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Resources » Paper

Luo S et al. (2018) Curr Opin Struct Biol "Structural biology of the separase-securin complex with crucial roles in chromosome segregation."

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  • Comments on Luo S et al. (2018) Curr Opin Struct Biol "Structural biology of the separase-securin complex with crucial roles in chromosome segregation." (0)

  • Overview

    PMID:
    29452922
    DOI:
    10.1016/j.sbi.2018.01.012
    Status:
    Publication type:
    Review
    WormBase ID:
    WBPaper00053714

    Luo S, & Tong L (2018). Structural biology of the separase-securin complex with crucial roles in chromosome segregation. Curr Opin Struct Biol, 49, 114-122. doi:10.1016/j.sbi.2018.01.012

    The cysteine protease separase opens the cohesin ring by cleaving its kleisin subunit and is a pivotal cell cycle factor for the transition from metaphase to anaphase. It is inhibited by forming a complex with the chaperone securin, and in vertebrates, also by the Cdk1-cyclin B1 complex. Separase is activated upon the destruction of securin or cyclin B1 by the proteasome, after ubiquitination by the anaphase-promoting complex/cyclosome (APC/C). Here we review recent structures of the active protease segment of Chaetomium thermophilum separase in complex with a substrate-mimic inhibitor and full-length Saccharomyces cerevisiae and Caenorhabditis elegans separase in complex with securin. These structures define the mechanism for substrate recognition and catalysis by separase, and show that securin has extensive contacts with separase, consistent with its chaperone function. They confirm that securin inhibits separase by binding as a pseudo substrate.


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