Proteins are typically acetylated on
lysine residues and this reaction relies on
acetyl-coenzyme A as the acetyl group donor. In
histone acetylation and deacetylation, histone proteins are acetylated and deacetylated on lysine residues in the N-terminal tail as part of
gene regulation. Typically, these reactions are catalyzed by
enzymes with
histone acetyltransferase (HAT) or
histone deacetylase (HDAC) activity, although HATs and HDACs can modify the acetylation status of non-histone proteins as well. The regulation of transcription factors, effector proteins,
molecular chaperones, and cytoskeletal proteins by acetylation and deacetylation is a significant post-translational regulatory mechanism These regulatory mechanisms are analogous to phosphorylation and dephosphorylation by the action of
kinases and
phosphatases. Not only can the acetylation state of a protein modify its activity but there has been recent suggestion that this
post-translational modification may also crosstalk with
phosphorylation,
methylation,
ubiquitination, sumoylation, and others for dynamic control of cellular signaling. In the field of
epigenetics,
histone acetylation (and
deacetylation) have been shown to be important mechanisms in the regulation of gene transcription. Histones, however, are not the only proteins regulated by
posttranslational acetylation. ==Nomenclature==