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Journal articles on the topic 'Hyperacetylation'

Author: Grafiati

Published: 6 September 2023

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1

Sudo, Haruka, and Akira Kubo. "The Aneugenicity of Ketone Bodies in Colon Epithelial Cells Is Mediated by Microtubule Hyperacetylation and Is Blocked by Resveratrol." International Journal of Molecular Sciences 22, no. 17 (August 30, 2021): 9397. http://dx.doi.org/10.3390/ijms22179397.

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Diabetes mellitus (DM) is considered to be associated with an increased risk of colorectal cancer. Recent studies have also revealed that tubulin hyperacetylation is caused by a diabetic status and we have reported previously that, under microtubule hyperacetylation, a microtubule severing protein, katanin-like (KL) 1, is upregulated and contributes to tumorigenesis. To further explore this phenomenon, we tested the effects of the ketone bodies, acetoacetate and β-hydroxybutyrate, in colon and fibroblast cells. Both induced microtubule hyperacetylation that responded differently to a histone deacetylase 3 knockdown. These two ketone bodies also generated intracellular reactive oxygen species (ROS) and hyperacetylation was commonly inhibited by ROS inhibitors. In a human fibroblast-based microtubule sensitivity test, only the KL1 human katanin family member showed activation by both ketone bodies. In primary cultured colon epithelial cells, these ketone bodies reduced the tau protein level and induced KL1- and α-tubulin acetyltransferase 1 (ATAT1)-dependent micronucleation. Resveratrol, known for its tumor preventive and tubulin deacetylation effects, inhibited this micronucleation. Our current data thus suggest that the microtubule hyperacetylation induced by ketone bodies may be a causal factor linking DM to colorectal carcinogenesis and may also represent an adverse effect of them that needs to be controlled if they are used as therapeutics.

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Rao, Rekha, Warren Fiskus, Yonghua Yang, Pearl Lee, Rajeshree Joshi, Pravina Fernandez, Aditya Mandawat, Peter Atadja, James E. Bradner, and Kapil Bhalla. "HDAC6 inhibition enhances 17-AAG–mediated abrogation of hsp90 chaperone function in human leukemia cells." Blood 112, no. 5 (September 1, 2008): 1886–93. http://dx.doi.org/10.1182/blood-2008-03-143644.

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Abstract Histone deacetylase 6 (HDAC6) is a heat shock protein 90 (hsp90) deacetylase. Treatment with pan-HDAC inhibitors or depletion of HDAC6 by siRNA induces hyperacetylation and inhibits ATP binding and chaperone function of hsp90. Treatment with 17-allylamino-demothoxy geldanamycin (17-AAG) also inhibits ATP binding and chaperone function of hsp90, resulting in polyubiquitylation and proteasomal degradation of hsp90 client proteins. In this study, we determined the effect of hsp90 hyperacetylation on the anti-hsp90 and antileukemia activity of 17-AAG. Hyperacetylation of hsp90 increased its binding to 17-AAG, as well as enhanced 17-AAG–mediated attenuation of ATP and the cochaperone p23 binding to hsp90. Notably, treatment with 17-AAG alone also reduced HDAC6 binding to hsp90 and induced hyperacetylation of hsp90. This promoted the proteasomal degradation of HDAC6. Cotreatment with 17-AAG and siRNA to HDAC6 induced more inhibition of hsp90 chaperone function and depletion of BCR-ABL and c-Raf than treatment with either agent alone. In addition, cotreatment with 17-AAG and tubacin augmented the loss of survival of K562 cells and viability of primary acute myeloid leukemia (AML) and chronic myeloid leukemia (CML) samples. These findings demonstrate that HDAC6 is an hsp90 client protein and hyperacetylation of hsp90 augments the anti-hsp90 and antileukemia effects of 17-AAG.

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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 (August 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 isoforms, and (or) histone variants against a backdrop of nonspecific acetylation across the domain in question. Here we review the characteristics of long-range histone acetylation in some higher eukaryotes and draw special attention to recent literature on the multiple effects that histone hyperacetylation has on chromatin’s structural integrity and how they affect transcription. These include the thermal, ionic, cumulative, and isoform-specific (H4 K16) consequences of acetylation that result in a more dynamic core complex and chromatin fiber.

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Kajino, Hidetoshi, Tomomi Nagatani, Miku Oi, Tomoya Kujirai, Hitoshi Kurumizaka, Atsuya Nishiyama, Makoto Nakanishi, Kenzo Yamatsugu, Shigehiro A. Kawashima, and Motomu Kanai. "Synthetic hyperacetylation of nucleosomal histones." RSC Chemical Biology 1, no. 2 (2020): 56–59. http://dx.doi.org/10.1039/d0cb00029a.

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5

Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (November 1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004-5014.1992.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of histone hyperacetylation on the linking number change which occurs during assembly in vivo. We find that butyrate treatment of cells infected with simian virus 40 results in hyperacetylation of the histones of the extracted viral minichromosome as expected. However, the change in constrained supercoils of the minichromosome DNA is minimal, a result which is inconsistent with the proposed model. These results indicate that the proposed mechanism of transcriptional activation is unlikely to take place in the cell.

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6

Lutter, L. C., L. Judis, and R. F. Paretti. "Effects of histone acetylation on chromatin topology in vivo." Molecular and Cellular Biology 12, no. 11 (November 1992): 5004–14. http://dx.doi.org/10.1128/mcb.12.11.5004.

