Evidence map›Paper›PMID 28290497›Full record

ArticleScientific reports2017

Structural Basis of Eco1-Mediated Cohesin Acetylation.

William C H Chao, Benjamin O Wade, Céline Bouchoux, Andrew W Jones, Andrew G Purkiss, Stefania Federico, Nicola O'Reilly, Ambrosius P Snijders, Frank Uhlmann, Martin R Singleton

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

6 citing papers in PubMed, 16 citations in OpenAlex.

  1. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  2. Article
  3. It's all in the numbers: Cohesin stoichiometry.Frontiers in molecular biosciences · 2022
    Review
  4. Review
  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

William C H ChaoStructural Biology of Chromosome Segregation Laboratory, 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.
Céline BouchouxChromosome 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.
Andrew G PurkissStructural Biology Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Stefania FedericoPeptide Chemistry Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.
Nicola O'ReillyPeptide Chemistry Laboratory, 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.
The Francis Crick Institute · GB

Funding

Cancer Research UK 19343Cancer Research UK FC001155Cancer Research UK FC001198Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Sister-chromatid cohesion is established by Eco1-mediated acetylation on two conserved tandem lysines in the cohesin Smc3 subunit. However, the molecular basis of Eco1 substrate recognition and acetylation in cohesion is not fully understood. Here, we discover and rationalize the substrate specificity of Eco1 using mass spectrometry coupled with in-vitro acetylation assays and crystallography. Our structures of the X. laevis Eco2 (xEco2) bound to its primary and secondary Smc3 substrates demonstrate the plasticity of the substrate-binding site, which confers substrate specificity by concerted conformational changes of the central β hairpin and the C-terminal extension.

Indexed as

Chromosome SegregationAcetylationAcetyltransferasesAmino Acid SequenceAnimalsBinding SitesCell Cycle ProteinsChromosomal Proteins, Non-HistoneCrystallography, X-RayGene ExpressionModels, MolecularNuclear ProteinsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsAcetyltransferasesCell Cycle ProteinsChromosomal Proteins, Non-HistoneECO1 protein, S cerevisiaeEco2 protein, XenopusNuclear ProteinsPDS5 protein, S cerevisiaeRAD61 protein, S cerevisiaeRecombinant ProteinsSaccharomyces cerevisiae ProteinsSMC3 protein, S cerevisiaeStructural Maintenance of Chromosome Protein 1Xenopus Proteins

Identifiers

PMID28290497
PMCPMC5349539
OpenAlexW2618934776

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.