Evidence map›Paper›PMID 22451921›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Histone H3R17me2a mark recruits human RNA polymerase-associated factor 1 complex to activate transcription.

Jiacai Wu, Wei Xu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

59 citing papers in PubMed, 88 citations in OpenAlex.

  1. KDM4A Erases the H3R17me2a Mark, Facilitating Chromosome Condensation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. The emerging role of CARM1 in cancer.Cellular oncology (Dordrecht, Netherlands) · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Science advances · 2023
    Article
  14. Review
  15. Effectors and effects of arginine methylation.Biochemical Society transactions · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

2 authors at 1 institution in 1 country.

Jiacai WuMcArdle Laboratory for Cancer Research, University of Wisconsin, Madison, WI 53706, USA.
Wei Xu
University of Wisconsin–Madison · US

Funding

UW COMPREHENSIVE CANCER CENTER SUPPORTP30CA014520 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI AMY TRENTHAM-DIETZ · 1985 to 2026
$142.6M
Transcriptional Regulation of Estrogen Receptor (ER) by CARM1R01CA125387 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI XU, WEI · 2008 to 2012
$1.6M
NCI NIH HHS CA125387NCI NIH HHS P30 CA014520NCI NIH HHS P30CA014520NCI NIH HHS R01 CA125387
6 · The paper itself

Abstract

The histone coactivator-associated arginine methyltransferase 1 (CARM1) is a coactivator for a number of transcription factors, including nuclear receptors. Although CARM1 and its asymmetrically deposited dimethylation at histone H3 arginine 17 (H3R17me2a) are associated with transcription activation, the mechanism by which CARM1 activates transcription remains unclear. Using an unbiased biochemical approach, we discovered that the transcription elongation-associated PAF1 complex (PAF1c) directly interacts with H3R17me2a. PAF1c binds to histone H3 tails harboring dimethylation at R17 in CARM1-methylated histone octamers. Knockdown of either PAF1c subunits or CARM1 affected transcription of CARM1-regulated, estrogen-responsive genes. Furthermore, either CARM1 knockdown or CARM1 enzyme-deficient mutant knockin resulted in decreased H3R17me2a accompanied by the reduction of PAF1c occupancy at the proximal promoter estrogen-responsive elements. In contrast, PAF1c knockdown elicited no effects on H3R17me2a but reduced the H3K4me3 level at estrogen-responsive elements. These observations suggest that, apart from PAF1c's established roles in directing histone modifications, PAF1c acts as an arginine methyl histone effector that is recruited to promoters and activates a subset of genes, including targets of estrogen signaling.

Indexed as

ArginineEstrogen Receptor alphaEstrogensGene Knockdown TechniquesHEK293 CellsHistonesHumansMethylationNuclear ProteinsPromoter Regions, GeneticProtein-Arginine N-MethyltransferasesProtein BindingResponse ElementsTranscriptional ActivationTranscription FactorsArgininecoactivator-associated arginine methyltransferase 1Estrogen Receptor alphaEstrogensHistonesNuclear ProteinsPAF1 protein, humanProtein-Arginine N-MethyltransferasesTranscription Factors

Identifiers

PMID22451921
PMCPMC3326481
OpenAlexW2071166565

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.