Relevant bibliographies by topics / Non-histone acetylation

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Academic literature on the topic 'Non-histone acetylation'

Author: Grafiati
Published: 4 June 2021
Last updated: 6 February 2022

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Journal articles on the topic "Non-histone acetylation"

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Demyanenko, Svetlana, and Svetlana Sharifulina. "The Role of Post-Translational Acetylation and Deacetylation of Signaling Proteins and Transcription Factors after Cerebral Ischemia: Facts and Hypotheses." International Journal of Molecular Sciences 22, no. 15 (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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Glozak, Michele A., Nilanjan Sengupta, Xiaohong Zhang, and Edward Seto. "Acetylation and deacetylation of non-histone proteins." Gene 363 (December 2005): 15–23. http://dx.doi.org/10.1016/j.gene.2005.09.010.

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Narita, Takeo, Brian T. Weinert, and Chunaram Choudhary. "Functions and mechanisms of non-histone protein acetylation." Nature Reviews Molecular Cell Biology 20, no. 3 (November 22, 2018): 156–74. http://dx.doi.org/10.1038/s41580-018-0081-3.

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Han, Qiuju, Jun Lu, Jizhou Duan, Dongmei Su, Xiaozhe Hou, Fen Li, Xiuli Wang, and Baiqu Huang. "Gcn5- and Elp3-induced histone H3 acetylation regulates hsp70 gene transcription in yeast." Biochemical Journal 409, no. 3 (January 15, 2008): 779–88. http://dx.doi.org/10.1042/bj20070578.

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The purpose of this study was to elucidate the mechanisms by which histone acetylation participates in transcriptional regulation of hsp70 (heat-shock protein 70) genes SSA3 and SSA4 in yeast. Our results indicated that histone acetylation was required for the transcriptional activation of SSA3 and SSA4. The HATs (histone acetyltransferases) Gcn5 (general control non-derepressible 5) and Elp3 (elongation protein 3) modulated hsp70 gene transcription by affecting the acetylation status of histone H3. Although the two HATs possessed overlapping function regarding the acetylation of histone H3, they affected hsp70 gene transcription in different ways. The recruitment of Gcn5 was Swi/Snf-dependent and was required for HSF (heat-shock factor) binding and affected RNAPII (RNA polymerase II) recruitment, whereas Elp3 exerted its roles mainly through affecting RNAPII elongation. These results provide insights into the effects of Gcn5 and Elp3 in hsp70 gene transcription and underscore the importance of histone acetylation for transcriptional initiation and elongation in hsp genes.
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Yan, Li-Ying, Jie Yan, Jie Qiao, Pan-Lin Zhao, and Ping Liu. "Effects of oocyte vitrification on histone modifications." Reproduction, Fertility and Development 22, no. 6 (2010): 920. http://dx.doi.org/10.1071/rd09312.

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Vitrification has been widely used as an assisted reproductive technology in animals and humans, yet the impact of oocyte vitrification and warming on survival and histone modifications has to be evaluated. In the present study, the survival of mouse MII oocytes was assessed after freezing, as were changes in histone 3 lysine 9 (H3K9) dimethylation, histone 4 lysine 5 (H4K5) acetylation and histone 3 lysine 14 (H3K14) acetylation. The results show that, in oocytes subjected to vitrification, H3K9 methylation and H4K5 acetylation were increased. H3K14 acetylation could not be detected in either non-vitrified or vitrified oocytes. Oocytes are very sensitive to changes in H3K9 and H4K5 following vitrification. Both these histone modifications could be useful markers to monitor epigenetic perturbations induced by various experimental vitrification protocols and eventually for optimising the cryopreservation of human oocytes.
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Kuninger, David, James Lundblad, Anthony Semirale, and Peter Rotwein. "A non-isotopic in vitro assay for histone acetylation." Journal of Biotechnology 131, no. 3 (September 2007): 253–60. http://dx.doi.org/10.1016/j.jbiotec.2007.07.498.

