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

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...

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Bibliographic Details
Published in:Nucleic acids research 2016-02, Vol.44 (3), p.1064-1079
Main Authors: Zabrady, Katerina, Adamus, Marek, Vondrova, Lucie, Liao, Chunyan, Skoupilova, Hana, Novakova, Marketa, Jurcisinova, Lenka, Alt, Aaron, Oliver, Antony W, Lehmann, Alan R, Palecek, Jan J
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Cell Cycle Proteins - chemistry
Cell Cycle Proteins - metabolism
Chromatin - metabolism
DNA - metabolism
DNA Replication
Gene regulation, Chromatin and Epigenetics
Humans
Molecular Sequence Data
Nuclear Proteins - metabolism
Protein Binding
Recombination, Genetic
Schizosaccharomyces - genetics
Schizosaccharomyces - metabolism
Schizosaccharomyces pombe Proteins - metabolism
Sequence Homology, Amino Acid
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Summary: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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkv1021