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Relevant bibliographies by topics / Histone acetylation

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Academic literature on the topic 'Histone acetylation'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 July 2024

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Journal articles on the topic "Histone acetylation"

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 (July 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, the activity of the extract is indistinguishable from postsynthetic, transcription-related histone acetylation that occurs in vivo or in isolated nuclei. Heat inactivation curves with both substrates are indistinguishable, and free histones compete with chromatin for limiting amounts of enzyme activity. These results argue strongly that two distinct, biologically important histone acetylations, one deposition related and one transcription related, are carried out by a single acetyltransferase.

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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 (July 23, 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 level of activating modifications at 3 and 6 h postinfection (hpi), followed by a marked reduction at 12 hpi. All viral promoters, as well as nonpromoter regions, are modified with activating acetylations at 24 to 72 hpi. The transient reduction in histone H3 acetylation at the major immediate-early promoter depends on the cis-repressive sequence to which the UL122-coded IE2 protein binds. A mutant virus lacking this element exhibited decreased IE2 binding at the major immediate-early promoter and failed to show reduced acetylation of histone H3 residing at this promoter at 12 hpi. Our results demonstrate that cytomegalovirus chromatin undergoes dynamic, promoter-specific histone modifications early in the infectious cycle, after which the entire chromosome becomes highly acetylated.

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Legartová, Soňa, Stanislav Kozubek, Michal Franek, Zbyněk Zdráhal, Gabriela Lochmanová, Nadine Martinet, and Eva Bártová. "Cell differentiation along multiple pathways accompanied by changes in histone acetylation status." Biochemistry and Cell Biology 92, no. 2 (April 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 tri-acetylation of histone H2B and a pronounced increase in di- and tri-acetylation of histone H4. In enterocytes, mono-acetylation of histone H2A also increased and tetra-acetylation of histone H4 appeared only after induction of this differentiation pathway. During differentiation of hESCs, we observed increased mono-acetylation and decreased tri-acetylation of H2B. Mono-, di-, and tri-acetylation of H4 were reduced, manifested by a significant increase in nonacetylated H4 histones. Levels of acetylated histones increased during induced differentiation in mESCs and during histone deacetylase (HDAC) inhibitor-induced enterocytic differentiation, whereas differentiation of human ESCs was associated with reduced acetylation of histones H2B and H4.

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Kring, Friedhelm, and Peter Böger. "Histone Acetylation is not Affected by Chloroacetamides in vitro." Zeitschrift für Naturforschung C 49, no. 5-6 (June 1, 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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CraneRobinson, Colyn. "Playing tag: Histone acetylation." Biochemist 29, no. 4 (August 1, 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 considerable extent determines the functional status of the local chromatin. HHe istone acetylation is deposited and removed by numerous histone acetyltransferases (HATs) and deacetylases (HDACs) and acetyl-lysines are recognised (i.e. the histone code is ‘read’) by bromodomain-containing proteins.

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6

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 (July 26, 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 ischemic damage. However, the role of different HDAC isoforms in the survival and death of brain cells after stroke is still controversial. HAT/HDAC activity depends on the acetylation site and the acetylation/deacetylation of the main proteins (c-Myc, E2F1, p53, ERK1/2, Akt) considered in this review, that are involved in the regulation of cell fate decisions. Our review aims to analyze the possible role of the acetylation/deacetylation of transcription factors and signaling proteins involved in the regulation of survival and death in cerebral ischemia.

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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 (June 1, 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 localized in highly acetylated chromatin, displayed faster acetyl turnover. Histone H2A with a low level of acetylation was not subject to rapid turnover or hyperacetylation. Patterns of acetate labeling revealed fundamental differences between histone H3 versus histones H4 and H2B. In H3, acetylation of all molecules, limited by lysine methylation, had similar rates, independent of the level of lysine acetylation. Acetylation of histones H4 and H2B was seen in only a fraction of all molecules and involved multiacetylation. Acetylation turnover rates increased from mono- to penta- and hexaacetylated forms, respectively. TSA was an effective inhibitor of alfalfa histone deacetylases in vivo and caused a doubling in steady-state acetylation levels by 46 h after addition. However, hyperacetylation was transient due to loss of TSA inhibition. TSA-induced overexpression of cellular deacetylase activity produced hypoacetylation by 18 h treatment with enhanced acetate turnover labeling of alfalfa histones. Thus, application of TSA to change gene expression in vivo in plants may have unexpected consequences.

