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Abstract
In eukaryotic cells, replicated DNA strands remain physically connected until their
segregation to opposite poles of the cell during anaphase. This "sister chromatid
cohesion" is essential for the alignment of chromosomes on the mitotic spindle during
metaphase. Cohesion depends on the multisubunit cohesin complex, which possibly forms
the physical bridges connecting sisters. Proteolytic cleavage of cohesin's Sccl subunit
at the metaphase to anaphase transition is essential for sister chromatid separation
and depends on a conserved protein called separin. We show here that separin is a
cysteine protease related to caspases that alone can cleave Sccl in vitro. Cleavage
of Sccl in metaphase arrested cells is sufficient to trigger the separation of sister
chromatids and their segregation to opposite cell poles.