Evidence map›Paper›PMID 23620281›Full record

ArticleNucleic acids research2013

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

Mingxuan Sun, Tatsuya Nishino, John F Marko

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

42 citing papers in PubMed, 70 citations in OpenAlex.

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  4. Review
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  10. Review
  11. DNA sliding and loop formation byBiochemistry and biophysics reports · 2022
    Article
  12. Reeling it in: how DNA topology drives loop extrusion by condensin.Nature structural & molecular biology · 2022
    Article
  13. Article
  14. TF-COMB - Discovering grammar of transcription factor binding sites.Computational and structural biotechnology journal · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Chromosome disentanglement driven via optimal compaction of loop-extruded brush structures.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Mingxuan SunDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500, USA.
Tatsuya Nishino
John F Marko
National Institute of Genetics · JPNorthwestern University · US

Funding

TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
NCI NIH HHS U54 CA143869NCI NIH HHS U54CA143869-01
6 · The paper itself

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.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneDimerizationDNA, SuperhelicalFungal ProteinsProtein Structure, TertiarySequence DeletionStructural Maintenance of Chromosome Protein 1Cell Cycle ProteinsChromosomal Proteins, Non-HistoneDNA, SuperhelicalFungal ProteinsStructural Maintenance of Chromosome Protein 1

Identifiers

PMID23620281
PMCPMC3695518
OpenAlexW2168055931

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.