Evidence map›Paper›PMID 30833788›Full record

ArticleNature structural & molecular biology2019

A folded conformation of MukBEF and cohesin.

Frank Bürmann, Byung-Gil Lee, Thane Than, Ludwig Sinn, Francis J O'Reilly, Stanislau Yatskevich, Juri Rappsilber, Bin Hu, Kim Nasmyth, Jan Löwe

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

71 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. NIPBL and STAG1 enable loop extrusion by providing differential DNA-cohesin affinity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Recollections of a Helmstetter Disciple.Life (Basel, Switzerland) · 2023
    Review
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

10 authors at 5 institutions in 2 countries.

Frank BürmannMRC Laboratory of Molecular Biology, Cambridge, UK.ORCID http://orcid.org/0000-0002-9428-0933
Byung-Gil LeeMRC Laboratory of Molecular Biology, Cambridge, UK.
Thane ThanDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Ludwig SinnBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0003-4692-0681
Francis J O'ReillyBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
Stanislau YatskevichDepartment of Biochemistry, University of Oxford, Oxford, UK.
Juri RappsilberBioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-5999-1310
Bin HuDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.ORCID http://orcid.org/0000-0001-6316-2830
Kim NasmythDepartment of Biochemistry, University of Oxford, Oxford, UK.
Jan LöweMRC Laboratory of Molecular Biology, Cambridge, UK. jyl@mrc-lmb.cam.ac.ORCID http://orcid.org/0000-0002-5218-6615
MRC Laboratory of Molecular Biology · GBTechnische Universität Berlin · DEUniversity of Sheffield · GBUniversity of Oxford · GBWellcome Centre for Cell Biology · GB

Funding

Cancer Research UK 12386Medical Research Council G0401545Medical Research Council MC_U105184326Wellcome Trust 103139/Z/13/Z
6 · The paper itself

Abstract

Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through the entrapment and active translocation of DNA, but the underlying conformational changes are largely unclear. Using structural biology, mass spectrometry and cross-linking, we investigated the architecture of two evolutionarily distant SMC-kleisin complexes: MukBEF from Escherichia coli, and cohesin from Saccharomyces cerevisiae. We show that both contain a dynamic coiled-coil discontinuity, the elbow, near the middle of their arms that permits a folded conformation. Bending at the elbow brings into proximity the hinge dimerization domain and the head-kleisin module, situated at opposite ends of the arms. Our findings favour SMC activity models that include a large conformational change in the arms, such as a relative movement between DNA contact sites during DNA loading and translocation.

Indexed as

Protein FoldingCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsEscherichia coliEscherichia coli ProteinsProtein ConformationRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsEscherichia coli ProteinsMukB protein, E colimukE protein, E colimukF protein, E coliRepressor ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID30833788
PMCPMC6433275
OpenAlexW2900190809

What OpenQuestion holds

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LicenceTDM
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.