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

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.

Chemically sumoylated histone H4 shows negative biochemical crosstalk with gene-activating histone acetylation and methylation marks, and directly inhibits RNA polymerase II-mediated gene transcription.

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

A histone modification that alters the nucleosome structure occurs in mitosis and promotes chromosome packaging and the timely removal of condensin I and cohesion, to achieve chromosome segregation.

In a synthetic system, spreading of chromatin-mediated silencing to nearby genes depends on distance and can bypass genetic insulators, while reactivation after release of gene targeting is coordinated by insulators and promoters.

HDAC SUMOylation promotes the association of other chromatin remodeling factors with the nuclear Argonaute WAGO-9, which is required for de novo heterochromatin silencing.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

Silencing of gene regulatory elements by modifications of DNA-bound proteins promotes the progression of early mouse development.

The E3 ubiquitin ligase activity of polycomb repressive complex 1 is stimulated by RYBP to support a histone modification-dependent communication between polycomb repressive complexes in mice.