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

Title data

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. Vol. 12 (June 2005) . - pp. 552-553.
ISSN 1545-9985
DOI: https://doi.org/10.1038/nsmb935

Official URL:

Abstract in another language

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.

Further data

Item Type:	Article in a journal
Refereed:	Yes
Institutions of the University:	Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics > Chair Genetics - Univ.-Prof. Dr. Olaf Stemmann Profile Fields > Advanced Fields > Molecular Biosciences Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Biology > Chair Genetics Profile Fields Profile Fields > Advanced Fields Research Institutions Research Institutions > Research Centres
Result of work at the UBT:	No
DDC Subjects:	500 Science > 570 Life sciences, biology
Date Deposited:	27 Mar 2015 07:59
Last Modified:	27 Mar 2015 07:59
URI:	https://eref.uni-bayreuth.de/id/eprint/8555