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Ito, K. "Impact of post-translational modifications of proteins on the inflammatory process." Biochemical Society Transactions 35, no. 2 (March 20, 2007): 281–83. http://dx.doi.org/10.1042/bst0350281.

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PTM (post-translational modification) is the chemical modification of a protein after its translation. The well-studied PTM is phosphorylation, but, recently, PTMs have been re-focused by extensive studies on histone modifications and the discovery of the ubiquitin system. Histone acetylation is the well-established epigenetic regulator for gene expression. Recent studies show that different patterns of PTMs and cross-talk of individual modifications (acetylation, methylation, phosphorylation) are keys of gene regulation (known as the ‘histone code’). As well as histone, non-histone proteins are also targets of acetylation. For instance, NF-κB (nuclear factor κB), a transcriptional factor, is regulated dynamically by acetylation/deacetylation. Acetylation of NF-κB [RelA (p65)] at Lys310 enhances its transcriptional activity, which is inhibited by SIRT1 deacetylase, type III HDAC (histone deacetylase). We also found that acetylated NF-κB preferentially bound to the IL-8 (interleukin 8) gene promoter, but not to GM-CSF (granulocyte/macrophage colony-stimulating factor), suggesting NF-κB acetylation is involved in selective gene induction as well as an increased level of transcription. A receptor of glucocorticoid, a potent anti-inflammatory agent, is also a target of acetylation. The glucocorticoid receptor is highly acetylated after ligand binding but its deacetylation is necessary for gene repression through binding to NF-κB. As well as acetylation, other PTMs, such as nitration, carbonylation and ubiquitination on transcriptional/nuclear factors, are taking part in the inflammatory process. Cross-talk of individual modifications on proteins deserves further evaluation in the future (as ‘protein code’).
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Wee, G., S. H. Kim, K. P. Kim, S. Yeo, D. B. Koo, S. J. Moon, K. K. Lee, and Y. M. Han. "134INCOMPLETE HISTONE ACETYLATION OF SOMATIC CHROMATIN IN BOVINE OOCYTES." Reproduction, Fertility and Development 16, no. 2 (2004): 189. http://dx.doi.org/10.1071/rdv16n1ab134.

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Histone acetylation as an important regulatory mechanism of chromatin structure preceeding zygotic gene expression in early embryo development. After fertilization, transcriptional activation of the embryo begins during the S/G2 phase of the first cell cycle. However, the precise mechanism underlying activation of zygotic transcription remains to be understood, especially in bovine nuclear transfer (NT) embryos. It is known that acetylation of histone H4 lysine 5 (H4K5) represents hyperacetylation state, which is correlated with gene expression. In this study, the acetylation of H4K5 was observed during pronuclear formation by using immunofluorescence analysis with anti-AcH4K5. Our data were analyzed by the general linear models (GLM) procedure of the SAS. In IVF embryos, acetylation of H4K5 occurred on the paternal chromatin at 8h after fertilization but did not occur on the maternal chromatin until 10h after fertilization. Reconstructed oocytes with deactylated somatic cell nuclei began to show signs of acetylation on chromatin at 3h after fusion. When acetylation intensity was calculated using an image analyzer, IVF embryos presented a higher acetylation signal than NT embryos (P<0.05). To induce hyperacetylation in NT embryos, somatic cells were exposed to trichostatin A (TSA, 1μM for 60h), a specific inhibitor of histone deacetylase (HDAC), prior to NT. Acetylated signals of H4K5 increased significantly in TSA-treated cells as compared with non-treated cells (P<0.05). The reconstructed embryos with TSA-treated cells showed a higher fluorescence intensity than the oocytes with non-treated cells (P<0.05), but weak signals compared to IVF embryos. Thus, the results demonstrated low histone acetylation level of somatic cell nuclei after NT during the zygotic progress. Our findings suggest that developmental failures of NT embryos may be due to incomplete chromatin remodeling of somatic cell nuclei during early embryonic development.
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Bertos, Nicholas R., Audrey H. Wang, and Xiang-Jiao Yang. "Class II histone deacetylases: Structure, function, and regulation." Biochemistry and Cell Biology 79, no. 3 (June 1, 2001): 243–52. http://dx.doi.org/10.1139/o01-032.

