Literatura académica sobre el tema "Histone acylation"
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Artículos de revistas sobre el tema "Histone acylation"
Xiao, Yanhui, Wenjing Li, Hui Yang, Lulu Pan, Liwei Zhang, Lu Lu, Jiwei Chen et al. "HBO1 is a versatile histone acyltransferase critical for promoter histone acylations". Nucleic Acids Research 49, n.º 14 (14 de julio de 2021): 8037–59. http://dx.doi.org/10.1093/nar/gkab607.
Texto completoYan, Kezhi, Justine Rousseau, Keren Machol, Laura A. Cross, Katherine E. Agre, Cynthia Forster Gibson, Anne Goverde et al. "Deficient histone H3 propionylation by BRPF1-KAT6 complexes in neurodevelopmental disorders and cancer". Science Advances 6, n.º 4 (enero de 2020): eaax0021. http://dx.doi.org/10.1126/sciadv.aax0021.
Texto completoNeja, Sultan, Wan Mohaiza Dashwood, Roderick H. Dashwood y Praveen Rajendran. "Histone Acyl Code in Precision Oncology: Mechanistic Insights from Dietary and Metabolic Factors". Nutrients 16, n.º 3 (30 de enero de 2024): 396. http://dx.doi.org/10.3390/nu16030396.
Texto completoSoffers, Jelly H. M., Xuanying Li, Susan M. Abmayr y Jerry L. Workman. "Reading and Interpreting the Histone Acylation Code". Genomics, Proteomics & Bioinformatics 14, n.º 6 (diciembre de 2016): 329–32. http://dx.doi.org/10.1016/j.gpb.2016.12.001.
Texto completoKlein, Brianna J., Johayra Simithy, Xiaolu Wang, JaeWoo Ahn, Forest H. Andrews, Yi Zhang, Jacques Côté, Xiaobing Shi, Benjamin A. Garcia y Tatiana G. Kutateladze. "Recognition of Histone H3K14 Acylation by MORF". Structure 25, n.º 4 (abril de 2017): 650–54. http://dx.doi.org/10.1016/j.str.2017.02.003.
Texto completoKhan, Abid, Joseph B. Bridgers y Brian D. Strahl. "Expanding the Reader Landscape of Histone Acylation". Structure 25, n.º 4 (abril de 2017): 571–73. http://dx.doi.org/10.1016/j.str.2017.03.010.
Texto completoJo, Chanhee, Seokjae Park, Sungjoon Oh, Jinmi Choi, Eun-Kyoung Kim, Hong-Duk Youn y Eun-Jung Cho. "Histone acylation marks respond to metabolic perturbations and enable cellular adaptation". Experimental & Molecular Medicine 52, n.º 12 (diciembre de 2020): 2005–19. http://dx.doi.org/10.1038/s12276-020-00539-x.
Texto completoZheng, Lanlan, Chen Li, Xueping Ma, Hanlin Zhou, Yuan Liu, Ping Wang, Huilan Yang et al. "Functional interplay of histone lysine 2-hydroxyisobutyrylation and acetylation in Arabidopsis under dark-induced starvation". Nucleic Acids Research 49, n.º 13 (24 de junio de 2021): 7347–60. http://dx.doi.org/10.1093/nar/gkab536.
Texto completoZhao, Dan, Yuanyuan Li, Xiaozhe Xiong, Zhonglei Chen y Haitao Li. "YEATS Domain—A Histone Acylation Reader in Health and Disease". Journal of Molecular Biology 429, n.º 13 (junio de 2017): 1994–2002. http://dx.doi.org/10.1016/j.jmb.2017.03.010.
Texto completoSharma, Deepika, Swati Sharma y Preeti Chauhan. "Acetylation of Histone and Modification of Gene Expression via HDAC Inhibitors Affects the Obesity". Biomedical and Pharmacology Journal 14, n.º 1 (28 de marzo de 2021): 153–61. http://dx.doi.org/10.13005/bpj/2110.
Texto completoTesis sobre el tema "Histone acylation"
Zeaiter, Nour. "Les effets des changements métaboliques sur le métabolome des acyl-CoAs et l'acylation d'histone épigénétique". Electronic Thesis or Diss., Université Grenoble Alpes, 2024. http://www.theses.fr/2024GRALV013.
