Persuasive evidence has emerged that acetyltransferases appear to truly function to acetylate both histones and transcription factors in vivo to effect gene activation. In the cell, acetyltransferases have been identified as components of large, multifunctional and evolutionarily conserved macromolecular assemblies, whose components and structures suggest complex functions. In addition, the first atomic resolution structures of HATs have revealed conserved mechanisms of acetyl-CoA interaction among the superfamily of GNATs (Gcn5-related N-acetyltransferases). Finally, enzymatic acetyltransferase activities are themselves regulated by phosphorylation and interaction with other proteins.
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