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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 (April 15, 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 observed, to a lesser extent, at promoters activated by Hap4, Adr1, Met4, and Ace1. Activation by heat shock factor has multiple effects; H4 acetylation increases at some promoters, whereas other promoters show an apparent decrease in H3 and H4 acetylation that probably reflects nucleosome loss or gross alteration of chromatin structure. Repression by targeted recruitment of the Sin3-Rpd3 histone deacetylase is associated with decreased H3 and H4 acetylation, whereas repression by Cyc8-Tup1 is associated with decreased H3 acetylation but variable effects on H4 acetylation; this suggests that Cyc8-Tup1 uses multiple mechanisms to reduce histone acetylation at promoters. Thus, individual activators confer distinct patterns of histone acetylation on target promoters, and transcriptional activation is not necessarily associated with increased acetylation. We speculate that the activator-specific decrease in histone H4 acetylation is due to blocking the access or function of an H4-specific histone acetylase such as Esa1.

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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 (August 1, 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-dependent chromatin remodeling by ACF is required for the acetylation of nucleosomal histones by p300. Thus, chromatin remodeling, which requires a transcriptional activator, ACF and ATP, is an early step in the transcriptional process that regulates subsequent core histone acetylation. Glycerol gradient sedimentation and immunoprecipitation assays demonstrate that the acetylation of histones by p300 facilitates the transfer of H2A–H2B from nucleosomes to NAP-1. The results from these biochemical experiments suggest that (1) transcriptional activators (e.g., Gal4–VP16) and chromatin remodeling complexes (e.g., ACF) induce chromatin remodeling in the absence of histone acetylation; (2) transcriptional activators recruit histone acetyltransferases (e.g., p300) to promoters after chromatin remodeling has occurred; and (3) histone acetylation is important for a step subsequent to chromatin remodeling and results in the transfer of histone H2A–H2B dimers from nucleosomes to a histone chaperone such as NAP-1. Our results indicate a precise role for histone acetylation, namely to alter the structure of nucleosomes (e.g., facilitate the loss of H2A–H2B dimers) that have been remodeled previously by the action of ATP-dependent chromatin remodeling complexes. Thus, transcription from chromatin templates is ordered and sequential, with precise timing and roles for ATP-dependent chromatin remodeling, subsequent histone acetylation, and alterations in nucleosome structure.

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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 (January 15, 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 mixtures. We demonstrate that the inhibition is due mainly to steric hindrance of H3 by the tails of linker histones and not to condensation of the chromatin fiber. Cellular PCAF, which is complexed with accessory proteins in a multiprotein complex, can overcome the linker histone repression. We suggest that linker histones hinder access of PCAF, and perhaps other HATs, to their target acetylation sites and that perturbation of the linker histone organization in chromatin is a prerequisite for efficient acetylation of the histone tails in nucleosomes.

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Dissertations / Theses on the topic "Histone acetylation"

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Choi, Jennifer Kristel. ""Open" chromatin : histone acetylation, linker histones & histone variants." Thesis, University of British Columbia, 2013. http://hdl.handle.net/2429/45271.

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Man, Pui-sum Ellen. "Histone acetylation in gynaecological malignancies." Click to view the E-thesis via HKUTO, 2004. http://sunzi.lib.hku.hk/hkuto/record/B31972068.

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Cervoni, Nadia. "DNA demethylation and histone acetylation." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=38166.

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Unlike in somatic cells, cancer cells adopt an aberrant pattern of methylation as well as histone acetylation, and therefore distort the chromatin structure. Chapters 2--4 of this thesis look at mechanisms carried out by the recently cloned DNA demethylase, how its demethylation activity is closely linked with the semblance of acetylation of chromatin, and how this relationship can be skewed in cancer. The three intriguing mechanisms described provide attractive models by which to explain general genome wide demethylation, site specific demethylation of genes upon their activation, and the relationship between aberrant methylation and histone acetylation in cancer. The thesis begins by characterizing the mechanism of demethylation carried out by the bona fida DNA demethylase---an enzyme identified and cloned in our laboratory found to demethylate both hemi and double-stranded DNA in vitro. This enzyme manifests the removal of methyl groups from DNA without damaging the DNA and is therefore a candidate protein responsible for hypomethylation seen during development as well as in transformed cells. One essential property of an enzyme that removes methylation from wide regions of the genome could be processivity. Southern blot analysis and sodium bisulfite mapping experiments determine that purified demethylase demethylates DNA in a processive manner in vitro. Experiments in Chapter 3 demonstrate how an active demethylase enzyme is involved in shaping patterns of methylation relative to the state of histone acetylation. We present evidence suggesting demethylase activity is directed by the state of histone acetylation, therefore contrasting the accepted dogma, and suggesting that the local histone acetylation state determines the resulting methylation pattern. Aberrant DNA methylation and histone deacetylation are frequently associated with silencing of tumor suppressor genes in cancer and yet cannot simply be explained by the level of methyltransferase(s) enzyme(s)

