Ontology highlight
ABSTRACT:
SUBMITTER: Hons MT
PROVIDER: S-EPMC4996973 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
Hons Michael T MT Huis In 't Veld Pim J PJ Kaesler Jan J Rombaut Pascaline P Schleiffer Alexander A Herzog Franz F Stark Holger H Peters Jan-Michael JM
Nature communications 20160823
The cohesin subunits Smc1, Smc3 and Scc1 form large tripartite rings which mediate sister chromatid cohesion and chromatin structure. These are thought to entrap DNA with the help of the associated proteins SA1/2 and Pds5A/B. Structural information is available for parts of cohesin, but analyses of entire cohesin complexes are limited by their flexibility. Here we generated a more rigid 'bonsai' cohesin by truncating the coiled coils of Smc1 and Smc3 and used single-particle electron microscopy, ...[more]