Evidence map›Paper›PMID 27257055›Full record

ArticleNucleic acids research2016

Synergy and antagonism in regulation of recombinant human INO80 chromatin remodeling complex.

Oliver Willhoft, Rohan Bythell-Douglas, Elizabeth A McCormack, Dale B Wigley

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 39 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Oliver WillhoftSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
Rohan Bythell-DouglasSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
Elizabeth A McCormackSection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK.
Dale B WigleySection of Structural Biology, Department of Medicine, Imperial College London, London SW7 2AZ, UK D.Wigley@imperial.ac.uk.
Imperial College London · GB

Funding

Cancer Research UK 12799Medical Research Council MR/N009258/1Wellcome Trust 095519
6 · The paper itself

Abstract

We have purified a minimal core human Ino80 complex from recombinant protein expressed in insect cells. The complex comprises one subunit each of an N-terminally truncated Ino80, actin, Arp4, Arp5, Arp8, Ies2 and Ies6, together with a single heterohexamer of the Tip49a and Tip49b proteins. This core complex has nucleosome sliding activity that is similar to that of endogenous human and yeast Ino80 complexes and is also inhibited by inositol hexaphosphate (IP6). We show that IP6 is a non-competitive inhibitor that acts by blocking the stimulatory effect of nucleosomes on the ATPase activity. The IP6 binding site is located within the C-terminal region of the Ino80 subunit. We have also prepared complexes lacking combinations of Ies2 and Arp5/Ies6 subunits that reveal regulation imposed by each of them individually and synergistically that couples ATP hydrolysis to nucleosome sliding. This coupling between Ies2 and Arp5/Ies6 can be overcome in a bypass mutation of the Arp5 subunit that is active in the absence of Ies2. These studies reveal several underlying mechanisms for regulation of ATPase activity involving a complex interplay between these protein subunits and IP6 that in turn controls nucleosome sliding.

Indexed as

Chromatin Assembly and DisassemblyAdenosine TriphosphatasesAnimalsATPases Associated with Diverse Cellular ActivitiesCell LineDNA-Binding ProteinsDNA HelicasesElectrophoresis, Polyacrylamide GelFluorescence Resonance Energy TransferHumansHydrolysisMultiprotein ComplexesMutationNucleosomesPhytic AcidProtein SubunitsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesDNA-Binding ProteinsDNA HelicasesINO80 protein, humanMultiprotein ComplexesNucleosomesPhytic AcidProtein SubunitsRecombinant Proteins

Identifiers

PMID27257055
PMCPMC5041457
OpenAlexW2415234617

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.