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Man, Pui-sum Ellen, and 萬佩心. "Histone acetylation in gynaecological malignancies." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2004. http://hub.hku.hk/bib/B31972068.

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Venkataraman, Shanmugasundaram. "Histone acetylation and nucleosome dynamics." Thesis, University of Edinburgh, 2001. http://hdl.handle.net/1842/23234.

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In this report, I will describe purification of core histone octamers from chicken blood, HeLa nuclei and yeast cells, along with preparation of DNA fragments containing the 208 bp 5S rDNA gene and the adult beta (b^A)-globin gene promoter. In vitro experiments studying the effect of histone acetylation on the positioning and mobility of nucleosomes on the sea urchin 5S rDNA gene and the chicken b^A-globin gene promoter will be described. The former provides a well studied nucleosome positioning and mobility model system, while the latter is a developmentally regulated gene, with globin gene switching through the early stages of the lifetime of the chicken, and a proposed involvement of positioned nucleosomes in its regulation. The aim was to determine the difference between hypoacetylated and hyperacetylated core histones in terms of their influence upon nucleosome positioning and mobility. In earlier studies, it was noted that there was a difference in relative positioning intensities between the two forms (ie. hypoacetylated core histones preferentially positioned at certain sites, while hyperacetylated core histones positioned at the same sites but with different relative affinities). Therefore, acetylation affects where a nucleosomes is able to position. I have carried on this work to further characterize nucleosome positioning and to study the implications of histone acetylation on nucleosome mobility. I have found subtle differences in the thermodynamics and kinetics of hyperacetylated nucleosomes compared to hypeoacetylated nucleosomes: hyperacetylated nucleosomes appear to have a lower threshold in both these parameters when studied using the 208 pb rDNA fragment. Experiments involving two other types of core histones, trypsinized chicken core histone octamers and chicken core histone tetramers will also be described, which will be placed into the context of the results found with the other types of core histones. Finally, I will describe the effect of reconstituting hyperacetylated core histones with methylated DNA, long known to be a mediator of transcriptional repression, in the form of the chicken b^A-globin gene promoter.

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Hebbes, T. R. "Histone acetylation and transcriptionally active chromatin." Thesis, University of Portsmouth, 1988. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.382541.

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Clayton, Alison Louise. "Core histone acetylation of active genes." Thesis, University of Portsmouth, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240358.

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Choudhury, Mahua Shukla Shivendra D. "Alcohol induced histone acetylation mediated by histone acetyl transferase GCN5 in liver." Diss., Columbia, Mo. : University of Missouri-Columbia, 2008. http://hdl.handle.net/10355/6866.

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The entire dissertation/thesis text is included in the research.pdf file; the official abstract appears in the short.pdf file (which also appears in the research.pdf); a non-technical general description, or public abstract, appears in the public.pdf file. Title from PDF of title page (University of Missouri--Columbia, viewed on April 6, 2010). Vita. Thesis advisor: Shivendra D. Shukla. "August 2008" Includes bibliographical references

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Ou, Jing Ni. "Epigenetic crosstalk between DNA demethylation and histone acetylation." Thesis, McGill University, 2009. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=32413.