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Recently a model for eukaryotic transcriptional activation has been proposed in which histone hyperacetylation causes release of nucleosomal supercoils, and this unconstrained tension in turn stimulates transcription (V. G. Norton, B. S. Imai, P. Yau, and E. M. Bradbury, Cell 57:449-457, 1989; V. G. Norton, K. W. Marvin, P. Yau, and E. M. Bradbury, J. Biol. Chem. 265:19848-19852, 1990). These studies analyzed the effect of histone hyperacetylation on the change in topological linking number which occurs during nucleosome assembly in vitro. We have tested this model by determining the effect of histone hyperacetylation on the linking number change which occurs during assembly in vivo. We find that butyrate treatment of cells infected with simian virus 40 results in hyperacetylation of the histones of the extracted viral minichromosome as expected. However, the change in constrained supercoils of the minichromosome DNA is minimal, a result which is inconsistent with the proposed model. These results indicate that the proposed mechanism of transcriptional activation is unlikely to take place in the cell.

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7

Na, Ann-Yae, Sanjita Paudel, Soyoung Choi, Jun Hyung Lee, Min-Sik Kim, Jong-Sup Bae, and Sangkyu Lee. "Global Lysine Acetylome Analysis of LPS-Stimulated HepG2 Cells Identified Hyperacetylation of PKM2 as a Metabolic Regulator in Sepsis." International Journal of Molecular Sciences 22, no. 16 (August 8, 2021): 8529. http://dx.doi.org/10.3390/ijms22168529.

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Sepsis-induced liver dysfunction (SILD) is a common event and is strongly associated with mortality. Establishing a causative link between protein post-translational modification and diseases is challenging. We studied the relationship among lysine acetylation (Kac), sirtuin (SIRTs), and the factors involved in SILD, which was induced in LPS-stimulated HepG2 cells. Protein hyperacetylation was observed according to SIRTs reduction after LPS treatment for 24 h. We identified 1449 Kac sites based on comparative acetylome analysis and quantified 1086 Kac sites on 410 proteins for acetylation. Interestingly, the upregulated Kac proteins are enriched in glycolysis/gluconeogenesis pathways in the Kyoto Encyclopedia of Genes and Genomes (KEGG) category. Among the proteins in the glycolysis pathway, hyperacetylation, a key regulator of lactate level in sepsis, was observed at three pyruvate kinase M2 (PKM2) sites. Hyperacetylation of PKM2 induced an increase in its activity, consequently increasing the lactate concentration. In conclusion, this study is the first to conduct global profiling of Kac, suggesting that the Kac mechanism of PKM2 in glycolysis is associated with sepsis. Moreover, it helps to further understand the systematic information regarding hyperacetylation during the sepsis process.

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8

Sudo, Haruka. "Microtubule Hyperacetylation Enhances KL1-Dependent Micronucleation under a Tau Deficiency in Mammary Epithelial Cells." International Journal of Molecular Sciences 19, no. 9 (August 23, 2018): 2488. http://dx.doi.org/10.3390/ijms19092488.

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Enhanced microtubule acetylation has been identified as a negative prognostic indicator in breast cancer. We reported previously that primary cultured human mammary epithelial cells manifest breast cancer-related aneuploidization via the activation of severing protein katanin-like (KL)1 when tau is deficient. To address in this current study whether microtubule hyperacetylation is involved in breast carcinogenesis through mitosis, the effects of tubacin on human mammary epithelial cells were tested using immunofluorescence techniques. Tau-knockdown cells showed enhancement of KL1-dependent events, chromosome-bridging and micronucleation in response to tubacin. These enhancements were suppressed by further expression of an acetylation-deficient tubulin mutant. Consistently, using a rat fibroblast-based microtubule sensitivity test, it was confirmed that KL1 also shows enhanced activity in response to microtubule hyperacetylation as well as katanin. It was further observed in rat fibroblasts that exogenously expressed KL1 results in more micronucleation under microtubule hyperacetylation conditions. These data suggest that microtubule acetylation upregulates KL1 and induces more aneuploidy if tau is deficient. It is thus plausible that microtubule hyperacetylation promotes tumor progression by enhancing microtubule sensitivity to KL1, thereby disrupting spindle microtubules and this process could be reversed by the microtubule-binding and microtubule protective octapeptide NAPVSIPQ (NAP) which recruits tau to the microtubules.

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9

Wu, James T., Sonia Y. Archer, Brian Hinnebusch, Shufen Meng, and Richard A. Hodin. "Transient vs. prolonged histone hyperacetylation: effects on colon cancer cell growth, differentiation, and apoptosis." American Journal of Physiology-Gastrointestinal and Liver Physiology 280, no. 3 (March 1, 2001): G482—G490. http://dx.doi.org/10.1152/ajpgi.2001.280.3.g482.

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The role of histone hyperacetylation in regard to growth, differentiation, and apoptosis in colon cancer cells was assessed in an in vitro model system. HT-29 cells were grown in ±10% fetal bovine serum with either 5 mM sodium butyrate or 0.3 μM trichostatin A [single dose (T) or 3 doses 8 h apart (TR)] for 24 h. Serum-starved HT-29 cells were further treated with epidermal growth factor or insulin-like growth factor I for an additional 24 h. Apoptosis was quantified with propidium iodide and characterized by electron microscopy. Northern blot analyses were performed with cDNA probes specific for intestinal alkaline phosphatase, Na-K-2Cl cotransporter, the cell cycle inhibitor p21, and the actin control. Flow cytometric analysis revealed a time-dependent growth suppression along with early induction of p21 mRNA in the butyrate, T, and TR groups. Histone hyperacetylation, assessed by acid-urea-triton gel electrophoresis, was transient in the T group but persisted for up to 24 h in the butyrate and TR groups. Induction of apoptosis, growth factor unresponsiveness, and differentiation occurred in the butyrate- and TR-treated cells but not those treated with a single dose of trichostatin A. Thus transient hyperacetylation of histones is sufficient to induce p21 expression and produce cellular growth arrest, but prolonged histone hyperacetylation is required for induction of the programs of differentiation, apoptosis, and growth factor unresponsiveness.

