Histones form the protein core of nucleosomes, the DNA/protein complexes that are the subunits of eukaryotic chromatin. The histones' N-terminal "tails" are subject to a variety of post-translational modifications, including phosphorylation, methylation, ubiquitination, ADP-ribosylation and acetylation. These modifications have been proposed to constitute a 'histone code' with profound regulatory functions in gene transcription1. The best studied of these modifications, acetylation of the ε-aminos of specific histone lysine residues, are catalyzed by histone acetyltransferases (HATs). Histone deacetylases (HDACs) are responsible for hydrolytic removal of these acetyl groups2-4.
1. B.D. Strahl and C.D. Allis Nature 2000 403 41
2. M. Grunstein Nature1997 389 349
3. H. H. Ng and A. Bird Trends Biochem. Sci. 2000 25 121
4. W. L. Cheung et al. Curr. Opin. Cell Biol. 2000 12 326