Histone acetylation and deacetylation
In histone acetylation and deacetylation, the histones 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. The source of the acetyl group in histone acetylation is Acetyl-Coenzyme A, and in histone deacetylation the acetyl group is transferred to Coenzyme A.
Acetylated histones and nucleosomes represent a type of epigenetic tag within chromatin. Acetylation brings in a negative charge and neutralizes the interaction of the N termini of histones with the phosphate groups of DNA. As a consequence, the condensed chromatin is transformed into a transiently relaxed structure which allows genes to be transcribed. Acetylated chromatin is thought to be more "relaxed" and is called euchromatin. Methylated chromatin is more condensed (tightly packed), and referred to as heterochromatin.
This charge neutralization model has been challenged by recent studies, according to which transcriptionally active genes are correlated with rapid turnover of histone acetylation. This requires that the HAts and HDAcs must act continuously on the affected histone tail. Methylation at a specific lysine residue (K4) is involved in targeting histone tails for continuous acetylation and deacetylation.
- Clayton A, Hazzalin C, Mahadevan L (2006). "Enhanced histone acetylation and transcription: a dynamic perspective". Mol Cell. 23 (3): 289–96. PMID 16885019.