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

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Publikace nespadá pod Ústav výpočetní techniky, ale pod Středoevropský technologický institut. Oficiální stránka publikace je na webu muni.cz.
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ZÁBRADY Kateřina ADAMUS Marek VONDROVÁ Lucie LIAO Chunyan SKOUPILOVÁ Hana NOVÁKOVÁ Markéta JURČIŠINOVÁ Lenka ALT Aaron OLIVER Antony W. LEHMANN Alan R. PALEČEK Jan

Rok publikování 2016
Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkv1021
Doi http://dx.doi.org/10.1093/nar/gkv1021
Obor Genetika a molekulární biologie
Klíčová slova SMC5-SMC6 COMPLEX; FISSION YEAST; SACCHAROMYCES-CEREVISIAE; CORE COMPONENT; REPAIR COMPLEX; ATP HYDROLYSIS; PROTEINS; COHESIN; REPLICATION; CHROMOSOMES
Popis 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.
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