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10

Glon, Damien, Géraldine Vilmen, Daniel Perdiz, Eva Hernandez, Guillaume Beauclair, Frédérique Quignon, Clarisse Berlioz-Torrent, et al. "Essential role of hyperacetylated microtubules in innate immunity escape orchestrated by the EBV-encoded BHRF1 protein." PLOS Pathogens 18, no. 3 (March 11, 2022): e1010371. http://dx.doi.org/10.1371/journal.ppat.1010371.

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Innate immunity constitutes the first line of defense against viruses, in which mitochondria play an important role in the induction of the interferon (IFN) response. BHRF1, a multifunctional viral protein expressed during Epstein-Barr virus reactivation, modulates mitochondrial dynamics and disrupts the IFN signaling pathway. Mitochondria are mobile organelles that move through the cytoplasm thanks to the cytoskeleton and in particular the microtubule (MT) network. MTs undergo various post-translational modifications, among them tubulin acetylation. In this study, we demonstrated that BHRF1 induces MT hyperacetylation to escape innate immunity. Indeed, the expression of BHRF1 induces the clustering of shortened mitochondria next to the nucleus. This “mito-aggresome” is organized around the centrosome and its formation is MT-dependent. We also observed that the α-tubulin acetyltransferase ATAT1 interacts with BHRF1. Using ATAT1 knockdown or a non-acetylatable α-tubulin mutant, we demonstrated that this hyperacetylation is necessary for the mito-aggresome formation. Similar results were observed during EBV reactivation. We investigated the mechanism leading to the clustering of mitochondria, and we identified dyneins as motors that are required for mitochondrial clustering. Finally, we demonstrated that BHRF1 needs MT hyperacetylation to block the induction of the IFN response. Moreover, the loss of MT hyperacetylation blocks the localization of autophagosomes close to the mito-aggresome, impeding BHRF1 to initiate mitophagy, which is essential to inhibiting the signaling pathway. Therefore, our results reveal the role of the MT network, and its acetylation level, in the induction of a pro-viral mitophagy.

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11

Shepard, Blythe-D. "Alcohol-induced protein hyperacetylation: Mechanisms and consequences." World Journal of Gastroenterology 15, no. 10 (2009): 1219. http://dx.doi.org/10.3748/wjg.15.1219.

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12

Natarajan, Umamaheswari, Thiagarajan Venkatesan, and Appu Rathinavelu. "Effect of the HDAC Inhibitor on Histone Acetylation and Methyltransferases in A2780 Ovarian Cancer Cells." Medicina 57, no. 5 (May 7, 2021): 456. http://dx.doi.org/10.3390/medicina57050456.

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Background andObjective: Epigenetic modifications are believed to play a significant role in the development of cancer progression, growth, differentiation, and cell death. One of the most popular histone deacetylases inhibitors (HDACIs), suberoylanilide hydroxamic acid (SAHA), also known as Vorinostat, can directly activate p21WAF1/CIP1 gene transcription through hyperacetylation of histones by a p53 independent mechanism. In the present investigation, we evaluated the correlation between histone modifications and DNA methyltransferase enzyme levels following SAHA treatments in A2780 ovarian cancer cells. Materials and Methods: Acetylation of histones and methyltransferases levels were analyzed using RT2 profiler PCR array, immunoblotting, and immunofluorescence methods in 2D and 3D cell culture systems. Results: The inhibition of histone deacetylases (HDAC) activities by SAHA can reduce DNA methyl transferases / histone methyl transferases (DNMTs/HMTs) levels through induction of hyperacetylation of histones. Immunofluorescence analysis of cells growing in monolayers and spheroids revealed significant up-regulation of histone acetylation preceding the above-described changes. Conclusions: Our results depict an interesting interplay between histone hyperacetylation and a decrease in methyltransferase levels in ovarian cancer cells, which may have a positive impact on the overall outcomes of cancer treatment.

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13

Schübeler, Dirk, Claire Francastel, Daniel M. Cimbora, Andreas Reik, David I. K. Martin, and Mark Groudine. "Nuclear localization and histone acetylation: a pathway for chromatin opening and transcriptional activation of the human β-globin locus." Genes & Development 14, no. 8 (April 15, 2000): 940–50. http://dx.doi.org/10.1101/gad.14.8.940.

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We have investigated the mechanism, structural correlates, andcis-acting elements involved in chromatin opening and gene activation, using the human β-globin locus as a model. Full transcriptional activity of the human β-globin locus requires the locus control region (LCR), composed of a series of nuclease hypersensitive sites located upstream of this globin gene cluster. Our previous analysis of naturally occurring and targeted LCR deletions revealed that chromatin opening and transcriptional activity in the endogenous β-globin locus are dissociable and dependent on distinctcis-acting elements. We now report that general histone H3/H4 acetylation and relocation of the locus away from centromeric heterochromatin in the interphase nucleus are correlated and do not require the LCR. In contrast, LCR-dependent promoter activation is associated with localized histone H3 hyperacetylation at the LCR and the transcribed β-globin-promoter and gene. On the basis of these results, we suggest a multistep model for gene activation; localization away from centromeric heterochromatin is required to achieve general hyperacetylation and an open chromatin structure of the locus, whereas a mechanism involving LCR/promoter histone H3 hyperacetylation is required for high-level transcription of the β-globin genes.

