Lysine acetylation: enzymes, bromodomains and links to different diseases

Lysine acetylation refers to transfer of the acetyl moiety from acetyl-CoA to the e-amino group of a lysine residue on a protein. This has recently emerged as a major covalent modifi cation and interplays with other modifi cations, such as phosphorylation, methylation, ubiquitination (addition of a small protein called ubiquitin) and SUMOylation [addition of a ubiquitin-like protein known as SUMO (small ubiquitin-related modifi er)], to form multisite modifi cation programmes for cellular regulation in diverse organisms. This modifi cation is post-translational (i.e. after synthesis of a protein) and reversible, with its level being dynamically balanced by two groups of enzymes known as lysine acetyltransferases and deacetylases. The acetyltransferases belong to three major families, whereas deacetylases have been divided into the classical and sirtuin