A versatile acetylation-methylation switch at lysine 31 on the lateral surface of histone H4 contributes to chromatin structure in apicomplexan parasites.

A previously unappreciated histone methylation pathway helps limit DNA double-strand break formation and recombination in heterochromatin during meiosis.

The BPTF PHD finger is inhibited from binding the methylated H3 tails in the context of the nucleosome due to their robust interaction with the nucleosomal DNA, which can be modulated by additional histone PTMs.

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

The structure of the COMPASS methyltransferase bound to an H2B-ubiquitinated nucleosome provides insights into mechanisms of trans-histone cross-talk and the dynamic role of H2B ubiquitination in stimulating histone methylation.

The physicochemical interactions among wild-type nucleosomes hold substantial significance and play a role in chromatin folding under physiological salt concentrations.

A novel system for expression of asymmetric nucleosomes in vivo enables mechanistic studies on histone modification readouts in the cell.

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.

A novel phenotypic screening platform based on immunofluorescent imaging of histone modifications enables accurate identification of cell fates and environmental perturbations.

In humans, specific sequence features can predict whether meiotic recombination occurs at sites bound by the protein PRDM9, whose DNA-binding zinc-finger domain can unexpectedly bind to gene promoters and to other copies of PRDM9.