HATs are a family of proteins that acetylate conserved lysine amino acids on histones and other proteins by transferring an acetyl group from acetyl-CoA to lysine to form ε-N-acetyl lysine. Lysine acetylation neutralizes the normally positive charge of histones, thus reducing their affinity towards (negatively charged) DNA which renders DNA more accessible to transcription factors and other processes. Moreover, histone acetylation generates binding sites for specific protein-protein interaction domains.
Histone acetylation is an important epigenetic mechanismperformed by acetyltransferases (HATs) that transfer an acetyl group to the ε-amino group of lysine residues on histone tails and bodies. Neutralization of the lysine positive charge weakens the binding between histones and DNA. This effect favors a relaxed chromatin structure permitting transcription,...