Evidence map›Paper›PMID 32755595›Full record

ArticleMolecular cell2020

A Structure-Based Mechanism for DNA Entry into the Cohesin Ring.

Torahiko L Higashi, Patrik Eickhoff, Joana S Sousa, Julia Locke, Andrea Nans, Helen R Flynn, Ambrosius P Snijders, George Papageorgiou, Nicola O'Reilly, Zhuo A Chen and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
9.8field-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

87 citing papers in PubMed, 175 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Bulk FRET Analysis of the Conformation of the Cohesin Ring.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  9. Structural basis for Lamassu-based antiviral immunity and its evolution from DNA repair machinery.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. 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
  13. Article
  14. Article
  15. Cohesin ring gates are specialized for meiotic cell division.Journal of molecular cell biology · 2025
    Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

27 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

14 authors at 3 institutions in 2 countries.

Torahiko L HigashiChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Patrik EickhoffMacromolecular Machines Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Joana S SousaMacromolecular Machines Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Julia LockeMacromolecular Machines Laboratory, The Francis Crick Institute, London NW1 1AT, UK.
Andrea NansStructural Biology STP, The Francis Crick Institute, London NW1 1AT, UK.
Helen R FlynnProteomics STP, The Francis Crick Institute, London NW1 1AT, UK.
Ambrosius P SnijdersProteomics STP, The Francis Crick Institute, London NW1 1AT, UK.
George PapageorgiouPeptide Chemistry STP, The Francis Crick Institute, London NW1 1AT, UK.
Nicola O'ReillyPeptide Chemistry STP, The Francis Crick Institute, London NW1 1AT, UK.
Zhuo A ChenBioanalytics Unit, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany.
Francis J O'ReillyBioanalytics Unit, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany.
Juri RappsilberBioanalytics Unit, Institute of Biotechnology, Technische Universität Berlin, 13355 Berlin, Germany; Wellcome Centre for Cell Biology, University of Edinburgh, Edinburgh EH9 3BF, UK.
Alessandro CostaMacromolecular Machines Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: alessandro.costa@crick.ac.uk.
Frank UhlmannChromosome Segregation Laboratory, The Francis Crick Institute, London NW1 1AT, UK. Electronic address: frank.uhlmann@crick.ac.uk.
The Francis Crick Institute · GBTechnische Universität Berlin · DEWellcome Centre for Cell Biology · GB

Funding

Cancer Research UK FC001198Medical Research Council FC001065Medical Research Council FC001198Medical Research Council MC_PC_17136Wellcome Trust FC001065Wellcome Trust FC001198
6 · The paper itself

Abstract

Despite key roles in sister chromatid cohesion and chromosome organization, the mechanism by which cohesin rings are loaded onto DNA is still unknown. Here we combine biochemical approaches and cryoelectron microscopy (cryo-EM) to visualize a cohesin loading intermediate in which DNA is locked between two gates that lead into the cohesin ring. Building on this structural framework, we design experiments to establish the order of events during cohesin loading. In an initial step, DNA traverses an N-terminal kleisin gate that is first opened upon ATP binding and then closed as the cohesin loader locks the DNA against the ATPase gate. ATP hydrolysis will lead to ATPase gate opening to complete DNA entry. Whether DNA loading is successful or results in loop extrusion might be dictated by a conserved kleisin N-terminal tail that guides the DNA through the kleisin gate. Our results establish the molecular basis for cohesin loading onto DNA.

Indexed as

Adenosine TriphosphatasesCell Cycle ProteinsChromatidsChromosomal Proteins, Non-HistoneChromosome SegregationCohesinsCryoelectron MicroscopyDNANucleic Acid ConformationProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSister Chromatid ExchangeAdenosine TriphosphatasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsDNASaccharomyces cerevisiae ProteinsABC-ATPasechromosome segregationcohesincryo-electron microscopyDNA loop extrusionDNA-protein crosslink mass spectrometryMis4/Scc2/NIPBLsister chromatid cohesionSMC complexesS. pombe

Identifiers

PMID32755595
PMCPMC7507959
OpenAlexW3046933533

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.