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Brief Communication
Nature Structural & Molecular Biology  12, 552 - 553 (2005)
Published online: 8 May 2005; | doi:10.1038/nsmb935

Domain structure of separase and its binding to securin as determined by EM

Hector Viadiu1, Olaf Stemmann3, Marc W Kirschner2 & Thomas Walz1

1  Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.

2  Department of Systems Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.

3  Max-Planck Institute of Biochemistry, Department of Molecular Cell Biology, Am Klopferspitz 18, 82152 Martinsried, Germany.

Correspondence should be addressed to Thomas Walz twalz@hms.harvard.edu
After the degradation of its inhibitor securin, separase initiates chromosome segregation during the metaphase-to-anaphase transition by cleaving cohesin. Here we present a density map at a resolution of 25 Å of negatively stained separase−securin complex. Based on labeling data and sequence analysis, we propose a model for the structure of separase, consisting of 26 ARM repeats, an unstructured region of 280 residues and two caspase-like domains, with securin binding to the ARM repeats.


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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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