Acetylation

Acetylation of lysine is a reversible posttranslational modification (PTM), which neutralizes the positive charge of this amino acid, changing protein function in diverse ways. It has a key role in the regulation of gene expression through the modification of core histone tails by histone acetyltransferases (HATs) or histone deacetylases (HDACs). Some modified lysines specifically bind bromodomain-containing proteins, which are part of large complexes that modulate chromatin architecture. Lysine acetylation is also important for p53 functions and interactions and for microtubule stabilization.

Lysine acetylation had been studied mainly on specific proteins such as histones, p53, or tubulin. While it was always clear that lysine acetylation would not be restricted to just these protein classes, our knowledge of other acetylated proteins was far from complete. Using MS based proteomics, we identified and quantified more than 3,600 specific lysine acetylation sites on 1,750 proteins in three human cell lines which is the first quantitative and proteome-wide study of lysine acetylation. (Choudhary C. et al, Science, 2009)

For more information please see