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Abnormal methylation patterns such as regional hypermethylation and genomic hypomethylation often result in transcriptional changes of critical genes that are central to the progression of human cancers. It is therefore important to identify the mechanisms that are responsible for the alterations in order to identify proper pharmacological targets. This thesis examines whether specific cellular factors are involved in establishing the state of DNA hypomethylation in cancer cells and whether changes in chromatin structure could affect DNA methylation. MBD2 is a protein that has been previously characterized to possess distinct transcription activities; it can either function as a methylation-dependent transcription repressor, a methylation-independent transcription activator, as well as an inducer of DNA demethylation. Chapters 3 and 4 demonstrate that MBD2 induces gene-specific DNA demethylation in pancreatic and bladder cancer cells by recruiting transcriptional activator AP-2, Sp1 and the histone acetyltransferase CBP to the associated promoters. These results substantiate the idea that demethylation induced by MBD2 might facilitate the recruitment of transcription factors to the gene to activate its expression. Histone deacetylase (HDAC) inhibitors are drugs designed to target chromatin modification. In chapter 5, we showed that increasing histone acetylation by HDAC inhibitor TSA was associated with a significant decrease in global methylation. TSA also induces histone acetylation, DNA demethylation and expression of specific methylated tumor suppressor genes, such as E-CADHERIN and RARβ2 in different human cancer cell lines. Our findings provide evidence for a
Un patron de méthylation anormal, tel que l'hyperméthylation régionale ou l'hypométhylation génomique, modifie la transcription de gènes critiques jouant ainsi un rôle central dans la progression de nombreux cancers chez l'humain. Il est donc devenu essentiel d'identifier les mécanismes responsables de ces altérations afin de développer des traitements pharmacologiques ciblés. Le but principal de cette thèse est d'examiner si certains facteurs cellulaires sont impliqués dans l'établissement de l'ADN hypométhylé des cellules cancéreuses, ainsi que l'effet des changements dans la structure de la chromatine sur la méthylation de l'ADN. Il a été préalablement démontré que la protéine MBD2 possède plusieurs rôles distincts lors de la transcription, elle peut agir à la fois comme un répresseur de la transcription dépendant de la méthylation, comme un inducteur de la déméthylation ainsi qu'un activateur de la transcription indépendant de la méthylation. Les chapitres 3 et 4 présentés dans cet ouvrage démontrent que MBD2 induit la déméthylation de gènes spécifiques dans les cellules cancéreuses pancréatiques et urinaires grâce au recrutement des activateurs transcriptionnels AP-2, Sp1 ainsi que de l'histone acétyltransférase CBP au promoteur impliqué. Ces résultats supportent l'hypothèse selon laquelle la déméthylation induite par MBD2 faciliterait le recrutement de facteurs de transcription au sein du gène afin d'activer son expression. Les inhibiteurs de l'Histone déacétylase (HDAC) sont des drogues pharmaceutiques développées afin de cibler les modifications de la chromatine. Nous sommes parvenus à démontrer, dans le

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Smith, Anna Elizabeth. "The role of histone acetylation in recognition memory." Thesis, University of Bristol, 2016. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.715770.

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Books on the topic "Histone acetylation"

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Gregory, Bock, Goode Jamie, Novartis Foundation, and Symposium on Reversible Protein Acetylation (2003 London, England), eds. Reversible protein acetylation. Chichester: Wiley, 2004.

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O'Neill, Laura Patricia. Histone acetylation and transcription in Eukaryotic cells. Birmingham: University of Birmingham, 1994.

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Johnson, Helen Louise. Site-specific acetylation of histone H4 and its functional significance. Birmingham: University of Birmingham, 1997.

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4

Evans, Dain R. Targeted and widespread acetylation of histones H3 and H4 at the chicken [beta]-globin locus. Portsmouth: Institute of Biomedical and Biomolecular Sciences, 2001.

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Johnston, Michael V. Coffin-Lowry Syndrome. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199937837.003.0057.

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Coffin-Lowry syndrome (CLS) is a relatively rare (1:50,000-100,000 incidence) sex-linked neurodevelopmental disorder that includes severe intellectual disability, dysmorphic features including facial and digital abnormalities, growth retardation, and skeletal changes. Most cases are sporadic with only 20% to 30% of cases having an additional family member. CLS is caused by variable loss of function mutations in the RPS6KA3 gene that maps to Xp22.2 and codes for the hRSK2 S6 kinase that phosphorylates the transcription factor CREB (cAMP response element binding protein) as well as other nuclear transcription factors. Phosphorylated CREB (pCREB) plays a major role in memory formation in fruit flies and mammals by activating specific genes through epigenetic histone acetylation.