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Acetylation of histones, as well as non-histone proteins, plays important roles in regulating various cellular processes. Dynamic control of protein acetylation levels in vivo occurs through the opposing actions of histone acetyltransferases and histone deacetylases (HDACs). In the past few years, distinct classes of HDACs have been identified in mammalian cells. Class I members, such as HDAC1, HDAC2, HDAC3, and HDAC8, are well-known enzymatic transcriptional corepressors homologous to yeast Rpd3. Class II members, including HDAC4, HDAC5, HDAC6, HDAC7, and HDAC9, possess domains similar to the deacetylase domain of yeast Hda1. HDAC4, HDAC5, and HDAC7 function as transcriptional corepressors that interact with the MEF2 transcription factors and the N-CoR, BCoR, and CtBP corepressors. Intriguingly, HDAC4, HDAC5, and probably HDAC7 are regulated through subcellular compartmentalization controlled by site-specific phosphorylation and binding of 14-3-3 proteins; the regulation of these HDACs is thus directly linked to cellular signaling networks. Both HDAC6 and HDAC9 possess unique structural modules, so they may have special biological functions. Comprehension of the structure, function, and regulation of class II deacetylases is important for elucidating how acetylation regulates functions of histones and other proteins in vivo.Key words: histone acetylation, protein acetylation, histone deacetylase, 14-3-3 proteins.
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Narita, Takeo, Brian T. Weinert, and Chunaram Choudhary. "Author Correction: Functions and mechanisms of non-histone protein acetylation." Nature Reviews Molecular Cell Biology 20, no. 8 (July 2, 2019): 508. http://dx.doi.org/10.1038/s41580-019-0156-9.

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Dissertations / Theses on the topic "Non-histone acetylation"

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Pourhanifeh-Lemeri, Roghayeh. "Identification of Non-histone Acetylation Targets in Saccharomyces cerevisiae." Thesis, Université d'Ottawa / University of Ottawa, 2012. http://hdl.handle.net/10393/22885.

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Lysine acetylation is a conserved post-translational modification (PTM) which was traditionally believed to be limited to histones and the regulation of gene expression. However, recent proteomic studies have identified lysine acetylation on proteins implicated in virtually all cellular processes indicating that this PTM plays a global regulatory role. Indeed, in humans, aberrance of lysine acetyltransferase (KAT) activity is associated with various pathogenesis. To date, over 2500 human proteins are known to be acetylated in vivo, but very few acetylations have been linked to specific KATs. Hence, to understand the biological relevance of KATs and acetylation in human pathology, it is important to learn about the mechanism regulating KAT activity and the identity of their in vivo targets. This is a complex task and will require the use of model organisms and system biology approaches. The work presented here explores the significance of self-acetylation in regulating KAT function by focusing on the highly NuA4 lysine acetyltransferase in the model organism Saccharomyces cerevisiae or budding yeast. Using genetics and biochemical assays I have identified NuA4 subunit Epl1 as a novel in vivo NuA4 substrate. I have also shown that Epl1 acetylation regulates NuA4 function at elevated temperatures. In an attempt to identify new biological processes regulated by yeast KATs and putative novel substrates, I have also performed a genome-wide synthetic dosage lethality screen with six non-essential yeast KATs; Hat1, Rtt109, Hpa2, Sas3, Sas2, and Elp3. My screen identified largely distinct sets of genetic interactions for each KAT suggesting that each KAT has specific cellular functions. Together, this study demonstrates the importance of auto-acetylation in regulating KAT function and the diversity of cellular processes impacted by KAT activity in vivo.
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Mortenson, Jeffrey Benjamin. "Histone Deacetylase 6 (HDAC6) Is Critical for Tumor Cell Survival and Promotes the Pro-Survival Activity of 14-3-3ζ viaDeacetylation of Lysines Within the14-3-3ζ Binding Pocket." BYU ScholarsArchive, 2015. https://scholarsarchive.byu.edu/etd/5568.

