Histone Acetyltransferase Pathway

1. Histone Acetyltransferase Pathway The most basic repeating unit in chromatin is the nucleosome core granule, which contains 147 bp of DNA wrapped around the central histone octamer. The nucleosome is a packing arrangement that compresses a piece of DNA about 2 m long into a nucleus with only 10 μm diameter, and this is also a dynamic structure containing many cellular processes. post-translationally modified by chromatin-modifying enzymes, and chromatin can also be mediated by chromatin-engineered enzymes. Post-translational modifications of histones include acetylation, phosphorylation, methylation, ubiquitination, and ADP-ribosylation, and often occur in unorganized histone tails. Histone acetylation is perhaps the earliest post-translational modification of research and is also closely related to gene activation. Histone acetylation occurs in a specific lysine residue in the N-terminal basic amino acid concentration region of the core histone, and the acetyl group of acetyl-CoA is transferred to NH+ of lysine to neutralize a positive charge. Histone acetylation levels are determined by both histone acetyltransferase and histone deacetylase. In the nucleus, histone acetylation and histone deacetylation processes are in dynamic equilibrium, precisely regulating gene transcription and expression. For example, nucleosomes can be Histone Acetyltransferase family At present, there are two types of molecules that have been found to contain histone acetyltransferase (HAT) activity. One is found in the nucleus, binds to histones on chromatin and acetylates it, and transcription of genes and corresponding organisms effect are related; one type exists in the cytoplasm, involved in chromatin replication, and has nothing to do with gene transcription. All acetylases can modify free-form histones, but only a portion of them can acetylate histones in nucleosome structures. In general, H3 and H4 are more susceptible to acetylation than H2A and H2B, but CBP and p300 can modify all four histones. In addition, each acetylase-modified lysine residue is different, indicating that the functions of different acetylases are different. At present, it is increasingly clear that acetylases are mostly present by forming larger complexes in the nucleus. Here, we focus on several of these acetyltransferases and their complexes, SAGA complex and NuA4 complex. Find more at: https://www.creative-diagnostics.com/histone-acetyltransferase-pathway.htm