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

Titelangaben

Viadiu, Hector ; Stemmann, Olaf ; Kirschner, Marc W. ; Walz, Thomas:
Domain structure of separase and its binding to securin as determined by EM.
In: Nature Structural & Molecular Biology. Bd. 12 (Juni 2005) . - S. 552-553.
ISSN 1545-9985
DOI: https://doi.org/10.1038/nsmb935

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Abstract

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 A 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.