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Fromm, George, Christina de Vries, Rachel Byron, Jennifer Fields, Steven Fiering, Mark Groudine, M. A. Bender, James Palis, and Michael Bulger. "Histone hyperacetylation within the β-globin locus is context-dependent and precedes high-level gene expression." Blood 114, no. 16 (October 15, 2009): 3479–88. http://dx.doi.org/10.1182/blood-2009-03-210690.

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Abstract Active gene promoters are associated with covalent histone modifications, such as hyperacetylation, which can modulate chromatin structure and stabilize binding of transcription factors that recognize these modifications. At the β-globin locus and several other loci, however, histone hyperacetylation extends beyond the promoter, over tens of kilobases; we term such patterns of histone modifications “hyperacetylated domains.” Little is known of either the mechanism by which these domains form or their function. Here, we show that domain formation within the murine β-globin locus occurs before either high-level gene expression or erythroid commitment. Analysis of β-globin alleles harboring deletions of promoters or the locus control region demonstrates that these sequences are not required for domain formation, suggesting the existence of additional regulatory sequences within the locus. Deletion of embryonic globin gene promoters, however, resulted in the formation of a hyperacetylated domain over these genes in definitive erythroid cells, where they are otherwise inactive. Finally, sequences within β-globin domains exhibit hyperacetylation in a context-dependent manner, and domains are maintained when transcriptional elongation is inhibited. These data narrow the range of possible mechanisms by which hyperacetylated domains form.

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Adenot, P. G., Y. Mercier, J. P. Renard, and E. M. Thompson. "Differential H4 acetylation of paternal and maternal chromatin precedes DNA replication and differential transcriptional activity in pronuclei of 1-cell mouse embryos." Development 124, no. 22 (November 15, 1997): 4615–25. http://dx.doi.org/10.1242/dev.124.22.4615.

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In the mouse embryo, transcriptional activation begins during S/G2 phase of the first cell cycle when paternal and maternal chromatin are still in separate nuclear entities within the same cytoplasm. At this time, the male pronucleus exhibits greater transcriptional activity than the female pronucleus. Since acetylation of histones in the nucleosome octamer exerts a regulatory influence on gene expression, we investigated changes in histone acetylation during the remodeling of paternal and maternal chromatin from sperm entry through to minor genome activation and mitosis. We found (1) neither mature sperm nor metaphase II maternal chromatin stained for hyperacetylated histone H4; (2) immediately following fertilization, hyperacetylated H4 was associated with paternal but not maternal chromatin while, in parthenogenetically activated oocytes, maternal chromatin became hyperacetylated; (3) in zygotes, differential levels and patterns of hyperacetylated H4 between male and female pronuclei persisted throughout most of G1 with histone deacetylases and acetyltransferases already active at this time; (4) when transcriptional differences are observed in S/G2, male and female pronuclei have equivalent levels of H4 hyperacetylation and DNA replication was not required to attain this equivalence and (5) in contrast to the lack of H4 hyperacetylation on gametic chromatin, chromosomes at the first mitosis showed distinct banding patterns of H4 hyperacetylation. These results suggest that sperm chromatin initially out-competes maternal chromatin for the pool of hyperacetylated H4 in the oocyte, that hyperacetylated H4 participates in the process of histone-protamine exchange in the zygote, and that differences in H4 acetylation in male and female pronuclei during G1 are translated across DNA replication to transcriptional differences in S/G2. Prior to fertilization, neither paternal nor maternal chromatin show memory of H4 hyperacetylation patterns but, by the end of the first cell cycle, before major zygotic genome activation at the 2-cell stage, chromosomes already show hyperacetylated H4 banding patterns.

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Shepard, Blythe D., Dean J. Tuma, and Pamela L. Tuma. "Chronic Ethanol Consumption Induces Global Hepatic Protein Hyperacetylation." Alcoholism: Clinical and Experimental Research 34, no. 2 (February 2010): 280–91. http://dx.doi.org/10.1111/j.1530-0277.2009.01091.x.

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Niles, Lennard P., Yi Pan, Sean Kang, and Ayush Lacoul. "Melatonin induces histone hyperacetylation in the rat brain." Neuroscience Letters 541 (April 2013): 49–53. http://dx.doi.org/10.1016/j.neulet.2013.01.050.

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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 (September 23, 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 hyperacetylation is unknown, as in vitro studies show no effect of the H3K4me3 modification on histone peptide acetylation by Gcn5. To determine how H3K4me3 binding by Sgf29 leads to histone hyperacetylation by Gcn5, we used differential fluorescent labeling of histones to monitor acetylation of individual subpopulations of methylated and unmodified nucleosomes in a mixture. We find that the SAGA HAT module preferentially acetylates H3K4me3 nucleosomes in a mixture containing excess unmodified nucleosomes and that this effect requires the Tudor domain of Sgf29. The H3K4me3 mark promotes processive, multisite acetylation of histone H3 by Gcn5 that can account for the different acetylation patterns established by SAGA at promoters versus coding regions. Our results establish a model for Sgf29 function at gene promoters and define a mechanism governing crosstalk between histone modifications.

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Párrizas, Marcelina, Miguel A. Maestro, Sylvia F. Boj, Amaya Paniagua, Roser Casamitjana, Ramon Gomis, Francisca Rivera, and Jorge Ferrer. "Hepatic Nuclear Factor 1-α Directs Nucleosomal Hyperacetylation to Its Tissue-Specific Transcriptional Targets." Molecular and Cellular Biology 21, no. 9 (May 1, 2001): 3234–43. http://dx.doi.org/10.1128/mcb.21.9.3234-3243.2001.

