Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review)

Abstract

Cells primarily rely on proteins to perform the majority of their physiological functions, and the function of proteins is regulated by post-translational modifications (PTMs). The acetylation of proteins is a dynamic and highly specific PTM, which has an important influence on the functions of proteins, such as gene transcription and signal transduction. The acetylation of proteins is primarily dependent on lysine acetyltransferases and lysine deacetylases. In recent years, due to the widespread use of mass spectrometry and the emergence of new technologies, such as protein chips, studies on protein acetylation have been further developed. Compared with histone acetylation, acetylation of non-histone proteins has gradually become the focus of research due to its important regulatory mechanisms and wide range of applications. The discovery of specific protein acetylation sites using bioinformatic tools can greatly aid the understanding of the underlying mechanisms of protein acetylation involved in related physiological and pathological processes. Contents 1. Introduction 2. Discovery and concepts of protein acetylation and deacetylation 3. Diseases and protein acetylation and deacetylation 4. Protein acetylation and deacetylation in stem cells 5. Tools to predict acetylation sites 6. Conclusions and prospects

The Pleiotropic Function of Human Sirtuins as Modulators of Metabolic Pathways and Viral Infections

“…This modification is a reversible process and takes place largely in histones, which are proteins that bind to DNA and form the basic structure of chromatin, the nucleosome. The group of enzymes that are responsible for the acetylation of histones are the histone acetyltransferase (HATs) [ 34 ]. The DNA has a negative charge while histones are rich in positively charged amino acid residues (lysine, arginine and histidine).…”

Post-Translational Modifications That Drive Prostate Cancer Progression

“…In the opposite reaction, proteins are deacetylated by the actions of deacetylases. Protein acetylation is one of the main regulators of gene transcription since most histone acetyltransferases are located in the nucleus where they act as transcriptional co-activators [ 290 ]. Historically, acetylation was first discovered as a process affecting histones and if lysine is acetylated, histones will no longer be positively charged, so the binding of DNA to the histone is relaxed, which facilitates gene transcription.…”

Regulation of the Human Papillomavirus Lifecyle through Post-Translational Modifications of the Viral E2 Protein

“…KAT enzymes target a wide range of substrates from histones to viral proteins. Acetylation of proteins is a highly specific PTM that controls many cellular processes [ 50 ]. Studies have now been expanded to analyze acetylation on viral proteins and how these modifications can regulate the viral lifecycle.…”