Separase–securin complex: a cunning way to control chromosome segregation

Separases are crucial cell cycle proteases that control the metaphase-to-anaphase transition by cleaving chromosomal cohesin rings. Two new high-resolution structures of separase bound by its inhibitory chaperone securin illustrate intriguing regulatory mechanisms.

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Figure 1: Ribbon representations of the budding yeast S. cerevisiae separase–securin complex (top) and the nematode worm C. elegans complex (bottom).
Figure 2: Active site diagrams of separase in active and inactive configurations.

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Correspondence to Martin R Singleton or Frank Uhlmann.

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Singleton, M., Uhlmann, F. Separase–securin complex: a cunning way to control chromosome segregation. Nat Struct Mol Biol 24, 337–339 (2017). https://doi.org/10.1038/nsmb.3393

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