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ABSTRACT Mutations in the gene encoding hepatic nuclear factor 1-α (HNF1-α) cause a subtype of human diabetes resulting from selective pancreatic β-cell dysfunction. We have analyzed mice lacking HNF1-α to study how this protein controls β-cell-specific transcription in vivo. We show that HNF1-α is essential for the expression ofglut2 glucose transporter and L-type pyruvate kinase (pklr) genes in pancreatic insulin-producing cells, whereas in liver, kidney, or duodenum tissue, glut2 andpklr expression is maintained in the absence of HNF1-α. HNF1-α nevertheless occupies the endogenous glut2 andpklr promoters in both pancreatic islet and liver cells. However, it is indispensable for hyperacetylation of histones inglut2 and pklr promoter nucleosomes in pancreatic islets but not in liver cells, where glut2 andpklr chromatin remains hyperacetylated in the absence of HNF1-α. In contrast, the phenylalanine hydroxylase promoter requires HNF1-α for transcriptional activity and localized histone hyperacetylation only in liver tissue. Thus, different HNF1-α target genes have distinct requirements for HNF1-α in either pancreatic β-cells or liver cells. The results indicate that HNF1-α occupies target gene promoters in diverse tissues but plays an obligate role in transcriptional activation only in cellular- and promoter-specific contexts in which it is required to recruit histone acetylase activity. These findings provide genetic evidence based on a live mammalian system to establish that a single activator can be essential to direct nucleosomal hyperacetylation to transcriptional targets.

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Burlibaşa, Liliana, Andreea Carmen Ionescu, and Delia-Mihaela Dragusanu. "Histone hyperacetylation and DNA methylation interplay during murine spermatogenesis." Zygote 27, no. 05 (August 15, 2019): 305–14. http://dx.doi.org/10.1017/s0967199419000303.

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SummaryMale germ cell development is a critical period during which epigenetic patterns are established and maintained. The progression from diploid spermatogonia to haploid spermatozoa involves the incorporation of testis-specific histone variants, mitotic and meiotic divisions, haploid gene expression, histone–protamine transitions and massive epigenetic reprogramming. Understanding the protein players and the epigenetic mark network involved in the setting of the epigenetic programme in spermatogenesis is an exciting new clue in the field of reproductive biology with translational outcomes. As information in the existing literature regarding cross-talk between DNA methylation and histone hyperacetylation in the advanced stages of murine spermatogenesis is still scarce and controversial we have investigated the effect of a DNA-methyltransferase inhibitor, 5-aza-2′-deoxycytidine, at the cytological and molecular level (by transmission electron microscopy, immunocytochemistry and immunoprecipitation methods). Our results revealed an important role for regulation of DNA methylation in controlling histone hyperacetylation and chromatin remodelling during spermatogenesis.

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Lee, Jin-Kwan, Janet Lee, Heounjeong Go, Chang Geun Lee, Suhyeon Kim, Hyun-Soo Kim, Hyeseong Cho, Kyeong Sook Choi, Geun-Hyoung Ha, and Chang-Woo Lee. "Oncogenic microtubule hyperacetylation through BEX4-mediated sirtuin 2 inhibition." Cell Death & Disease 7, no. 8 (August 2016): e2336-e2336. http://dx.doi.org/10.1038/cddis.2016.240.

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Sarg, Bettina, Wilfried Helliger, Heribert Talasz, Elisavet Koutzamani, and Herbert H. Lindner. "Histone H4 Hyperacetylation Precludes Histone H4 Lysine 20 Trimethylation." Journal of Biological Chemistry 279, no. 51 (September 28, 2004): 53458–64. http://dx.doi.org/10.1074/jbc.m409099200.

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Libertini, L. J., J. Ausió, K. E. van Holde, and E. W. Small. "Histone hyperacetylation. Its effects on nucleosome core particle transitions." Biophysical Journal 53, no. 4 (April 1988): 477–87. http://dx.doi.org/10.1016/s0006-3495(88)83126-6.

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Lu, B., D. J. Antoine, K. Kwan, P. Lundback, H. Wahamaa, H. Schierbeck, M. Robinson, et al. "JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation." Proceedings of the National Academy of Sciences 111, no. 8 (January 27, 2014): 3068–73. http://dx.doi.org/10.1073/pnas.1316925111.

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Ausio, Juan, and K. E. Van Holde. "Histone hyperacetylation: its effects on nucleosome conformation and stability." Biochemistry 25, no. 6 (March 1986): 1421–28. http://dx.doi.org/10.1021/bi00354a035.

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Li, Lin, Sriram Jayabal, Mohammad Ghorbani, Lisa-Marie Legault, Serge McGraw, Alanna J. Watt, and Xiang-Jiao Yang. "ATAT1 regulates forebrain development and stress-induced tubulin hyperacetylation." Cellular and Molecular Life Sciences 76, no. 18 (April 5, 2019): 3621–40. http://dx.doi.org/10.1007/s00018-019-03088-3.

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Gryder, Berkley E., Silvia Pomella, Carly Sayers, Xiaoli S. Wu, Young Song, Anna M. Chiarella, Sukriti Bagchi, et al. "Histone hyperacetylation disrupts core gene regulatory architecture in rhabdomyosarcoma." Nature Genetics 51, no. 12 (November 29, 2019): 1714–22. http://dx.doi.org/10.1038/s41588-019-0534-4.

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Granit, Avital, Nino Tetro, Miri Shmuel, Tamar Peretz, and Sara Eyal. "Lacosamide at therapeutic concentrations induces histone hyperacetylation in vitro." Epilepsia Open 3, no. 4 (October 30, 2018): 535–39. http://dx.doi.org/10.1002/epi4.12269.

