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Structural basis of cohesin cleavage by separase

Author

Listed:
  • Zhonghui Lin

    (Howard Hughes Medical Institute, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Xuelian Luo

    (University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

  • Hongtao Yu

    (Howard Hughes Medical Institute, University of Texas Southwestern Medical Center
    University of Texas Southwestern Medical Center)

Abstract

The crystal structures of the protease domain of separase are reported, showing how separase recognizes cohesin, and how phosphorylation of the cleavage site enhances separase activity.

Suggested Citation

  • Zhonghui Lin & Xuelian Luo & Hongtao Yu, 2016. "Structural basis of cohesin cleavage by separase," Nature, Nature, vol. 532(7597), pages 131-134, April.
    • Handle: RePEc:nat:nature:v:532:y:2016:i:7597:d:10.1038_nature17402
    DOI: 10.1038/nature17402
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    Cited by:

    1. Christopher Thomas & Benjamin Wetherall & Mark D. Levasseur & Rebecca J. Harris & Scott T. Kerridge & Jonathan M. G. Higgins & Owen R. Davies & Suzanne Madgwick, 2021. "A prometaphase mechanism of securin destruction is essential for meiotic progression in mouse oocytes," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    2. Ning Cui & Jun-Tao Zhang & Zhuolin Li & Xiao-Yu Liu & Chongyuan Wang & Hongda Huang & Ning Jia, 2022. "Structural basis for the non-self RNA-activated protease activity of the type III-E CRISPR nuclease-protease Craspase," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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