Antigen Ki-67, which is widely used as a cell proliferation marker, controls heterochromatin organisation and gene expression.

Cooperative association of a histone-binding complex with pairs of appropriately modified nucleosomes, which form fundamental units of binding, mediates selective heterochromatin assembly and spreading.

Epigenetic restriction of herpes simplex virus occurs in a biphasic manner, in which ATRX maintains viral heterochromatin after an initial phase of chromatin deposition.

Origin recognition complex-associated (ORCA) is crucial for the stability of the Histone H3 lysine 9 methyltransferase megacomplex, which is essential for heterochromatin organization.

An RNA-mediated mechanism that stabilizes association of the Suv39h enzymes at mouse heterochromatin is defined.

Redundant pathways prevent heterochromatin spreading and ectopic heterochromatin assembly; and plasticity of heterochromatin assembly allows cells to adapt to heterochromatin stress.

SUV39H1 histone methyltransferase directly binds chromosome associated RNA to promote constitutive heterochromatin formation.

Identification of novel components and regulators of heterochromatin reveals a spatially complex and dynamic organization.

Suv39h1 chromodomain possesses nucleic acid-binding activity and this activity is coupled with its H3K9 methylation recognition in assembling heterochromatin.

Heterochromatin spreading in fission yeast predominantly produces intergenerationally unstable outcomes, requiring an accessory element that represses histone turnover.