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Blottiere, Herve M., Bruno Buecher, Jean-Paul Galmiche, and Christine Cherbut. "Molecular analysis of the effect of short-chain fatty acids on intestinal cell proliferation." Proceedings of the Nutrition Society 62, no. 1 (February 2003): 101–6. http://dx.doi.org/10.1079/pns2002215.

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Short-chain fatty acids (SCFA), particularly butyrate, were shown to regulate cell proliferation in vitro and in vivo. Indeed, butyrate is the major fuel for colonic epithelial cells, and it can influence cell proliferation through the release of growth factors or gastrointestinal peptides such as gastrin, or through modulation of mucosal blood flow. Lastly, SCFA can act directly on genes regulating cell proliferation, and butyrate is the main SCFA to display such an effect. Butyrate inhibits histone deacetylase, which will allow histone hyperacetylation. Such hyperacetylation leads to transcription of several genes, including p21/Cipl. Moreover, it will allow cyclin D3 hyper-expression by inhibiting its degradation. The induction of the cyclin-dependent kinase inhibitory protein p21/Cipl accounts for cell arrest in the Gl phase of the cell cycle. However, in the absence of p21 other mechanisms are initiated, leading to inhibition of cell proliferation.

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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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Xie, Xina, Xuhong Song, Song Yuan, Haitao Cai, Yequn Chen, Xiaolan Chang, Bin Liang, and Dongyang Huang. "Histone acetylation regulates orphan nuclear receptor NR4A1 expression in hypercholesterolaemia." Clinical Science 129, no. 12 (October 30, 2015): 1151–61. http://dx.doi.org/10.1042/cs20150346.

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(i) mRNA levels of orphan nuclear receptor NR4A1 positively correlate with increased total cholesterol and low-density lipoprotein cholesterol levels in plasma. (ii) Histone H3 hyperacetylation is involved in hypercholesterolaemia-induced NR4A1 expression in monocytes. (iii) NR4A1 mediates self-protection responses in hypercholesterolaemia-induced inflammation.

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Tong, Dan, Gabriele G. Schiattarella, Nan Jiang, Francisco Altamirano, Pamela A. Szweda, Abdallah Elnwasany, Dong I. Lee, et al. "NAD + Repletion Reverses Heart Failure With Preserved Ejection Fraction." Circulation Research 128, no. 11 (May 28, 2021): 1629–41. http://dx.doi.org/10.1161/circresaha.120.317046.

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Rationale: Heart failure with preserved ejection fraction (HFpEF) is a mortal clinical syndrome without effective therapies. We recently demonstrated in mice that a combination of metabolic and hypertensive stress recapitulates key features of human HFpEF. Objective: Using this novel preclinical HFpEF model, we set out to define and manipulate metabolic dysregulations occurring in HFpEF myocardium. Methods and Results: We observed impairment in mitochondrial fatty acid oxidation associated with hyperacetylation of key enzymes in the pathway. Downregulation of sirtuin 3 and deficiency of NAD + secondary to an impaired NAD + salvage pathway contribute to this mitochondrial protein hyperacetylation. Impaired expression of genes involved in NAD + biosynthesis was confirmed in cardiac tissue from patients with HFpEF. Supplementing HFpEF mice with nicotinamide riboside or a direct activator of NAD + biosynthesis led to improvement in mitochondrial function and amelioration of the HFpEF phenotype. Conclusions: Collectively, these studies demonstrate that HFpEF is associated with myocardial mitochondrial dysfunction and unveil NAD + repletion as a promising therapeutic approach in the syndrome.

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Li, Xiao-Xue, Jun Lu, Yan-Mei Zhao, and Bai-Qu Huang. "Function of c-Fos-like and c-Jun-like Proteins on Trichostatin A-induced G2/M Arrest in Physarum polycephalum." Acta Biochimica et Biophysica Sinica 37, no. 11 (November 1, 2005): 767–72. http://dx.doi.org/10.1111/j.1745-7270.2005.00105.x.

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Abstract The homologs of transcription factors c-Fos and c-Jun have been detected in slime mold Physarum polycephalum during progression of the synchronous cell cycle. Here we demonstrated that c-Fos-like and c-Jun-like proteins participated in G2/M transition by the regulation of the level of Cyclin B1 protein in P. polycephalum. The study of antibody neutralization revealed that interruption of the functions of c-Fos-like and c-Jun-like proteins resulted in G2/M transition arrest, implicating their functional roles in cell cycle control. When G2/M transition was blocked by histone deacetylase inhibitor trichostatin A, changes in c-Fos- and c-Jun-like protein levels, and hyperacetylation of c-Jun-like protein, were observed. The data suggest that in P. polycephalum, c-Fos- and c-Jun-like proteins may be the key factors in the regulation of histone acetylation-related G2/M transition, involving the coordinated expression and hyperacetylation of these proteins.

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Lombard, David B., Frederick W. Alt, Hwei-Ling Cheng, Jakob Bunkenborg, Ryan S. Streeper, Raul Mostoslavsky, Jennifer Kim, et al. "Mammalian Sir2 Homolog SIRT3 Regulates Global Mitochondrial Lysine Acetylation." Molecular and Cellular Biology 27, no. 24 (October 8, 2007): 8807–14. http://dx.doi.org/10.1128/mcb.01636-07.

