Evidence map›Paper›PMID 15776017›Full record

ArticleEMBO reports2005

Nucleosome binding and histone methyltransferase activity of Drosophila PRC2.

Maxim Nekrasov, Brigitte Wild, Jürg Müller

Open access · greenAbstract readComparative Study
In one paragraph

Article in EMBO reports, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

84 citing papers in PubMed, 173 citations in OpenAlex.

  1. Article
  2. Article
  3. Epigenetics · 2023
    Review
  4. Article
  5. Critical Roles of Polycomb Repressive Complexes in Transcription and Cancer.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Article
  8. Review
  9. The Role of Polycomb Group Protein BMI1 in DNA Repair and Genomic Stability.International journal of molecular sciences · 2021
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. Article
  17. Precision Targeting with EZH2 and HDAC Inhibitors in Epigenetically Dysregulated Lymphomas.Clinical cancer research : an official journal of the American Association for Cancer Research · 2019
    Article
  18. Article
  19. Article
  20. Article

24 more citing papers are in PubMed but not listed here.

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

3 authors at 1 institution in 1 country.

Maxim NekrasovGene Expression Programme, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Brigitte Wild
Jürg Müller
European Molecular Biology Organization · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Drosophila Polycomb group protein E(z) is a histone methyltransferase (HMTase) that is essential for maintaining HOX gene silencing during development. E(z) exists in a multiprotein complex called Polycomb repressive complex 2 (PRC2) that also contains Su(z)12, Esc and Nurf55. Reconstituted recombinant PRC2 methylates nucleosomes in vitro, but recombinant E(z) on its own shows only poor HMTase activity on nucleosomes. Here, we investigate the function of the PRC2 subunits. We show that PRC2 binds to nucleosomes in vitro but that individual PRC2 subunits alone do not bind to nucleosomes. By analysing PRC2 subcomplexes, we show that Su(z)12-Nurf55 is the minimal nucleosome-binding module of PRC2 and that Esc contributes to high-affinity binding of PRC2 nucleosomes. We find that nucleosome binding of PRC2 is not sufficient for histone methylation and that only complexes that contain Esc protein show robust HMTase activity. These observations suggest that different subunits provide mechanistically distinct functions within the PRC2 HMTase: the nucleosome-binding subunits Su(z)12 and Nurf55 anchor the E(z) enzyme on chromatin substrates, whereas Esc is needed to boost enzymatic activity.

Indexed as

AnimalsBaculoviridaeChromatinChromosomal Proteins, Non-HistoneDrosophilaDrosophila ProteinsElectrophoretic Mobility Shift AssayGene SilencingHistone-Lysine N-MethyltransferaseHistone MethyltransferasesMethylationMolecular ChaperonesNuclear ProteinsNucleosomesPlasmidsPolycomb Repressive Complex 1Caf1-55 protein, DrosophilaChromatinChromosomal Proteins, Non-HistoneDrosophila Proteinsesc protein, DrosophilaE(z) protein, DrosophilaHistone-Lysine N-MethyltransferaseHistone MethyltransferasesMolecular ChaperonesNuclear ProteinsNucleosomesPc protein, DrosophilaPolycomb Repressive Complex 1Polycomb Repressive Complex 2Protein MethyltransferasesProtein SubunitsRepressor ProteinsRetinoblastoma-Binding Protein 4Su(z)12 protein, Drosophila

Identifiers

PMID15776017
PMCPMC1299286
OpenAlexW2155929185

What OpenQuestion holds

Textmetadata
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.