Evidence map›Paper›PMID 27117189›Full record

ArticleJournal of molecular biology2016

The Nucleosome Remodeling and Deacetylase Complex NuRD Is Built from Preformed Catalytically Active Sub-modules.

W Zhang, A Aubert, J M Gomez de Segura, M Karuppasamy, S Basu, A S Murthy, A Diamante, T A Drury, J Balmer, J Cramard and 13 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Human mutation · 2026
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  11. Article
  12. Article
  13. TgKDAC4: A Unique Deacetylase ofMicroorganisms · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Chromatin Remodeling in the Brain-aInternational journal of molecular sciences · 2021
    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

23 authors at 4 institutions in 3 countries.

W ZhangDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
A AubertEMBL Grenoble, 71 avenue des Martyrs, CS 90181, 38042 Grenoble Cedex 9, France.
J M Gomez de SeguraEMBL Grenoble, 71 avenue des Martyrs, CS 90181, 38042 Grenoble Cedex 9, France.
M KaruppasamyEMBL Grenoble, 71 avenue des Martyrs, CS 90181, 38042 Grenoble Cedex 9, France.
S BasuDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
A S MurthyDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
A DiamanteDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
T A DruryDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
J BalmerDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
J CramardWellcome Trust, Medical Research Council Stem Cell Institute, University of Cambridge, Gleeson Building, Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
A A WatsonDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
D LandoDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
S F LeeDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
M PalayretDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
S L KloetDepartment of Molecular Biology, Radboud Institute of Molecular Life Sciences, M850/3.79 Geert Grooteplein Zuid 30, 6525 GA Nijmegen, the Netherlands.
A H SmitsDepartment of Molecular Biology, Radboud Institute of Molecular Life Sciences, M850/3.79 Geert Grooteplein Zuid 30, 6525 GA Nijmegen, the Netherlands.
M J DeeryCambridge Centre for Proteomics, Cambridge System Biology Centre, Wellcome Trust Stem Cell building, University of Cambridge, Department of Biochemistry, Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
M VermeulenDepartment of Molecular Biology, Radboud Institute of Molecular Life Sciences, M850/3.79 Geert Grooteplein Zuid 30, 6525 GA Nijmegen, the Netherlands.
B HendrichWellcome Trust, Medical Research Council Stem Cell Institute, University of Cambridge, Gleeson Building, Tennis Court Road, Cambridge CB2 1QR, United Kingdom.
D KlenermanDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom.
C SchaffitzelEMBL Grenoble, 71 avenue des Martyrs, CS 90181, 38042 Grenoble Cedex 9, France; The School of Biochemistry, University of Bristol, University Walk, Clifton BS8 1TD, United Kingdom.
I BergerEMBL Grenoble, 71 avenue des Martyrs, CS 90181, 38042 Grenoble Cedex 9, France; The School of Biochemistry, University of Bristol, University Walk, Clifton BS8 1TD, United Kingdom.
E D LaueDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
University of Cambridge · GBWellcome/MRC Cambridge Stem Cell Institute · GBEuropean Molecular Biology Laboratory · FRRadboud University Nijmegen · NL

Funding

Medical Research Council MC_PC_12009Medical Research Council MR/M010082/1Wellcome Trust 098021
6 · The paper itself

Abstract

The nucleosome remodeling deacetylase (NuRD) complex is a highly conserved regulator of chromatin structure and transcription. Structural studies have shed light on this and other chromatin modifying machines, but much less is known about how they assemble and whether stable and functional sub-modules exist that retain enzymatic activity. Purification of the endogenous Drosophila NuRD complex shows that it consists of a stable core of subunits, while others, in particular the chromatin remodeler CHD4, associate transiently. To dissect the assembly and activity of NuRD, we systematically produced all possible combinations of different components using the MultiBac system, and determined their activity and biophysical properties. We carried out single-molecule imaging of CHD4 in live mouse embryonic stem cells, in the presence and absence of one of core components (MBD3), to show how the core deacetylase and chromatin-remodeling sub-modules associate in vivo. Our experiments suggest a pathway for the assembly of NuRD via preformed and active sub-modules. These retain enzymatic activity and are present in both the nucleus and the cytosol, an outcome with important implications for understanding NuRD function.

Indexed as

AnimalsCell NucleusChromatinChromatin Assembly and DisassemblyCytosolDrosophilaHistone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexMiceNucleosomesProtein SubunitsStem CellsChromatinHistone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexNucleosomesProtein Subunitschromatin-remodelingcomplex assemblyhistone modificationnucleosome remodeling and deacetylase NuRDtranscription

Identifiers

PMID27117189
PMCPMC4942838
OpenAlexW2337221221

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.