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ABSTRACT Homologs of the Saccharomyces cerevisiae Sir2 protein, sirtuins, promote longevity in many organisms. Studies of the sirtuin SIRT3 have so far been limited to cell culture systems. Here, we investigate the localization and function of SIRT3 in vivo. We show that endogenous mouse SIRT3 is a soluble mitochondrial protein. To address the function and relevance of SIRT3 in the regulation of energy metabolism, we generated and phenotypically characterized SIRT3 knockout mice. SIRT3-deficient animals exhibit striking mitochondrial protein hyperacetylation, suggesting that SIRT3 is a major mitochondrial deacetylase. In contrast, no mitochondrial hyperacetylation was detectable in mice lacking the two other mitochondrial sirtuins, SIRT4 and SIRT5. Surprisingly, despite this biochemical phenotype, SIRT3-deficient mice are metabolically unremarkable under basal conditions and show normal adaptive thermogenesis, a process previously suggested to involve SIRT3. Overall, our results extend the recent finding of lysine acetylation of mitochondrial proteins and demonstrate that SIRT3 has evolved to control reversible lysine acetylation in this organelle.

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Fu, Qi, Robert A. McKnight, Xing Yu, Laiyi Wang, Christopher W. Callaway, and Robert H. Lane. "Uteroplacental insufficiency induces site-specific changes in histone H3 covalent modifications and affects DNA-histone H3 positioning in day 0 IUGR rat liver." Physiological Genomics 20, no. 1 (December 15, 2004): 108–16. http://dx.doi.org/10.1152/physiolgenomics.00175.2004.

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Uteroplacental insufficiency and subsequent intrauterine growth retardation (IUGR) increase the risk of adult onset insulin resistance and dyslipidemia in humans and rats. IUGR rats are further characterized by postnatal alterations in hepatic PPAR-γ coactivator (PGC-1) and carnitine-palmitoyl-transferase I (CPTI) expression, as well as overall hyperacetylation of histone H3. However, it is unknown whether the histone H3 hyperacetylation is site specific or relates to the changes in gene expression previously described in IUGR rats. We therefore hypothesized that uteroplacental insufficiency causes site-specific modifications in hepatic H3 acetylation and affects the association of acetylated histone H3 with PGC-1 and CPTI promoter sequences. Uteroplacental insufficiency was used to produce asymmetrical IUGR rats. IUGR significantly increased acetylation of H3 lysine-9 (H3/K9), lysine-14 (H3/K14), and lysine-18 (H3/K18) at day 0 of life, and these changes occurred in association with decreased nuclear protein levels of histone deacetylase 1 (HDAC1) and HDAC activity. Chromatin immunoprecipitation using acetyl-H3/K9 antibody and day 0 chromatin revealed that uteroplacental insufficiency affected the association between acetylated H3/K9 and the promoters of PGC-1 and CPTI, respectively, in IUGR liver. At day 21 of life, the neonatal pattern of H3 hyperacetylation persisted only in the IUGR males. We conclude that uteroplacental insufficiency increases H3 acetylation in a site-specific manner in IUGR liver and that these changes persist in male IUGR animals. The altered association of the PGC-1 and CPTI promoters with acetylated H3/K9 correlates with previous reports of IUGR altering the expression of these genes. We speculate that in utero alterations of chromatin structure contribute to fetal programming.

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Arima, Yuichiro, Yoshiko Nakagawa, Toru Takeo, Toshifumi Ishida, Toshihiro Yamada, Shinjiro Hino, Mitsuyoshi Nakao, et al. "Murine neonatal ketogenesis preserves mitochondrial energetics by preventing protein hyperacetylation." Nature Metabolism 3, no. 2 (February 2021): 196–210. http://dx.doi.org/10.1038/s42255-021-00342-6.

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37

Celic, Ivana, Alain Verreault, and Jef D. Boeke. "Histone H3 K56 Hyperacetylation Perturbs Replisomes and Causes DNA Damage." Genetics 179, no. 4 (June 24, 2008): 1769–84. http://dx.doi.org/10.1534/genetics.108.088914.

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38

Tomczyk, Mateusz M., Kyle G. Cheung, Bo Xiang, Prasoon Agarwal, Stephanie M. Kereliuk, John A. Wilkins, and Vernon W. Dolinsky. "Mitochondrial Protein Hyperacetylation in Rodents with Doxorubicin‐Induced Cardiac Dysfunction." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04617.

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39

Bartling, Toni R., and Mitchell L. Drumm. "Oxidative Stress CausesIL8Promoter Hyperacetylation in Cystic Fibrosis Airway Cell Models." American Journal of Respiratory Cell and Molecular Biology 40, no. 1 (January 2009): 58–65. http://dx.doi.org/10.1165/rcmb.2007-0464oc.

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40

Mosley, Amber L., and Sabire Özcan. "Glucose Regulates Insulin Gene Transcription by Hyperacetylation of Histone H4." Journal of Biological Chemistry 278, no. 22 (March 28, 2003): 19660–66. http://dx.doi.org/10.1074/jbc.m212375200.

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41

Perrella, Giorgio, M. Federica Consiglio, Riccardo Aiese-Cigliano, Gaetana Cremona, Eugenio Sanchez-Moran, Lucia Barra, Angela Errico, Ray A. Bressan, F. Christopher H. Franklin, and Clara Conicella. "Histone hyperacetylation affects meiotic recombination and chromosome segregation in Arabidopsis." Plant Journal 62, no. 5 (March 2, 2010): 796–806. http://dx.doi.org/10.1111/j.1365-313x.2010.04191.x.

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42

Sasaki, K., T. Ito, N. Nishino, S. Khochbin, and M. Yoshida. "Real-time imaging of histone H4 hyperacetylation in living cells." Proceedings of the National Academy of Sciences 106, no. 38 (September 3, 2009): 16257–62. http://dx.doi.org/10.1073/pnas.0902150106.

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43

Oliva, R., D. P. Bazett-Jones, L. Locklear, and G. H. Dixon. "Histone hyperacetylation can induce unfolding of the nucleosome core particle." Nucleic Acids Research 18, no. 9 (1990): 2739–47. http://dx.doi.org/10.1093/nar/18.9.2739.