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Our understanding of non-histone acetylation as a means of cellular regulation is in its infancy. Using a mass spectrometry approach we identified acetylated lysine residues and monitored acetylation changes across the proteome as a consequence of metabolic stress (hypoxia). We observed changes in acetylation status of non-histone lysines in tumor cells. Through the use of small molecule inhibitors of histone deacetylase enzymes (HDACs) and siRNA screening identified HDAC6 as a pro-survival regulator of lysine acetylation during hypoxia. The phospho-binding protein 14-3-3ζ acts as a signaling hub controlling a network of interacting partners and oncogenic pathways. We show here that lysines within the 14-3-3ζ binding pocket and protein-protein interface can be modified by acetylation. The positive charge on two of these lysines, K49 and K120, is critical for coordinating 14-3-3ζ-phosphoprotein interactions. Through screening, we identified HDAC6 as the K49/K120 deacetylase. Inhibition of HDAC6 blocks 14-3-3ζ interactions with two well-described interacting partners, Bad and AS160, which triggers their dephosphorylation at S112 and T642, respectively. Expression of an acetylation-refractory K49R/K120R mutant of 14-3-3ζ rescues both the HDAC6 inhibitor-induced loss of interaction and S112/T642 phosphorylation. Furthermore, expression of the K49R/K120R mutant of 14-3-3ζ inhibits the cytotoxicity of HDAC6 inhibition. These data demonstrate a novel role for HDAC6 in controlling 14-3-3ζ binding activity.
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Yuan, Zhigang. "Functional characterization of roles of histone deacetylases in the regulation of DNA damage response." [Tampa, Fla.] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0002175.

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Lu, Cheng-Tsung, and 呂承宗. "Identification of Lysine Acetylation Sites on Histone and non-Histone Proteins." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/81609115384199772080.

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碩士
元智大學
生物與醫學資訊碩士學位學程
99
Protein acetylation, which is catalyzed by acetyltransferases, is a type of post-translational modification and crucial to numerous essential biological processes, including transcriptional regulation, apoptosis, and cytokine signaling. As the experimental identification of protein acetylation sites is time consuming and laboratory intensive, several computational approaches have been developed for identifying the candidates of experimental validation. In this work, we attempt to investigate the substrate site specificities of acetylated lysine on histone and non-histone proteins. Maximal dependence decomposition (MDD) is employed to cluster a large set of acetylation data into subgroups containing significantly conserved motifs. In order to consider the biochemical property of amino acids when doing MDD, we categorize the twenty types of amino acids into five groups such as neutral, acid, basic, aromatic, and imino groups. Herein, support vector machine (SVM) was applied to learn the computational models with combinations of amino acid pair composition and BLOSUM62 matrix of proteins. According to the five-fold cross-validation, the proposed method could reach the predictive accuracies of 77.2% and 89.1% on histone and non-histone proteins, respectively. To help biologists investigating lysine acetylation on the uncharacterized proteins, a web-based system is constructed and is freely available at http://csb.cse.yzu.edu.tw/AceK/.
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Ming-ching and 李明璟. "The influence of hTERT promoter methylation and histone core acetylation status to telomerase activity in non-small cell lung cancers." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/86360695957134268925.

