Evidence map›Paper›PMID 24688059›Full record

ArticleNucleic acids research2014

The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution.

Andrew Bowman, Colin M Hammond, Andrew Stirling, Richard Ward, Weifeng Shang, Hassane El-Mkami, David A Robinson, Dmitri I Svergun, David G Norman, Tom Owen-Hughes

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018
    Article
  5. Article
  6. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  7. Article
  8. Article
  9. Article
  10. Rotameric preferences of a protein spin label at edge-strand β-sheet sites.Protein science : a publication of the Protein Society · 2016
    Article
  11. Article
  12. Accurate Extraction of Nanometer Distances in Multimers by Pulse EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

10 authors at 3 institutions in 2 countries.

Andrew BowmanCentre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
Colin M HammondCentre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
Andrew StirlingCentre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK.
Richard WardNucleic Acids Structure Research Group, University of Dundee, Dundee, DD1 5EH, UK.
Weifeng ShangEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Hassane El-MkamiSchool of Physics and Astronomy, University of St Andrews, St Andrews FE2 4KM, UK.
David A RobinsonDivision of Biological Chemistry and Drug Discovery, University of Dundee, Dundee, DD1 5EH, UK.
Dmitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
David G NormanNucleic Acids Structure Research Group, University of Dundee, Dundee, DD1 5EH, UK.
Tom Owen-HughesCentre for Gene Regulation and Expression, University of Dundee, Dundee, DD1 5EH, UK t.a.owenhughes@dundee.ac.uk.
University of Dundee · GBEuropean Molecular Biology Laboratory · DEUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E022286/1Medical Research Council G1100021Wellcome Trust 094090Wellcome Trust 095062Wellcome Trust 097945
6 · The paper itself

Abstract

NAP-1 fold histone chaperones play an important role in escorting histones to and from sites of nucleosome assembly and disassembly. The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation. In this study, a combination of small angle X-ray scattering, multi angle light scattering and pulsed electron-electron double resonance approaches were used to show that both Vps75 and Nap1 adopt ring-shaped tetrameric conformations in solution. This suggests that the formation of homotetramers is a common feature of NAP-1 fold histone chaperones. The tetramerisation of NAP-1 fold histone chaperones may act to shield acidic surfaces in the absence of histone cargo thus providing a 'self-chaperoning' type mechanism.

Indexed as

Saccharomyces cerevisiaeModels, MolecularMolecular ChaperonesNucleosome Assembly Protein 1Protein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternarySaccharomyces cerevisiae ProteinsScattering, Small AngleSolutionsX-Ray DiffractionMolecular ChaperonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1Saccharomyces cerevisiae ProteinsSolutionsVps75 protein, S cerevisiae

Identifiers

PMID24688059
PMCPMC4027167
OpenAlexW2161864053

What OpenQuestion holds

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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.