Texto completoAccumulating evidence suggests that metabolism can affect epigenetic post-translational modifications of histones, thus potentially linking nutrient availability or environmental conditions to gene expression and human physiopathology. However, there is still a lack of more detailed insight into this relationship. Here we study the role of short-chain (sc)-acyl-CoAs, generated in various metabolic pathways, as substrates for histone acylation. Analyzing acyl-CoAs is challenging due to their diverging (sub)cellular concentrations and physico-chemical properties. First, we applied a panel of analytical methods to establish reliable acyl-CoAs quantification, using liver ischemia as a model for inducing a metabolic shift. HPLC and MS emerged as the most suitable methods for unbiased analysis of sc-acyl-CoAs. Second, we employed HepG2 cells as a model system to explore the role of metabolic key enzymes and nutrient-induced metabolic shifts on acyl-CoA levels and histone acylation. Here and in the following, sc-acyl-CoAs were quantified by MS, and histone acylation was assessed at H4K5 and H4K8 by immunoblotting. Knockdown (KD) of enzymes involved in nucleocytosolic generation of acetyl-CoA (and potentially other acyl-CoAs) confirmed that ATP citrate lyase (ACLY) and acetyl-CoA synthetase short chain 2 (ACSS2) are the two major sources for nucleo-cytosolic acetyl-CoA. Moreover, we demonstrated that contrary to widespread believe, ACSS2 is not involved in biosynthesis of sc-acyl-CoAs other than acetyl-CoA. Further, KD of carnitine palmitoyltransferase 1A (CPT1A) did not yield clear evidence for its involvement in the export of mitochondrial sc-acyl-CoAs. Among the metabolic shifts studied, changes in acyl-CoA levels correlated with altered histone acylation only in some cases, namely octanoate fatty acid supplementation and glucose deprivation. These data suggest that substrate availability can be a determining factor for histone acylation, but that other factors can also be involved. Third, a transgenerational rat model for the effects of an environmental pollutant, endocrine disruptors (ED), revealed altered histone acylation patterns. Here we developed a HepG2 cell model that recapitulates direct ED effects on histone acylation, in particular an increased level of acetylation, together with increased acetyl-CoA levels. These data suggest HepG2 cells as a suitable model to study epigenetic ED effects mechanistically. In summary, this work established a basis to study epigenetic effects of nutrients and environmental pollutants in more detail
Goudarzi, Afsaneh. "Male genome programming guided by histone acylations". Thesis, Université Grenoble Alpes (ComUE), 2016. http://www.theses.fr/2016GREAV059/document.
Texto completoThe main focus of the investigations reported in this manuscript is the understanding of the regulatory events that are based on histone lysine modifications in post-meiotic male germ cells, where specific and chromosome-wide regulations of gene expression occur. In the first part of my work we designed a strategy to specifically investigate the role of the histone acetyl-transferases (HATs), Cbp and p300, in post-meiotic male germ cells.Accordingly, we generated double Cbp and p300 conditional knock-out mice resulting in a partial depletion of Cbp and p300 in post-meiotic cells. Although the mice were fertile and spermatogenesis seemed to take place normally, a transcriptomic analysis of early and late post-meiotic germ cells led to the identification of a specific subset of genes with an increased expression in late spermatogenic cells that is highly sensitive to the decreased amounts of Cbp and p300. In conclusion, these results have revealed an interesting new gene expression program specific to post-meiotic male germ cells that are specifically regulated by the considered HATs.Taking into account the occurrence of a variety of histone lysine acylations, we extended these investigations to a four-carbon histone lysine modification, butyrylation. Accordingly, we have undertaken a comprehensive comparative analysis of histone H4 acetylation and butyrylation on its K5 and K8 positions in differentiating male germ cells. Genome-wide mapping of H4K5ac, H4K5bu, H4K8ac and H4K8bu at two critical developmental stages, meiotic and post-meiotic haploid cells, shows an interchangeable use of acetylation and butyrylation in the Transcriptional Start Sites (TSSs) of the most highly expressed genes in both meiotic and haploid round spermatids. Interestingly, many of these promoters are also bound by the essential regulator of spermatogenic gene expression, the BET bromodomain-containing factor, Brdt. A detailed analysis of Brdt binding capacity of H4 tails bearing various combinations of K5 and K8 acetylation and butyrylation showed that H4K5 butyrylation severely interferes with Brdt-binding. Our results therefore indicate that not only Brdt is required for the activation of a meiotic and post-meiotic gene expression program, but also its turnover induced by H4K5 butyrylation is equally important. This work hence highlights how an interplay between two different acylations occurring on the same lysines can play an essential regulatory role by increasing the chromatin binding dynamics of a critical lysine acetyl-reader, Brdt.Finally, in a collaborative work with structural biologists we showed that while p300 is a robust acetylase, its activity gets weaker with increasing acyl chain length. These results suggest that in vivo, p300 would use a specific co-factor to ensure non-acetyl histone acylations.Overall, these investigations shed an important light on how the male genome programming is guided by histone acylations and revealed for the first time a molecular network that regulates histone acylations and mediates its functional impact
Crespo, Marion. "Analyse multi-omique des acylations de lysines d'histones pendant la gamétogénèse". Thesis, Université Grenoble Alpes (ComUE), 2019. http://www.theses.fr/2019GREAV066.
