Nucl. Acids Res.-2015-Zabrady-nar-gkv1021.pdf (7.51 MB)
Chromatin association of the SMC5/6 complex is dependent on binding of its NSE3 subunit to DNA
journal contribution
posted on 2023-06-08, 23:37 authored by Katerina Zabrady, Marek Adamus, Lucie Vondrova, Chunyan Liao, Hana Skoupilova, Marketa Novakova, Lenka Jurcisinova, Aaron Alt, Antony OliverAntony Oliver, Alan LehmannAlan Lehmann, Jan J PalecekSMC5/6 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.
History
Publication status
- Published
File Version
- Published version
Journal
Nucleic Acids ResearchISSN
1362-4962Publisher
Oxford JournalsExternal DOI
Issue
3Volume
44Page range
1064-1079Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2015-12-03First Open Access (FOA) Date
2015-12-03First Compliant Deposit (FCD) Date
2015-12-03Usage metrics
Categories
No categories selectedKeywords
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC