Evidence map›Paper›PMID 28332978›Full record

ArticleeLife2017

Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes.

Ramasubramanian Sundaramoorthy, Amanda L Hughes, Vijender Singh, Nicola Wiechens, Daniel P Ryan, Hassane El-Mkami, Maxim Petoukhov, Dmitri I Svergun, Barbara Treutlein, Salina Quack and 5 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
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  20. Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019
    Review
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

15 authors at 6 institutions in 3 countries.

Ramasubramanian SundaramoorthyCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Amanda L HughesCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Vijender SinghCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Nicola WiechensCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.
Daniel P RyanCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID 0000-0001-9842-2620
Hassane El-MkamiSchool of Physics and Astronomy, University of St Andrews, St Andrews, United Kingdom.
Maxim PetoukhovHamburg Outstation, European Molecular Biology Laboratory, Hamburg, Germany.
Dmitri I SvergunHamburg Outstation, European Molecular Biology Laboratory, Hamburg, Germany.
Barbara TreutleinInstitute for Biophysics, Faculty of Natural Sciences, Ulm University, Ulm, Germany.
Salina QuackInstitute for Biophysics, Faculty of Natural Sciences, Ulm University, Ulm, Germany.
Monika FischerInstitute for Biophysics, Faculty of Natural Sciences, Ulm University, Ulm, Germany.
Jens MichaelisInstitute for Biophysics, Faculty of Natural Sciences, Ulm University, Ulm, Germany.
Bettina BöttcherLehrstuhl für Biochemie, Rudolf-Virchow Zentrum, Universitat Würzburg, Würzburg, Germany.
David G NormanNucleic Acids Structure Research Group, University of Dundee, Dundee, United Kingdom.ORCID 0000-0002-7658-7720
Tom Owen-HughesCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee, United Kingdom.ORCID 0000-0002-0618-8185
University of Dundee · GBUniversität Ulm · DEEuropean Molecular Biology Laboratory · DEAustralian National University · AUUniversity of St Andrews · GBUniversity of Würzburg · DE

Funding

Biotechnology and Biological Sciences Research Council BB/E022286/1Wellcome TrustWellcome Trust 097945/B/11/ZWellcome Trust 099149/Z/12/Z
6 · The paper itself

Abstract

The yeast Chd1 protein acts to position nucleosomes across genomes. Here, we model the structure of the Chd1 protein in solution and when bound to nucleosomes. In the apo state, the DNA-binding domain contacts the edge of the nucleosome while in the presence of the non-hydrolyzable ATP analog, ADP-beryllium fluoride, we observe additional interactions between the ATPase domain and the adjacent DNA gyre 1.5 helical turns from the dyad axis of symmetry. Binding in this conformation involves unravelling the outer turn of nucleosomal DNA and requires substantial reorientation of the DNA-binding domain with respect to the ATPase domains. The orientation of the DNA-binding domain is mediated by sequences in the N-terminus and mutations to this part of the protein have positive and negative effects on Chd1 activity. These observations indicate that the unfavorable alignment of C-terminal DNA-binding region in solution contributes to an auto-inhibited state.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsMagnetic Resonance SpectroscopyModels, MolecularNucleosomesProtein BindingProtein ConformationSaccharomyces cerevisiae ProteinsCHD1 protein, S cerevisiaeDNA-Binding ProteinsNucleosomesSaccharomyces cerevisiae ProteinsATPasebiophysicsChd1chromatin remodelingchromosomesgenesnucleosomeS. cerevisiaestructural biology

Identifiers

PMID28332978
PMCPMC5391205
OpenAlexW2558067435

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.