Evidence map›Paper›PMID 21518915›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Dynamic acetylation of all lysine-4 trimethylated histone H3 is evolutionarily conserved and mediated by p300/CBP.

Nicholas T Crump, Catherine A Hazzalin, Erin M Bowers, Rhoda M Alani, Philip A Cole, Louis C Mahadevan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
–field-weighted citation impact
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

67 citing papers in PubMed.

  1. Trial
  2. Article
  3. Biochemistry and regulation of histone lysine L-lactylation.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Review
  6. Targeting lysine acetylation readers and writers.Nature reviews. Drug discovery · 2025
    Review
  7. Basic Epigenetic Mechanisms.Sub-cellular biochemistry · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Olfactory Receptor OR7A17 Expression Correlates with All-International journal of molecular sciences · 2021
    Article
  17. Review
  18. Article
  19. Article
  20. Is There a Histone Code for Cellular Quiescence?Frontiers in cell and developmental biology · 2021
    Review

7 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

6 authors.

Nicholas T CrumpNuclear Signalling Laboratory, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom.
Catherine A Hazzalin
Erin M Bowers
Rhoda M Alani
Philip A Cole
Louis C Mahadevan

Funding

Medical Research CouncilWellcome Trust
6 · The paper itself

Abstract

Histone modifications are reported to show different behaviors, associations, and functions in different genomic niches and organisms. We show here that rapid, continuous turnover of acetylation specifically targeted to all K4-trimethylated H3 tails (H3K4me3), but not to bulk histone H3 or H3 carrying other methylated lysines, is a common uniform characteristic of chromatin biology in higher eukaryotes, being precisely conserved in human, mouse, and Drosophila. Furthermore, dynamic acetylation targeted to H3K4me3 is mediated by the same lysine acetyltransferase, p300/cAMP response element binding (CREB)-binding protein (CBP), in both mouse and fly cells. RNA interference or chemical inhibition of p300/CBP using a newly discovered small molecule inhibitor, C646, blocks dynamic acetylation of H3K4me3 globally in mouse and fly cells, and locally across the promoter and start-site of inducible genes in the mouse, thereby disrupting RNA polymerase II association and the activation of these genes. Thus, rapid dynamic acetylation of all H3K4me3 mediated by p300/CBP is a general, evolutionarily conserved phenomenon playing an essential role in the induction of immediate-early (IE) genes. These studies indicate a more global function of p300/CBP in mediating rapid turnover of acetylation of all H3K4me3 across the nuclei of higher eukaryotes, rather than a tight promoter-restricted function targeted by complex formation with specific transcription factors.

Indexed as

AcetylationAnimalsBinding SitesCell LineDrosophilaDrosophila ProteinsEvolution, MolecularGene Knockdown TechniquesGenes, fosGenes, Immediate-EarlyGenes, junHistone AcetyltransferasesHistone Deacetylase InhibitorsHistonesHumansHydroxamic AcidsDrosophila ProteinsHistone AcetyltransferasesHistone Deacetylase InhibitorsHistonesHydroxamic AcidsLysinep300-CBP Transcription Factorstrichostatin A

Identifiers

PMID21518915
PMCPMC3093510

What OpenQuestion holds

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Registered trials

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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.