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Walley, Justin W., Zhouxin Shen, Maxwell R. McReynolds, Eric A. Schmelz, and Steven P. Briggs. "Fungal-induced protein hyperacetylation in maize identified by acetylome profiling." Proceedings of the National Academy of Sciences 115, no. 1 (December 19, 2017): 210–15. http://dx.doi.org/10.1073/pnas.1717519115.

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Lysine acetylation is a key posttranslational modification that regulates diverse proteins involved in a range of biological processes. The role of histone acetylation in plant defense is well established, and it is known that pathogen effector proteins encoding acetyltransferases can directly acetylate host proteins to alter immunity. However, it is unclear whether endogenous plant enzymes can modulate protein acetylation during an immune response. Here, we investigate how the effector molecule HC-toxin (HCT), a histone deacetylase inhibitor produced by the fungal pathogen Cochliobolus carbonum race 1, promotes virulence in maize through altering protein acetylation. Using mass spectrometry, we globally quantified the abundance of 3,636 proteins and the levels of acetylation at 2,791 sites in maize plants treated with HCT as well as HCT-deficient or HCT-producing strains of C. carbonum. Analyses of these data demonstrate that acetylation is a widespread posttranslational modification impacting proteins encoded by many intensively studied maize genes. Furthermore, the application of exogenous HCT enabled us to show that the activity of plant-encoded enzymes (histone deacetylases) can be modulated to alter acetylation of nonhistone proteins during an immune response. Collectively, these results provide a resource for further mechanistic studies examining the regulation of protein function by reversible acetylation and offer insight into the complex immune response triggered by virulent C. carbonum.

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McLendon, Patrick M., Bradley S. Ferguson, Hanna Osinska, Md Shenuarin Bhuiyan, Jeanne James, Timothy A. McKinsey, and Jeffrey Robbins. "Tubulin hyperacetylation is adaptive in cardiac proteotoxicity by promoting autophagy." Proceedings of the National Academy of Sciences 111, no. 48 (November 17, 2014): E5178—E5186. http://dx.doi.org/10.1073/pnas.1415589111.

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Rosencrance, Celeste D., Haneen N. Ammouri, Qi Yu, Tiffany Ge, Emily J. Rendleman, Stacy A. Marshall, and Kyle P. Eagen. "Chromatin Hyperacetylation Impacts Chromosome Folding by Forming a Nuclear Subcompartment." Molecular Cell 78, no. 1 (April 2020): 112–26. http://dx.doi.org/10.1016/j.molcel.2020.03.018.

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47

Wan, M. "MECP2 truncating mutations cause histone H4 hyperacetylation in Rett syndrome." Human Molecular Genetics 10, no. 10 (May 1, 2001): 1085–92. http://dx.doi.org/10.1093/hmg/10.10.1085.

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Xu, Li-Hui, Fang-Fang Mu, Jian-Hong Zhao, Qiang He, Cui-Li Cao, Hui Yang, Qi Liu, Xue-Hui Liu, and Su-Ju Sun. "Lead Induces Apoptosis and Histone Hyperacetylation in Rat Cardiovascular Tissues." PLOS ONE 10, no. 6 (June 15, 2015): e0129091. http://dx.doi.org/10.1371/journal.pone.0129091.

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Krajewski, Wladyslaw A. "Effect ofin vivoHistone Hyperacetylation on the State of Chromatin Fibers." Journal of Biomolecular Structure and Dynamics 16, no. 5 (April 1999): 1097–106. http://dx.doi.org/10.1080/07391102.1999.10508318.

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Wang, Yao, Sabine Groeger, Jiawen Yong, and Sabine Ruf. "Orthodontic Compression Enhances Macrophage M2 Polarization via Histone H3 Hyperacetylation." International Journal of Molecular Sciences 24, no. 4 (February 4, 2023): 3117. http://dx.doi.org/10.3390/ijms24043117.

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Orthodontic tooth movement is a complex periodontal remodeling process triggered by compression that involves sterile inflammation and immune responses. Macrophages are mechanically sensitive immune cells, but their role in orthodontic tooth movement is unclear. Here, we hypothesize that orthodontic force can activate macrophages, and their activation may be associated with orthodontic root resorption. After force-loading and/or adiponectin application, the migration function of macrophages was tested via scratch assay, and Nos2, Il1b, Arg1, Il10, ApoE, and Saa3 expression levels were detected using qRT-PCR. Furthermore, H3 histone acetylation was measured using an acetylation detection kit. The specific inhibitor of H3 histone, I-BET762, was deployed to observe its effect on macrophages. In addition, cementoblasts were treated with macrophage-conditioned medium or compression force, and OPG production and cellular migration were measured. We further detected Piezo1 expression in cementoblasts via qRT-PCR and Western-blot, and its effect on the force-induced impairment of cementoblastic functions was also analyzed. Compressive force significantly inhibited macrophage migration. Nos2 was up-regulated 6 h after force-loading. Il1b, Arg1, Il10, Saa3, and ApoE increased after 24 h. Meanwhile, higher H3 histone acetylation was detected in the macrophages subjected to compression, and I-BET762 dampened the expression of M2 polarization markers (Arg1 and Il10). Lastly, even though the activated macrophage-conditioned medium showed no effect on cementoblasts, compressive force directly impaired cementoblastic function by enhancing mechanoreceptor Piezo1. Compressive force activates macrophages; specifically, it causes M2 polarization via H3 histone acetylation in the late stage. Compression-induced orthodontic root resorption is macrophage-independent, but it involves the activation of mechanoreceptor Piezo1.

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