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Book chapters on the topic "Histone acetylation"

1

Turner, Bryan M. "Histone Acetylation." In Genome Structure and Function, 155–71. Dordrecht: Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-011-5550-2_8.

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Wang, Shaowen, Yan Yan-Neale, Marija Zeremski, and Dalia Cohen. "Transcription Regulation by Histone Deacetylases." In Reversible Protein Acetylation, 238–48. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch18.

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Marks, Paul A., Victoria M. Richon, Wm Kevin Kelly, Judy H. Chiao, and Thomas Miller. "Histone Deacetylase Inhibitors: Development as Cancer Therapy." In Reversible Protein Acetylation, 269–84. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch20.

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Schotta, Gunnar, Monika Lachner, Antoine H. F. M. Peters, and Thomas Jenuwein. "The Indexing Potential of Histone Lysine Methylation." In Reversible Protein Acetylation, 22–47. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch3.

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Marmorstein, Ronen. "Structural and Chemical Basis of Histone Acetylation." In Reversible Protein Acetylation, 78–101. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch6.

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Kiss, Anna K. "Polyphenols and Histone Acetylation." In Handbook of Nutrition, Diet, and Epigenetics, 1977–96. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-55530-0_105.

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Kiss, Anna K. "Polyphenols and Histone Acetylation." In Handbook of Nutrition, Diet, and Epigenetics, 1–21. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-31143-2_105-1.

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Wang, Yanming, Wolfgang Fischle, Wang Cheung, Steven Jacobs, Sepideh Khorasanizadeh, and C. David Allis. "Beyond the Double Helix: Writing and Reading the Histone Code." In Reversible Protein Acetylation, 3–21. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch2.

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McKinsey, Timothy A., and Eric N. Olson. "Dual Roles of Histone Deacetylases in the Control of Cardiac Growth." In Reversible Protein Acetylation, 132–45. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch9.

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Mahadevan, Louis C., Alison L. Clayton, Catherine A. Hazzalin, and Stuart Thomson. "Phosphorylation and Acetylation of Histone H3 at Inducible Genes: Two Controversies Revisited." In Reversible Protein Acetylation, 102–14. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862637.ch7.

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Conference papers on the topic "Histone acetylation"

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Price, Bo J. "Histone binding factor ENAP1 retrains seed germination through ABI5 dependent histone acetylation regulation." In ASPB PLANT BIOLOGY 2020. USA: ASPB, 2020. http://dx.doi.org/10.46678/pb.20.1048264.

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Deng, Yangyang, and Xianhua Dai. "Similar Histone Acetylation Pattern of Neighboring Genes in Yeast." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering. IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.91.

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Stefanowicz, Dorota, Tillie-Louise Hackett, Peter D. Paré, and Darryl A. Knight. "Alterations In Histone Acetylation In Asthmatic Airway Epithelial Cells." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a1448.

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Zakarya, R., H. Chen, C. A. A. Brandsma, I. M. Adcock, and B. G. G. Oliver. "Small Airway Fibrosis in COPD Is Mediated by Histone Acetylation." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5776.

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Purushothaman, Anurag, and Ralph D. Sanderson. "Abstract A17: Glycosaminoglycans regulates histone acetylation status in multiple myeloma." In Abstracts: AACR Special Conference on Chromatin and Epigenetics in Cancer - June 19-22, 2013; Atlanta, GA. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.cec13-a17.

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Carrer, Alessandro, Joyce V. Lee, Supriya Shah, Nicole M. Aiello, Nathaniel W. Snyder, Andrew J. Worth, Ian A. Blair, Ben Z. Stanger, and Kathryn E. Wellen. "Abstract PR03: Exploring the link between Kras and histone acetylation." In Abstracts: AACR Special Conference: Chromatin and Epigenetics in Cancer; September 24-27, 2015; Atlanta, GA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.chromepi15-pr03.

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Roccaro, Aldo M., Antonio Sacco, Abdel Kareem Azab, Feda Azab, Hai T. Ngo, Patricia Maiso, and Irene M. Ghobrial. "Abstract 2060: microRNA-dependent modulation of histone acetylation in Waldenstrom's Macroglobulinemia." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2060.

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Zakarya, R., Y. L. Chan, H. Chen, C. A. A. Brandsma, I. M. Adcock, and B. G. G. Oliver. "BET Protein Propagated Histone Acetylation Mediates ECM Changes in COPD Airways." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6431.

