Evidence map›Paper›PMID 27036862›Full record

ArticleNucleic acids research2016

The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.

Colin M Hammond, Ramasubramanian Sundaramoorthy, Mark Larance, Angus Lamond, Michael A Stevens, Hassane El-Mkami, David G Norman, Tom Owen-Hughes

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. 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 9% 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, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Structural Characterization ofMolecules (Basel, Switzerland) · 2019
    Article
  10. Article
  11. Molecular basis for chromatin assembly and modification by multiprotein complexes.Protein science : a publication of the Protein Society · 2019
    Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017
    Review
  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

8 authors at 2 institutions in 1 country.

Colin M HammondCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Ramasubramanian SundaramoorthyCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Mark LaranceCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Angus LamondCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK.
Michael A StevensNucleic Acids Structure Research Group, University of Dundee, Dundee DD1 5EH, UK.
Hassane El-MkamiSchool of Physics and Astronomy, University of St Andrews, St Andrews, KY16 9SS, UK.
David G NormanNucleic Acids Structure Research Group, University of Dundee, Dundee DD1 5EH, UK.
Tom Owen-HughesCentre for Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK t.a.owenhughes@dundee.ac.uk.
University of Dundee · GBUniversity of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E022286/1Medical Research Council G1100021Wellcome Trust 094090Wellcome Trust 097945Wellcome Trust 099149
6 · The paper itself

Abstract

Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice. We show Vps75 associates with histones in multiple oligomers. In the presence of equimolar H3-H4 and Vps75, the major species is a reconfigured Vps75 tetramer bound to a histone H3-H4 tetramer. However, in the presence of excess histones, a Vps75 dimer bound to a histone H3-H4 tetramer predominates. We show the Vps75-H3-H4 interaction is compatible with the histone chaperone Asf1 and deduce a structural model of the Vps75-Asf1-H3-H4 (VAH) co-chaperone complex using the Pulsed Electron-electron Double Resonance (PELDOR) technique and cross-linking MS/MS distance restraints. The model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer. This provides a structural explanation for many of the complexes detected biochemically and illustrates the ability of Vps75 to interact with dimeric or tetrameric H3-H4 using the same interaction surface.

Indexed as

AcetylationCell Cycle ProteinsCrystallography, X-RayHistone AcetyltransferasesHistone ChaperonesHistonesMolecular ChaperonesMultiprotein ComplexesProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASF1 protein, S cerevisiaeCell Cycle ProteinsHistone AcetyltransferasesHistone ChaperonesHistonesMolecular ChaperonesMultiprotein ComplexesSaccharomyces cerevisiae ProteinsVps75 protein, S cerevisiae

Identifiers

PMID27036862
PMCPMC5291247
OpenAlexW2320510676

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.