Texto completoThe innovative aspect of this project lies in the study of acylations at lysine 27 from histone H3 (H3K27), conventionally studied in a methylated or an acetylated form. We performed this work on meiotic and post-meiotic mouse germ cells. Spermiogenesis, which involves a specific expression program as well as a fine regulation of transcription, is a process that is particularly well suited to understanding the roles of new histone modifications. This work combines the use of four different omics approaches, namely proteomics, metabolomics, transcriptomics and ChIP- sequencing to decipher the regulation of acylations on H3K27.In the first part of this project, we explored the dynamics of acetylation and crotonylation on histone lysines during the processes of yeast sporulation and mouse spermatogenesis, which allowed us to highlight in particular crotonylated H3K27. Its accumulation on the histone variant H3.3 and its important stoichiometry compared to the acetylated form H3K27ac in mouse post-meiotic germ cells led us to study the genomic distribution of this mark by ChIP-seq analysis. The comparative analysis of H3K27ac and H3K27cr revealed a synergy between the presence of these acylations at both promoters and distal enhancers, suggesting a possible alternation of the two marks to regulate transcription. At the promoter level, we observed an increase of these modifications between the meiotic and post-meiotic stages upstream of the genes characteristic of spermiogenesis. In addition, the simultaneous presence of the two marks coincides with the co-localization of several transcriptional regulators specific for this process (SLY, SOX30) and of chromatin-binding proteins (BRD4, BORIS and CTCF), whereas a binding selectivity is observed when H3K27ac and H3K27cr are identified alone at promoters. Interestingly, we observe similar results at enhancers as well as super-enhancers, confirming that the regulation of transcription is modulated by the alternative presence of these two acylations.The second part of my thesis focused on the study of the possible propionylation and butyrylation of H3K27 during yeast sporulation and mouse spermatogenesis. However, this part proved to be full of surprises because the MS/MS analyses and the comparison with the corresponding synthetic peptides did not make it possible to validate a propionylation and a butyrylation on H3K27. It turned out that the modifications observed on H3K27 from mouse histones were strictly isobaric with these known modifications, but of a different nature, since they are more hydrophilic. Several hypotheses were tested in order to determine the structure of these modifications, but at the time of finalizing this manuscript, we have not found out what it is all about.My PhD work contributes further to the idea of a dynamics between acetylation and acylations on lysine residues at the origin of the differential binding of chromatin-binding proteins responsible for regulating transcription. It also highlighted an important role of H3K27crat enhancers which are not classically considered in studies aiming at understanding the roles of new acylations
Libros sobre el tema "Histone acylation"
Worden, Edward Chauncey. Technology of Cellulose Esters: A Theoretical and Practical Treatise on the Origin, History, Chemistry, Manufacture, Technical Application and Analysis of the Products of Acylation and Alkylation of Normal and Modified Cellulose. Creative Media Partners, LLC, 2022.
Buscar texto completoTechnology of Cellulose Esters: A Theoretical and Practical Treatise on the Origin, History, Chemistry, Manufacture, Technical Application and Analysis of the Products of Acylation and Alkylation of Normal and Modified Cellulose. Creative Media Partners, LLC, 2022.
Buscar texto completoCapítulos de libros sobre el tema "Histone acylation"
Balcerczyk, Aneta, Marta Biesiekierska, Varvara Vialichka y Luciano Pirola. "Histone acylation in the epigenomic regulation of insulin action and metabolic disease". En Nutritional Epigenomics, 101–17. Elsevier, 2019. http://dx.doi.org/10.1016/b978-0-12-816843-1.00007-2.
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