Function
Histone acetyltransferase (HAT) catalyzes the acetylation of lysine residues on histone proteins. The acetyl group is transferred from acetyl-CoA to form ε-N-acetyl lysine. HAT contains a bromodomain – a ca. 110 amino acids domain which binds acetylated lysine. Histone acetylation is linked to transcription activation[1].
See also Histone acetyltransferase 1-2 Complex (HAT1/2).
- Histone acetyltransferase P300 acetylates all 4 core histones in nucleosomes and also non-histone targets.
Relevance
Inhibitors of HAT are potential drugs for inflammatory diseases[2].
Disease
Aberrant forms of HAT have been linked to congenital developmental disorders and various forms of cancer[3].
Structural highlights
in a of the protein[4]. Water molecules shown as red spheres.
3D Structures of histone acetyltransferase
Histone acetyltransferase 3D structures
