Part I: Basic Knowledge of Quantitative Analysis of Protein Acetylation Modification

After the protein is translated in the cell, it is processed through a very important step before being transported to the corresponding organelle and undergoing specific biological effects. The role of protein post-translational modification (PTM) is primarily to alter the activity, localization or function of the protein. Protein PTM also further increases the diversity and complexity of cellular pathway mechanisms and life activities.

Except for acetylation, common protein PTM includes phosphorylation, glycosylation, ubiquitination, and the like.

Protein Acetylation Modification

Protein acetylation modification, as the name suggests, refers to the grafting of acetylated groups on the original basis of the protein. In cells, the acetylation modification reaction is catalyzed by an acetyltransferase, and the acetyl group of acetyl-CoA is transferred and added to the protein lysine residue. In earlier studies, acetylation has been considered to be a post-translational modification unique to eukaryotic cells, and it has since been discovered that prokaryotic cells also have protein acetylation modifications in the middle years. Therefore, acetylation modification is a type of post-translational modification common to prokaryotic and eukaryotic organisms.
protein acetylation
Functions of Protein Acetylation Modification

At present, the research on the function of acetylation modification mainly focuses on the regulation of cell transcription and the regulation of metabolic pathways. Among plenty of acetylated proteins, more study has been made on the histones surrounding the DNA in the nucleus. Histones and DNA entangled to form nucleosomes. The methylation and acetylation of histones can regulate the tightness of DNA entanglement and regulate gene expression. Therefore, post-translational modification of histones is an important part in epigenetic research. In addition, study has also found that acetylation modifications are ubiquitous in human metabolic enzymes and is involved in the regulation of metabolic pathways as well as the activity of metabolic enzymes. Among them, a variety of metabolic enzymes are highly acetylated in metabolic organs such as the liver. Therefore, the study of new acetylation sites of proteins and acetylation modification omics can provide important guiding advice for revealing the causes of more diseases, and carry out new ideas for the development of new drugs related to diseases.

Histone Acetylation Regulation Process

In the nucleus, histone acetylation is in a dynamic equilibrium with histone deacetylation, and histone acetylation is jointly regulated by histone acetyltransferase (HAT) and histone deacetylase (HDAC). HAT transfers the acetyl group of acetyl-CoA to a specific lysine residue at the amino terminus of histones. The histones, after carrying a negatively charged acetylation group, repel each other from the same negatively charged DNA, so that the DNA entanglement becomes slack and can bind to the transcription factor to initiate expression of the gene. In contrast, HDAC deacetylates histones and promotes tight binding of negatively charged DNA. The nucleosomes are, therefore, more tightly packed, making DNA unable to bind to transcription factors, and gene transcription is inhibited accordingly.

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