Evidence map›Paper›PMID 28059076›Full record

ArticleNature communications2017

Structure of the cohesin loader Scc2.

William C H Chao, Yasuto Murayama, Sofía Muñoz, Andrew W Jones, Benjamin O Wade, Andrew G Purkiss, Xiao-Wen Hu, Aaron Borg, Ambrosius P Snijders, Frank Uhlmann and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Cohesin ATPase activities regulate DNA binding and coiled-coil configuration.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. PDS5A and PDS5B in Cohesin Function and Human Disease.International journal of molecular sciences · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. De novoMedicina (Kaunas, Lithuania) · 2020
    Article
  18. Suppressor screening reveals common kleisin-hinge interaction in condensin and cohesin, but different modes of regulation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. A folded conformation of MukBEF and cohesin.Nature structural & molecular biology · 2019
    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

11 authors at 2 institutions in 2 countries.

William C H ChaoStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Yasuto MurayamaChromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Sofía MuñozChromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Andrew W JonesProtein Analysis and Proteomics Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Benjamin O WadeStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Andrew G PurkissStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Xiao-Wen HuStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Aaron BorgProtein Analysis and Proteomics Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Ambrosius P SnijdersProtein Analysis and Proteomics Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Frank UhlmannChromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Martin R SingletonStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.ORCID 0000-0001-5716-7715
The Francis Crick Institute · GBTokyo Institute of Technology · JP

Funding

Cancer Research UK 15656Cancer Research UK 19343
6 · The paper itself

Abstract

The functions of cohesin are central to genome integrity, chromosome organization and transcription regulation through its prevention of premature sister-chromatid separation and the formation of DNA loops. The loading of cohesin onto chromatin depends on the Scc2-Scc4 complex; however, little is known about how it stimulates the cohesion-loading activity. Here we determine the large 'hook' structure of Scc2 responsible for catalysing cohesin loading. We identify key Scc2 surfaces that are crucial for cohesin loading in vivo. With the aid of previously determined structures and homology modelling, we derive a pseudo-atomic structure of the full-length Scc2-Scc4 complex. Finally, using recombinantly purified Scc2-Scc4 and cohesin, we performed crosslinking mass spectrometry and interaction assays that suggest Scc2-Scc4 uses its modular structure to make multiple contacts with cohesin.

Indexed as

Cell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsConserved SequenceModels, MolecularProtein BindingProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsProtein SubunitsSaccharomyces cerevisiae ProteinsSCC2 protein, S cerevisiaeSCC4 protein, S cerevisiae

Identifiers

PMID28059076
PMCPMC5227109
OpenAlexW2571270016

What OpenQuestion holds

Textmetadata
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.