The state transition acetyltransferase GNAT2 interacts with GNAT1 and GNAT3 in independent complexes

The acetylation of amino groups within proteins is one of the major posttranslational modifications (PTMs) in all organisms. N-terminal acetyltransferases (NATs) or lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from the donor substrate acetyl coenzyme A (Ac-CoA) to the targeted amino group, which is either the α-amino groups of N-termini or the ε-amino group of internal lysine residues. In contrast to N-terminal acetylation (NTA), the acetylation of lysine residues (KA) is reversible, whereby lysine deacetylases (KDACs) are responsible for the removal of acetyl groups from proteins. Furthermore, KA occurs posttranslationally, whereas NTA is described mainly as a cotranslational modification with the exception for N-terminally processed proteins, which are imported to chloroplasts and mitochondria