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碩士
中山醫學大學
醫學分子毒理學研究所
98
Telomeres consist of tandem oligonucleotide repeats (5’-TTAGGG-3’) that cap the ends of eukaryotic chromosomes to prevent further degradation and loss of human essential gene. Functional Telomeres are also essential for continued cell proliferation. By present research report, telomeres progressively shorten during each cell division without increasing the telomerase activity in most human cell. However, tumor cell generally have functional and short telomere lengths and revealed upregulated telomerase activity. Therefore, telomerase activity is hallmarks of tumorgenesis. On the other hand, DNA methylation and histone acetylation are important mechanism of epigenetic regulation without affecting the DNA sequence. Our in vitro and in vivo experiences tried to prove the relationship between telomerase activity and the methylation or histone acetylation of promoter region in human telomerase reverse transcriptase (hTERT). 5-Aza-2’-deoxycytidine (5-aza-dC) and Trichostatin A (TSA) are both added into the culture medium of two human non-small cell lung cancer cell line (H1299 and A549). Demethylating agent (5-aza-dC) activated the hTERT mRNA expression in H1299 and A549 cell lines. However, the TSA repressed the hTERT mRNA expression and telomerase activity in H1299 and A549 cell lines. TSA targets c-Myc and Ets-2 binding sites within the core region of the hTERT promoter to suppress the telomerase activity of H1299 and A549 cell lines. Genomic DNAs were extracted from non-small cell lung cancer samples and adjacent normal lung tissue of 62 patients. Hypermethylation status of the promoter of hTERT was found in low expressed hTERT of tumor sample and adjacent normal lung tissue (p=0.029 and p=0.01). Extremely shortened telomere length in tumor sample than adjacent normal lung tissue without correlated with the methylation status of promoter of hTERT and telomerase activity also noted in our experience. Base on these two experiences, the data show that the methylation and histone acetylation status in core promoter of hTERT could control the expression of hTERT and further telomerase activity. However, we can’t demonstrate that they could be potential biologic marker targets for clinical outcome of non-small cell lung cancer patients.
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Book chapters on the topic "Non-histone acetylation"

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Batta, Kiran, Chandrima Das, Shrikanth Gadad, Jayasha Shandilya, and Tapas K. Kundu. "Reversible Acetylation Of Non Histone Proteins." In Subcellular Biochemistry, 193–214. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/1-4020-5466-1_9.

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Lucchesi, John C. "Epigenetic chromatin changes and the transcription cycle." In Epigenetics, Nuclear Organization & Gene Function, 57–68. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780198831204.003.0005.

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In order to allow transcription to occur, the association of DNA with histone octamers and the compacted physical state of the chromatin fiber must be modified by the opportunistic binding of pioneer transcription factors to their cognate DNA binding sites. Once bound, pioneer factors recruit chromatin remodelers and histone-modifying enzymes for the purpose of repositioning nucleosomes and exposing regulatory regions (enhancers and gene promoters) to the components necessary for the initiation of transcription. Histone modifications, such as acetylation, methylation and ubiquitination, and the dynamic phosphorylation of specific amino acids on the major RNA polymerase II subunit activate transcription and attract the factors necessary to eliminate the pausing that normally occurs soon after initiation. Further histone modifications and the replacement of certain core histones by histone variants facilitate transcript elongation and termination. Two additional major epigenetic modifications that impact the process of transcription consist of the action of non-coding RNAs and DNA methylation.
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Subramanian, Subha, and James B. Potash. "Epigenetics in Psychiatry." In Psychiatric Genetics, 165–83. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190221973.003.0011.

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Epigenetic modifications such as DNA methylation (DNAm), histone acetylation and methylation, and those directed by small RNAs, are widely studied in psychiatry and may play a role in the etiology and pathophysiology of psychiatric disorders. This chapter provides a brief overview of the mechanisms regulating these epigenetic marks and the challenges in obtaining biologically meaningful epigenetic data, given the inaccessibility of the living human brain. Significant results to date from studies on the epigenetics of psychiatric disorders are presented, including the impact of stress on DNAm in psychiatric risk genes such as FKBP5, and the impact of drugs of abuse and of psychiatric medications on histone modifications. Future directions are discussed, including the study of newly discovered aspects of DNAm: 5-hydroxymethylcytosine and non-CpG methylation. Ongoing work aims to uncover neurobiological mechanisms of illness and to find epigenetic biomarkers in peripheral tissues that inform diagnosis, prognosis, and therapeutic response.
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Conference papers on the topic "Non-histone acetylation"

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Singh, Tripti, and Santosh K. Katiyar. "Abstract 4079: Proanthocyanidins reactivate silenced tumor suppressor genesp16INK4aandCip1/p21by reducing DNA methylation and increasing histone acetylation in human non-small cell lung cancer cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4079.

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