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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: Volltext

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