The acetylation of histones at specific sites close to DNA can regulate transcription.

A yeast genetic model for studying the function of sister histones in chromatin dynamics.

Mutation of Glycine 34 to Arginine within the N-terminal tail of histone H3 alters post-translational modifications on Lysine 36 and is associated with a delay in replication restart, defective homologous recombination and an increase in genomic instability.

Biochemical approaches reveal that an epigenetic histone deacetylase complex called CoREST is slow to deacetylate histone H3 lysine-14 in nucleosomes, and this inhibits demethylation of histone H3 lysine-4 by the CoREST complex.

CBP/p300 acetylation of histone H3 at promoters and enhancers stimulates transcriptional elongation through recruitment of the super-elongation complex and BRD4.

Nucleosomes at enhancers are unusually dynamic and change histone turnover rates during differentiation.

Histone H3T11 phosphorylation regulates chronological lifespan by linking nutritional stress-response signals to chromatin.

The CAF1 complex binds single histone H3-H4 dimers, and two such complexes associate with extended DNA elements to ensure the deposition of H3-H4 tetramers, the first step in the assembly of nucleosomes.

A widely studied chromatin modification associated with gene promoters is important for proper gene expression across organismal lifetime.

Chromatin structure is altered following DNA replication stress through the activity of protein kinase C signalling which leads to functionally coupled histone H3 phosphorylation and acetylation events.