Histone acetylation

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Reproductive Biology and Endocrinology volume 18 , Article number: 84 Cite this article. Metrics details. Histone acetylation is a critical epigenetic modification that changes chromatin architecture and regulates gene expression by opening or closing the chromatin structure. It plays an essential role in cell cycle progression and differentiation. The human endometrium goes through cycles of regeneration, proliferation, differentiation, and degradation each month; each phase requiring strict epigenetic regulation for the proper functioning of the endometrium.

Histone acetylation

Thank you for visiting nature. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript. The amino termini of histones extend from the nucleosomal core and are modified by acetyltransferases and deacetylases during the cell cycle. These acetylation patterns may direct histone assembly and help regulate the unfolding and activity of genes. This is a preview of subscription content, access via your institution. Allfrey, V. Book Google Scholar. Hebbes, T. Adirect link between core histone acetylation and transcriptionally active chromatin. EMBO J.

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Histone acetylation is highly conserved across eukaryotes and has been linked to gene activation since its discovery nearly 60 years ago. Over the past decades, histone acetylation has been evidenced to play crucial roles in plant development and response to various environmental cues. In this review, we briefly describe the discovery of histone acetylation, the mechanism of histone acetylation regulating transcription in yeast and mammals, and summarize the research progress of plant histone acetylation. Furthermore, we also emphasize the effect of histone acetylation on seed development and its potential use in plant breeding. A comprehensive knowledge of histone acetylation might provide new and more flexible research perspectives to enhance crop yield and stress resistance.

Endothelial cell EC , consisting of the innermost cellular layer of all types of vessels, is not only a barrier composer but also performing multiple functions in physiological processes. Therefore, endothelial dysfunction contributes to the pathogenesis of many diseases. Growing pieces of evidence suggest that histone protein acetylation, an epigenetic mark, is altered in ECs under different conditions, and the acetylation status change at different lysine sites on histone protein plays a key role in endothelial dysfunction and involved in hyperglycemia, hypertension, inflammatory disease, cancer and so on. In this review, we highlight the importance of histone acetylation in regulating endothelial functions and discuss the roles of histone acetylation across the transcriptional unit of protein-coding genes in ECs under different disease-related pathophysiological processes. Since histone acetylation changes are conserved and reversible, the knowledge of histone acetylation in endothelial function regulation could provide insights to develop epigenetic interventions in preventing or treating endothelial dysfunction-related diseases.

Histone acetylation

In eukaryotic cells, DNA is tightly packed with the help of histone proteins into chromatin. Chromatin architecture can be modified by various post-translational modifications of histone proteins. For almost 60 years now, studies on histone lysine acetylation have unraveled the contribution of this acylation to an open chromatin state with increased DNA accessibility, permissive for gene expression. Additional complexity emerged from the discovery of other types of histone lysine acylations. The acyl group donors are products of cellular metabolism, and distinct histone acylations can link the metabolic state of a cell with chromatin architecture and contribute to cellular adaptation through changes in gene expression. Currently, various technical challenges limit our full understanding of the actual impact of most histone acylations on chromatin dynamics and of their biological relevance. In this review, we summarize the state of the art and provide an overview of approaches to overcome these challenges. We further discuss the concept of subnuclear metabolic niches that could regulate local CoA availability and thus couple cellular metabolisms with the epigenome. Keywords: acylation; chromatin; histones; metabolism; microdomains. Abstract In eukaryotic cells, DNA is tightly packed with the help of histone proteins into chromatin.

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Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification. Modifications of histones can not only cause secondary structural changes at their specific points, but can cause many structural changes in distant locations which inevitably affects function. Enhancers and their target promoters often share chromatin features, such as histone acetylation at specific lysine residues. Gene expression is affected by the positioning of individual nucleosomes relative to regulatory sequence elements, by the folding of the nucleosomal fiber into higher-order structures and by the compartmentalization of functional domains within the nucleus. Acetylation removes the positive charge on the histones, thereby decreasing the interaction of the N termini of histones with the negatively charged phosphate groups of DNA. Crystal structure of the nucleosome core particle at 2. Biochem Biophys Res Commun. This specific addition of single or multiple modifications on histone cores can be interpreted by transcription factors and complexes which leads to functional implications. Although some basic principles are emerging, our present understanding of HAT involvement in gene activation remains dominated by inherent complexities. Kadonaga, G. An ARID domain-containing protein within nuclear bodies is required for sperm cell formation in Arabidopsis thaliana.

Reproductive Biology and Endocrinology volume 18 , Article number: 84 Cite this article. Metrics details.

There are other proteins that have acetylating abilities but differ in structure to the previously mentioned families. It inhibits the response to DNA damage in melanoma cells [ 40 ]. Deregulation of histones modification are found to be responsible for deregulated gene expression and hence associated with neurological and psychological disorders, such as Schizophrenia [59] and Huntington disease. So far, about 30 HATs have been identified in humans. Secretory phase and implantation. Zhu JK. HDAC7 Regulates histone 3 lysine 27 acetylation and transcriptional activity at super-enhancer-associated genes in breast cancer stem cells. Condensation can be brought about by processes including deacetylation and methylation. The pathogenesis of atherosclerosis is very complex and this disease occurs through multiple processes. Cell Res. Bannister, A. These reactions occur post-translation and are reversible. Acetylation of histones H3 and H4 counteracts the tendency of nucleosomal fibers to fold into highly compact structures in vitro Garcia-Ramirez et al. Histone acetylation and deacetylation are essential parts of gene regulation. Trichostatin A are used somewhat sporadically, and both are currently applied in tissue culture Zhao et al.