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.

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.

In vivo single-molecule imaging demonstrates that Smc5/6 chromatin association depends on ATP hydrolysis and dsDNA binding, requires Nse6 and is modulated by Brc1 after DNA damage.

Genetic analyses in budding yeast coupled with biochemical assays have revealed an unexpected role for the Smc5/6 complex in cellular pathways responsible for the prevention of RNA formation in genomic DNA.

Chromosome condensation by condensin II is inhibited during interphase by direct interaction with MCPH1, which regulates opening of the condensin II interface between SMC2 and NCAPH2, in a similar fashion to how WAPL regulates Cohesin.

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.

SIMC1 and SLF1 bind exclusively to SLF2 to form two separate complexes that direct the human SMC5/6 complex to its antiviral defense or DNA lesion repair activities.

SCC3 not only functions as a member of cohesin complex but also participates in homologous pairing and synapsis during rice meiosis.

First evidence of cohesin folding occurring in vivo and during cohesion together with a detailed description of the structural aspects of cohesin's elbow folding through a series of novel structures.

Multi-dimensional global proteomics describes the SUMO-modified proteome during meiosis and reveals novel roles in regulating the key events of meiotic chromosome metabolism.