Evidence map›Paper›PMID 28585918›Full record

ArticleeLife2017

Crosstalk within a functional INO80 complex dimer regulates nucleosome sliding.

Oliver Willhoft, Elizabeth A McCormack, Ricardo J Aramayo, Rohan Bythell-Douglas, Lorraine Ocloo, Xiaodong Zhang, Dale B Wigley

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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Mechanistic insights into INO80-type chromatin remodelers.Current opinion in structural biology · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Microscale Thermophoresis Analysis of Chromatin Interactions.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Molecular basis for chromatin assembly and modification by multiprotein complexes.Protein science : a publication of the Protein Society · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Cryo-EM structures of the human INO80 chromatin-remodeling complex.Nature structural & molecular biology · 2018
    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

7 authors at 1 institution in 1 country.

Oliver WillhoftDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.ORCID 0000-0003-2422-1839
Elizabeth A McCormackDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.
Ricardo J AramayoDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.
Rohan Bythell-DouglasDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.
Lorraine OclooDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.
Xiaodong ZhangDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.ORCID 0000-0001-9786-7038
Dale B WigleyDepartment of Medicine, Section of Structural Biology, Imperial College London, London, United Kingdom.ORCID 0000-0002-0786-6726
Imperial College London · GB

Funding

Cancer Research UK 12799Medical Research Council MR/N009258/1Wellcome Trust 095519/Z/11/ZWellcome Trust 098412/Z/12/Z
6 · The paper itself

Abstract

Several chromatin remodellers have the ability to space nucleosomes on DNA. For ISWI remodellers, this involves an interplay between H4 histone tails, the AutoN and NegC motifs of the motor domains that together regulate ATPase activity and sense the length of DNA flanking the nucleosome. By contrast, the INO80 complex also spaces nucleosomes but is not regulated by H4 tails and lacks the AutoN and NegC motifs. Instead nucleosome sliding requires cooperativity between two INO80 complexes that monitor DNA length simultaneously on either side of the nucleosome during sliding. The C-terminal domain of the human Ino80 subunit (Ino80CTD) binds cooperatively to DNA and dimerisation of these domains provides crosstalk between complexes. ATPase activity, rather than being regulated, instead gradually becomes uncoupled as nucleosome sliding reaches an end point and this is controlled by the Ino80CTD. A single active ATPase motor within the dimer is sufficient for sliding.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesDNADNA-Binding ProteinsDNA HelicasesHumansNucleosomesProtein BindingProtein MultimerizationAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesDNADNA-Binding ProteinsDNA HelicasesINO80 protein, humanNucleosomeschromatinchromosomescooperativitygeneshumanIno80nonenucleosomeremodelling

Identifiers

PMID28585918
PMCPMC5472440
OpenAlexW2622035844

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.