Journal
NUCLEIC ACIDS RESEARCH
Volume 41, Issue 12, Pages 6149-6160Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt303
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Funding
- NSF [MCB-1022117, DMR-1206868]
- NIH-NCI [U54CA143869-01]
- Chicago Biomedical Consortium
- Searle Funds at The Chicago Community Trust
- American Heart Association
- International Human Frontier Science Program grant
- MEXT
- NIH [U54CA14869-01]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1022117] Funding Source: National Science Foundation
- Division Of Materials Research
- Direct For Mathematical & Physical Scien [1206868] Funding Source: National Science Foundation
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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 approximate to 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.
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