Parrish, Lei Wang, in Comprehensive Natural Products II, 2010 5.18.3.4.3 AcetylationĪcetylation is a reversible modification on proteins that can also contribute to protein localization and function. 66 Acetylation is documented to exert other biological effects such as regulation of the translocation of nuclear transcription factors.Īngela R.
Acetylation of ERα and AR results in completely different outcomes: ERα transactivation is attenuated, but AR transcription activity is induced. 73 In addition, some nuclear hormone receptors can also be acetylated (e.g., ERα and AR). This CBP acetylase process can therefore provide negative regulation of ligand-dependent transcription. 66 CBP/p300 is also known to acetylate other coregulators, resulting in a disruption of the association between histone acetyltransferase (HAT) coactivator complexes and promoter-bound NR. Many NR coregulators, including CBP, possess intrinsic histone acetylation activity. For example, the hyperacetylation of histones 3 and 4 correlates with increased transcriptional activity. Murphy, in Comprehensive Medicinal Chemistry II, 2007 2.25.4.3.2 AcetylationĪcetylation of both histone proteins and coregulators constitutes an important regulatory event for the NR transcriptional apparatus. The method is most suitable to apply to pure proteins or relatively simple protein mixtures. The chemical treatment enables to determine the stoichiometry of acetylation at individual sites by measuring the abundance of the endogenously acetylated group (carrying a natulally abundant 12C 2-acetyl group) and the chemically introduced acetyl group (carrying an isotopically labeled 13C 2-acetyl group) in the subsequent mass spectrometry analysis. The method chemically acetylates all of the lysine residues in proteins that are not endogenously acetylated with an isotopically labeled acetyl ( 13C 2-acetyl) group. Here we describe a method that allows us to determine the site-specific stoichiometry of lysine acetylation. To understand better the site-specific roles of this modification, it is important to investigate what fraction of each modified site is actually acetylated (stoichiometry of acetylation) in vivo in different physiological conditions. Although numerous lysine acetylation sites have been identified in many proteins involved in a diverse range of cellular processes, little has been revealed about the roles of this modification at the level of individual sites. The modification is reversible and catalyzed by lysine acetyltransferases in one direction and lysine deacetylases in the other direction.
Miyagi, in Methods in Enzymology, 2017 AbstractĪcetylation of ɛ-amino group of lysine is one of the most common protein posttranslational modifications.