Rigorous biochemical and structural analyses reveal the precise topology of cohesin's association with DNA and suggest a mechanism for how DNA is transported inside the ring.

Characterization of PML subnuclear structures during human cytomegalovirus infection demonstrates that prolonged interferon and DNA damage signaling can induce giant PML nuclear bodies which sequentially entrap both nucleic acids and viral proteins as a cytoprotective mechanism.

The interface formed where Smc3p and Mcd1p bind each other regulates cohesin DNA binding and cohesion by a mechanism independently from its putative role as a DNA exit gate.

By identifying cohesin's DNA entry gate(s) and through understanding the corresponding topology between the two the mechanism behind cohesin's activity is slowly deciphered and will aid in understanding how the SMC family at large functions.

The Smc–ScpAB complex-a prokaryotic ancestor of cohesin, condensin and Smc5/6-loads onto the bacterial chromosome by employing ATP hydrolysis to capture DNA fibers within its tripartite ring.

The Cohesin subunit Scc3 contains a hook-shaped domain that binds to DNA substrate, thus revealing that Cohesin-chromatin transactions are driven not only by topological interactions, but also by direct protein-DNA contacts.

Sister chromatid cohesion is established during replication by two independent pathways operating in parallel, one converts chromosomal cohesin into cohesive structures while the other loads cohesin onto nascent DNAs.

Bacterial chromosome folding by DNA loop extrusion is here shown to rely on avoidance of SMC collisions by low SMC abundance, clustering of loading sites, efficient translocation, and rare unloading.

A structural and biochemical approach shows that CTP binding and hydrolysis regulate nucleation, spreading, and recycling of a chromosome segregation protein ParB.

Misalignment between light and temperature cycles leads to disrupted circadian behavior and a substantially altered rhythmic transcriptome.