Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA

Investor logo
Investor logo
Investor logo

Warning

This publication doesn't include Faculty of Arts. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.
Authors

ZÁBRADY Kateřina ADAMUS Marek VONDROVÁ Lucie LIAO Chunyan SKOUPILOVÁ Hana NOVÁKOVÁ Markéta JURČIŠINOVÁ Lenka ALT Aaron OLIVER Antony W. LEHMANN Alan R. PALEČEK Jan

Year of publication 2016
Type Article in Periodical
Magazine / Source Nucleic Acids Research
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkv1021
Doi http://dx.doi.org/10.1093/nar/gkv1021
Field Genetics and molecular biology
Keywords SMC5-SMC6 COMPLEX; FISSION YEAST; SACCHAROMYCES-CEREVISIAE; CORE COMPONENT; REPAIR COMPLEX; ATP HYDROLYSIS; PROTEINS; COHESIN; REPLICATION; CHROMOSOMES
Description SMC5/6 is a highly conserved protein complex related to cohesin and condensin, which are the key components of higher-order chromatin structures. The SMC5/6 complex is essential for proliferation in yeast and is involved in replication fork stability and processing. However, the precise mechanism of action of SMC5/6 is not known. Here we present evidence that the NSE1/NSE3/NSE4 sub-complex of SMC5/6 binds to double-stranded DNA without any preference for DNA-replication/recombination intermediates. Mutations of key basic residues within the NSE1/NSE3/NSE4 DNA-binding surface reduce binding to DNA in vitro. Their introduction into the Schizosaccharomyces pombe genome results in cell death or hypersensitivity to DNA damaging agents. Chromatin immunoprecipitation analysis of the hypomorphic nse3 DNA-binding mutant shows a reduced association of fission yeast SMC5/6 with chromatin. Based on our results, we propose a model for loading of the SMC5/6 complex onto the chromatin.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.