Sister chromatid cohesion, which is essential for mitosis, is mediated by a multi-subunit
protein complex called cohesin whose Scc1, Smc1, and Smc3 subunits form a tripartite
ring structure. It has been proposed that cohesin holds sister DNAs together by trapping
them inside its ring. To test this, we used site-specific cross-linking to create chemical
connections at the three interfaces between the ring’s three constituent polypeptides,
thereby creating covalently closed cohesin rings. As predicted by the ring entrapment
model, this procedure produces dimeric DNA/cohesin structures that are resistant to
protein denaturation. We conclude that cohesin rings concatenate individual sister
minichromosome DNAs
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