Evidence map›Paper›PMID 24019522›Full record

ArticleThe Journal of biological chemistry2013

Histone H2A ubiquitination inhibits the enzymatic activity of H3 lysine 36 methyltransferases.

Gang Yuan, Ben Ma, Wen Yuan, Zhuqiang Zhang, Ping Chen, Xiaojun Ding, Li Feng, Xiaohua Shen, She Chen, Guohong Li and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  5. Review
  6. Review
  7. Review
  8. Article
  9. DNA Damage Response Regulation by Histone Ubiquitination.International journal of molecular sciences · 2022
    Review
  10. Know when to fold 'em: Polycomb complexes in oncogenic 3D genome regulation.Frontiers in cell and developmental biology · 2022
    Review
  11. Review
  12. Review
  13. Article
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  16. Article
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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

11 authors at 3 institutions in 1 country.

Gang YuanFrom the College of Life Sciences, Beijing Normal University, Beijing, 100875.
Ben Ma
Wen Yuan
Zhuqiang Zhang
Ping Chen
Xiaojun Ding
Li Feng
Xiaohua Shen
She Chen
Guohong Li
Bing Zhu
National Institute of Biological Sciences, Beijing · CNChinese Academy of Sciences · CNTsinghua University · CN

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Histone H3 lysine 27 (H3K27) methylation and H2A monoubiquitination (ubH2A) are two closely related histone modifications that regulate Polycomb silencing. Previous studies reported that H3K27 trimethylation (H3K27me3) rarely coexists with H3K36 di- or tri-methylation (H3K36me2/3) on the same histone H3 tails, which is partially controlled by the direct inhibition of the enzymatic activity of H3K27-specific methyltransferase PRC2. By contrast, H3K27 methylation does not affect the catalytic activity of H3K36-specific methyltransferases, suggesting other Polycomb mechanism(s) may negatively regulate the H3K36-specific methyltransferase(s). In this study, we established a simple protocol to purify milligram quantities of ubH2A from mammalian cells, which were used to reconstitute nucleosome substrates with fully ubiquitinated H2A. A number of histone methyltransferases were then tested on these nucleosome substrates. Notably, all of the H3K36-specific methyltransferases, including ASH1L, HYPB, NSD1, and NSD2 were inhibited by ubH2A, whereas the other histone methyltransferases, including PRC2, G9a, and Pr-Set7 were not affected by ubH2A. Together with previous reports, these findings collectively explain the mutual repulsion of H3K36me2/3 and Polycomb modifications.

Indexed as

AnimalsCarrier ProteinsCell LineDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansIntracellular Signaling Peptides and ProteinsMethylationMiceNuclear ProteinsTranscription FactorsUbiquitinationASH1L protein, humanCarrier ProteinsDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesIntracellular Signaling Peptides and ProteinsNSD1 protein, humanNsd1 protein, mouseNuclear ProteinsTranscription FactorsChromatinChromatin Histone ModificationHistone MethylationTranscription RegulationUbiquitination

Identifiers

PMID24019522
PMCPMC3829398
OpenAlexW2144102293

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.