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Post-translational modification of proteins, such as acetylation, phosporylation, methylation, ubiquitination, sumoylation, and ADP-ribosylation are important governing processes to alter activity and stability of proteins. Eukaryotic DNA is packed in histone and histone like protein constructed nucleosomes, and hyperacetylation of histone lysine residues results in reduced interactions of positively charged histone and negatively charged DNA back-bone, providing excellent conditions to chromatin opening and gene transcription. On the other hand, deacetyaltion of histone residues results in compact chromatin and silencing of gene transcription. Therefore, acetylation/deacetylation level of histone residues is a well known modulator a gene transcription. Although, based on the result of histone deacetylase(HDAC) inhibitor studies, it appears that histone hyperacetyaltion is not a very accurate predictor of gene transcription. f-NH2 group of the amino acid side chain of lysine residues of histone proteins readily acetylated by histone acetyl transferases(HAT), but it turned out that this f-NH2 group of lysine is valid target in all kinds of proteins to acetylation. Unlike phosphorylation, which turns on proteins, acetylation has much wider, broader consequences on function and fate of proteins. In deed, acetylation, in general, alters the electrostatic state of lysine to neutral from positive charge and the addition of acetyl group leads to increase in the size of amino acid side chain. The acetylation affects enzymatic activity, DNA binding, protein localization, protein interaction, mRNA and protein stability, hence overall the whole fate and function of protein is influenced by acetylation.

The Effects of Aging and Exercise on Protein Acetylation/Deacetylation : Role of Sirtuins