Heterochromatin proteins like the SIR complex in budding yeast use different mechanisms for recruitment to nucleation sites and long-range spread to create a domain of transcriptional silencing.

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.

The histone chaperone FACT and the deubiquitinating enzyme Ubp10 act in concert to remove ubiquitin from histone H2B in nucleosomes, and likely coordinate nucleosome assembly during DNA replication and transcription.

In yeast, the secondary pathway for recruiting telomerase to chromosome ends requires a component of telomeric transcriptionally silent chromatin.

A protein called SIR-2.1 helps to protect worms from the effects of aging by regulating metabolic processes that would otherwise generate damaging reactive oxygen species.

A model of pathogen co-evolving with host population continuously acquiring immunity is used to identify evolutionary parameters allowing pathogen population to persist without going extinct or splitting into independent lineages.

Diverse histories of viral exposure, for example in individuals of different age, makes viral evolution less predictable with features of adaptive and neutral evolution.

Cell-cycle progression is crucial for heterochromatin formation in budding yeast because S phase promotes the removal of active chromatin marks.

Countrywide agent-based simulations with building-level resolution reveal the importance of demographic repartition and population density on epidemic dynamics of respiratory infections.

To control centriole duplication, centriolar satellite proteins assemble a microcephaly-associated protein complex at the centrosome and activate cyclin-dependent kinase 2.