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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.

Structural predictions using AlphaFold suggest a mechanism by which Wapl mediates cohesin's dissociation from chromatin, a process whose downregulation is essential for VDJ recombination and diverse protocadherin gene expression.

A structure-based model of the chromosomal cohesin complex, accompanied by molecular-mechanistic simulations, explains cohesin's key role in topologically entrapping DNA, as well as its ability to alternatively extrude DNA loops.

In G1 cells, Scc2 loads and maintains cohesin on chromosomes by counteracting a Wapl-independent releasing activity, which is neutralized in S phase by CDK1.

The structural maintenance of chromosomes complex, SMC5/6, is crucial for brain development and function as it ensures proficient DNA replication in neural progenitor cells prior to chromosome segregation.

DNA loops can be formed by a mechanism in which the cohesin complex pulls DNA strands through its ring structure using biased Brownian motion.

A critical second step in DNA tethering by cohesin occurs after its stable binding to DNA, and this second step is modulated by the Smc3 ATPase active site in Saccharomyces cerevisiae.

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.

In Escherichia coli structural maintenance of chromosomes (SMC) complex, MukBEF, a dimeric MukF kleisin binds and activates MukB SMC ATPases through two independent interfaces provided by distinct MukF N- and C-terminal domains.

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.