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Shah, Supriya, Joyce V. Lee, Alessandro Carrer, Nathaniel W. Snyder, and Kathryn E. Wellen. "Abstract A31: Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-a31.

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Carrer, Alessandro, Joyce V. Lee, Supriya Shah, Nathaniel W. Snyder, Ellen Jackson, Nicole M. Aiello, Benjamin A. Garcia, et al. "Abstract B40: Oncogenic Kras induces histone acetylation in pancreatic ductal adenocarcinoma." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-b40.

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Reports on the topic "Histone acetylation"

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Kovacs, Jeffrey J. Regulation of EGF Receptor Signaling by Histone Deacetylase 6 (HDAC6)-Mediated Reversible Acetylation. Fort Belvoir, VA: Defense Technical Information Center, April 2005. http://dx.doi.org/10.21236/ada435267.

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Meiri, Noam, Michael D. Denbow, and Cynthia J. Denbow. Epigenetic Adaptation: The Regulatory Mechanisms of Hypothalamic Plasticity that Determine Stress-Response Set Point. United States Department of Agriculture, November 2013. http://dx.doi.org/10.32747/2013.7593396.bard.

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Abstract:

Our hypothesis was that postnatal stress exposure or sensory input alters brain activity, which induces acetylation and/or methylation on lysine residues of histone 3 and alters methylation levels in the promoter regions of stress-related genes, ultimately resulting in long-lasting changes in the stress-response set point. Therefore, the objectives of the proposal were: 1. To identify the levels of total histone 3 acetylation and different levels of methylation on lysine 9 and/or 14 during both heat and feed stress and challenge. 2. To evaluate the methylation and acetylation levels of histone 3 lysine 9 and/or 14 at the Bdnfpromoter during both heat and feed stress and challenge. 3. To evaluate the levels of the relevant methyltransferases and transmethylases during infliction of stress. 4. To identify the specific localization of the cells which respond to both specific histone modification and the enzyme involved by applying each of the stressors in the hypothalamus. 5. To evaluate the physiological effects of antisense knockdown of Ezh2 on the stress responses. 6. To measure the level of CpG methylation in the promoter region of BDNF in thermal treatments and free-fed, 12-hour fasted, and re-fed chicks during post-natal day 3, which is the critical period for feed-control establishment, and 10 days later to evaluate longterm effects. 7. The phenotypic effect of antisense “knock down” of the transmethylaseDNMT 3a. Background: The growing demand for improvements in poultry production requires an understanding of the mechanisms governing stress responses. Two of the major stressors affecting animal welfare and hence, the poultry industry in both the U.S. and Israel, are feed intake and thermal responses. Recently, it has been shown that the regulation of energy intake and expenditure, including feed intake and thermal regulation, resides in the hypothalamus and develops during a critical post-hatch period. However, little is known about the regulatory steps involved. The hypothesis to be tested in this proposal is that epigenetic changes in the hypothalamus during post-hatch early development determine the stress-response set point for both feed and thermal stressors. The ambitious goals that were set for this proposal were met. It was established that both stressors i.e. feed and thermal stress, can be manipulated during the critical period of development at day 3 to induce resilience to stress later in life. Specifically it was established that unfavorable nutritional conditions during early developmental periods or heat exposure influences subsequent adaptability to those same stressful conditions. Furthermore it was demonstrated that epigenetic marks on the promoter of genes involved in stress memory are altered both during stress, and as a result, later in life. Specifically it was demonstrated that fasting and heat had an effect on methylation and acetylation of histone 3 at various lysine residues in the hypothalamus during exposure to stress on day 3 and during stress challenge on day 10. Furthermore, the enzymes that perform these modifications are altered both during stress conditioning and challenge. Finally, these modifications are both necessary and sufficient, since antisense "knockdown" of these enzymes affects histone modifications, and as a consequence stress resilience. DNA methylation was also demonstrated at the promoters of genes involved in heat stress regulation and long-term resilience. It should be noted that the only goal that we did not meet because of technical reasons was No. 7. In conclusion: The outcome of this research may provide information for the improvement of stress responses in high yield poultry breeds using epigenetic adaptation approaches during critical periods in the course of early development in order to improve animal welfare even under suboptimum environmental conditions.

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