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reported that histone acetylation (H3K9ac and H3K27ac) post-translational modifications (PTMs) at certain gene promotors varied substantially between 0 and 50 h post-mortem . Histone Post-Translational Modifications The nucleosome, a fundamental unit of chromatin, consists of 146–147 bp of DNA that is wrapped around 1 histone octamer, which includes 2 molecules of each of the core histones H2A, H2B, H3, and H4 ( Kouzarides, 2007 ). Keywords:Histone, acetylation, phosphorylation, methylation, memory, plasticity, hippocampus. This process is dynamically regulated by specific modifying enzymes whose activities require metabolites that either serve as cosubstrates or act as activators/inhibitors. Representation showing post-translational modifications associated with histone particles. Title:Histone Post-translational Modifications to Target Memory-related Diseases VOLUME: 19 ISSUE: 28 Author(s):Barbara Monti Affiliation:Dept. Epigenetic heritage describes the ability of cells to transmit chromatin structural modifications during cell division and thereby maintaining differentiation status in eukaryotes. Histone acetylation adds an acetyl group on the lysine residue commonly found within the N-terminal tail protruding from the histone core of the nucleosome, and is important for chromosome structure and function in gene transcription and chromatin remodeling. Acetylation levels are regulated by a dynamic equilibrium between acetylation and deacetylation reactions. 51,52 Lysine crotonylation (Kcr) has been considered as the conserved histone post-translational modification in the kidney. Also depicted are the positions of PTMs located on the histone proteins H2A (and H2A.X), H2B, H3, and H4. Pharmacy and Bio- Technology, University of Bologna, Via Selmi 3, 40126, Bologna, Italy. Histone phosphorylation at serine and threonine residues can influence transcription, chromosome condensation, DNA repair and apoptosis. Barrachina et al. Histone crotonylation consists of the transfer of crotonyl groups to lysine residues of histones, that similar to acetylation, confers histones with negative charge. Histone acetylation is a post-translational modification that affects the nucleosome structure and therefore the ability of transcription factors to access the DNA and regulate gene expression. Histone post-translational modifications take place mainly on the N-terminal tails of histones. Chromosoma 112(2), 77–86. Abstract:Epigenetic mechanisms, i.e. Histone post-translational modifications regulate transcription and other DNA-templated functions. Therefore, metabolism can influence histone modification by changing local concentrations of key metabolites. Additionally, several histone modulators (histone methyl- and acetyltransferases) contain bromodomains, suggesting that acetylation of the histone tail lysines can precede subsequent modification of the “histone code” [7]. Nucleosomes are represented by red spheres wrapped by DNA (shown in gray). Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation Cuiling Li , 1, † Han-Pil Choi , 2, † Xiaoyue Wang , 1, † Fei Wu , 1 Xinjun Chen , 1 Xin Lü , 1 Ruirui Jing , 1 Hoon Ryu , 2 Xingyuan Wang , 3 Kazem M. Azadzoi , 2, * and Jing-Hua Yang 1, 2, * Post-Translational Modification of Human Histone by Wide Tolerance of Acetylation. Lysine methyltransferase and acetyltransferase enzyme activities, which generate histone PTMs, were measured in 12 human post-mortem brain samples. Zhang L, Eugeni EE, Parthun MR, Freitas MA (2003) Identification of novel histone post-translational modifications by peptide mass fingerprinting. 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