Structure of the Pds5-Scc1 Complex and Implications for Cohesin Function

• The structure of Pds5 reveals conserved surface features in the HEAT repeat domain
• Pds5 interacts with a discrete binding module on Scc1
• Enduring sister chromatid cohesion requires robust Pds5-Scc1 interactions
• A conserved surface spine in the Pds5 N terminus may contribute to cohesin release

SummarySister chromatid cohesion is a fundamental prerequisite to faithful genome segregation. Cohesion is precisely regulated by accessory factors that modulate the stability with which the cohesin complex embraces chromosomes. One of these factors, Pds5, engages cohesin through Scc1 and is both a facilitator of cohesion, and, conversely also mediates the release of cohesin from chromatin. We present here the crystal structure of a complex between budding yeast Pds5 and Scc1, thus elucidating the molecular basis of Pds5 function. Pds5 forms an elongated HEAT repeat that binds to Scc1 via a conserved surface patch. We demonstrate that the integrity of the Pds5-Scc1 interface is indispensable for the recruitment of Pds5 to cohesin, and that its abrogation results in loss of sister chromatid cohesion and cell viability.

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