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Nucleic Acids Res. 2013 Jul;41(12):6149-60. doi: 10.1093/nar/gkt303. Epub 2013 Apr 24.

The SMC1-SMC3 cohesin heterodimer structures DNA through supercoiling-dependent loop formation.

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1
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500, USA.

Abstract

Cohesin plays a critical role in sister chromatid cohesion, double-stranded DNA break repair and regulation of gene expression. However, the mechanism of how cohesin directly interacts with DNA remains unclear. We report single-molecule experiments analyzing the interaction of the budding yeast cohesin Structural Maintenance of Chromosome (SMC)1-SMC3 heterodimer with naked double-helix DNA. The cohesin heterodimer is able to compact DNA molecules against applied forces of 0.45 pN, via a series of extension steps of a well-defined size ≈130 nm. This reaction does not require ATP, but is dependent on DNA supercoiling: DNA with positive torsional stress is compacted more quickly than negatively supercoiled or nicked DNAs. Un-nicked torsionally relaxed DNA is a poor substrate for the compaction reaction. Experiments with mutant proteins indicate that the dimerization hinge region is crucial to the folding reaction. We conclude that the SMC1-SMC3 heterodimer is able to restructure the DNA double helix into a series of loops, with a preference for positive writhe.

PMID:
23620281
PMCID:
PMC3695518
DOI:
10.1093/nar/gkt303
[Indexed for MEDLINE]
Free PMC Article
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