Evidence map›Paper›PMID 25964121›Full record

ArticleNature communications2015

Structural analyses of the chromatin remodelling enzymes INO80-C and SWR-C.

Shinya Watanabe, Dongyan Tan, Mahadevan Lakshminarasimhan, Michael P Washburn, Eun-Jin Erica Hong, Thomas Walz, Craig L Peterson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

55 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
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  8. Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024
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  20. H2A Variants inPlant communications · 2020
    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

7 authors at 4 institutions in 1 country.

Shinya WatanabeProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Maasachusetts 01605, USA.
Dongyan Tan1] Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA [2] Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Mahadevan LakshminarasimhanStowers Institute for Medical Research, 1000 E 50th Street, Kansas, Missouri 64110, USA.
Michael P Washburn1] Stowers Institute for Medical Research, 1000 E 50th Street, Kansas, Missouri 64110, USA [2] Departments of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas, Kansas 66160, USA.ORCID 0000000175682585
Eun-Jin Erica HongDepartment of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Thomas Walz1] Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA [2] Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Craig L PetersonProgram in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Maasachusetts 01605, USA.
Howard Hughes Medical Institute · USStowers Institute for Medical Research · USUniversity of Massachusetts Chan Medical School · USHarvard University · US

Funding

YEAST CHROMATIN STRUCTURE/FUNCTIONR01GM054096 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 1997 to 2017
$5.7M
Analysis of the yeast SWI1, SWI2, and SWI3 proteinsR37GM049650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 2006 to 2015
$4.9M
YEAST SWI1, SWI2, AND SWI3 PROTEINSR01GM049650 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI PETERSON, CRAIG L · 1993 to 2016
$2.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM49650NIGMS NIH HHS R01 GM049650NIGMS NIH HHS R01 GM054096NIGMS NIH HHS R37 GM049650
6 · The paper itself

Abstract

INO80-C and SWR-C are conserved members of a subfamily of ATP-dependent chromatin remodelling enzymes that function in transcription and genome-maintenance pathways. A crucial role for these enzymes is to control chromosomal distribution of the H2A.Z histone variant. Here we use electron microscopy (EM) and two-dimensional class averaging to demonstrate that these remodelling enzymes have similar overall architectures. Each enzyme is characterized by a dynamic 'tail' domain and a compact 'head' that contains Rvb1/Rvb2 subunits organized as hexameric rings. EM class averages and mass spectrometry support the existence of single heterohexameric rings in both SWR-C and INO80-C. EM studies define the position of the Arp8/Arp4/Act1 module within INO80-C, and we find that this module enhances nucleosome-binding affinity but is largely dispensable for remodelling activities. In contrast, the Ies6/Arp5 module is essential for INO80-C remodelling, and furthermore this module controls conformational changes that may couple nucleosome binding to remodelling.

Indexed as

Adenosine TriphosphatasesChromatin Assembly and DisassemblyGene Expression Regulation, FungalImage Processing, Computer-AssistedMicroscopy, ElectronMolecular ImagingProtein ConformationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesINO80 complex, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID25964121
PMCPMC4431590
OpenAlexW211291674

What OpenQuestion holds

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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.