are resistant to acetylation, suggesting that the reduced H4K12 acetylation that occurs following acrolein exposure is probably due to the formation of acrolein-histone lysine adducts. Accordingly, the association of

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Vezzoli, Marco, Lara Isabel de Llobet Cucalon, Chiara Di Vona, et al. "TFIIIC as a Potential Epigenetic Modulator of Histone Acetylation in Human Stem Cells." International Journal of Molecular Sciences 24, no. 4 (2023): 3624. http://dx.doi.org/10.3390/ijms24043624.

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Regulation of histone acetylation dictates patterns of gene expression and hence cell identity. Due to their clinical relevance in cancer biology, understanding how human embryonic stem cells (hESCs) regulate their genomic patterns of histone acetylation is critical, but it remains largely to be investigated. Here, we provide evidence that acetylation of histone H3 lysine-18 (H3K18ac) and lysine-27 (H3K27ac) is only partially established by p300 in stem cells, while it represents the main histone acetyltransferase (HAT) for these marks in somatic cells. Our analysis reveals that whereas p300 m

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Ito, Kazuhiro, and Ian M. Adcock. "Histone Acetylation and Histone Deacetylation." Molecular Biotechnology 20, no. 1 (2002): 099–106. http://dx.doi.org/10.1385/mb:20:1:099.

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Zerzaihi, Ouafa, Sabrina Chriett, Hubert Vidal, and Luciano Pirola. "Insulin-dependent transcriptional control in L6 rat myotubes is associated with modulation of histone acetylation and accumulation of the histone variant H2A.Z in the proximity of the transcriptional start site." Biochemistry and Cell Biology 92, no. 1 (2014): 61–67. http://dx.doi.org/10.1139/bcb-2013-0071.

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Besides its direct metabolic effects, insulin induces transcriptional alterations in its target tissues. However, whether such changes are accompanied by epigenetic changes on the chromatin template encompassing insulin responsive genes is unclear. Here, mRNA levels of insulin-responsive genes hexokinase 2 (Hk2), insulin receptor substrate (Irs2), and the PI3K subunit p85β (Pik3r2) were compared in control versus insulin-stimulated L6 myotubes. Chromatin immunoprecipitation (ChIP) was performed with antibodies directed to histone H2A, histone variant H2A.Z, acetylated histone H3 on lysines 9/1

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Letting, Danielle L., Carrie Rakowski, Mitchell J. Weiss, and Gerd A. Blobel. "Formation of a Tissue-Specific Histone Acetylation Pattern by the Hematopoietic Transcription Factor GATA-1." Molecular and Cellular Biology 23, no. 4 (2003): 1334–40. http://dx.doi.org/10.1128/mcb.23.4.1334-1340.2003.

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ABSTRACT One function of lineage-restricted transcription factors may be to control the formation of tissue-specific chromatin domains. In erythroid cells, the β-globin gene cluster undergoes developmentally regulated hyperacetylation of histones at the active globin genes and the locus control region (LCR). However, it is unknown which transcription factor(s) governs the establishment of this erythroid-specific chromatin domain. We measured histone acetylation at the β-globin locus in the erythroid cell line G1E, which is deficient for the essential hematopoietic transcription factor GATA-1.

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Ringel, Alison E., Anne M. Cieniewicz, Sean D. Taverna, and Cynthia Wolberger. "Nucleosome competition reveals processive acetylation by the SAGA HAT module." Proceedings of the National Academy of Sciences 112, no. 40 (2015): E5461—E5470. http://dx.doi.org/10.1073/pnas.1508449112.

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The Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator complex hyperacetylates histone tails in vivo in a manner that depends upon histone 3 lysine 4 trimethylation (H3K4me3), a histone mark enriched at promoters of actively transcribed genes. SAGA contains a separable subcomplex known as the histone acetyltransferase (HAT) module that contains the HAT, Gcn5, bound to Sgf29, Ada2, and Ada3. Sgf29 contains a tandem Tudor domain that recognizes H3K4me3-containing peptides and is required for histone hyperacetylation in vivo. However, the mechanism by which H3K4me3 recognition leads to lysine hype

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