Evidence map›Paper›PMID 22914091›Full record

ArticleNature2012

Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes.

Swaminathan Venkatesh, Michaela Smolle, Hua Li, Madelaine M Gogol, Malika Saint, Shambhu Kumar, Krishnamurthy Natarajan, Jerry L Workman

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 213 papers.

0numbers the graph read from it
0cells of the map it votes in
213citing papers in PubMed
15.2field-weighted citation impact, top 1% 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

213 citing papers in PubMed, 320 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. The Roles of Topoisomerases in Transcriptional Regulation.International journal of molecular sciences · 2026
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Set2 and H3K36 regulate thebioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Swaminathan VenkateshStowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, Missouri 64110, USA.
Michaela Smolle
Hua Li
Madelaine M Gogol
Malika Saint
Shambhu Kumar
Krishnamurthy Natarajan
Jerry L Workman
Stowers Institute for Medical Research · USJawaharlal Nehru University · IN

Funding

MECHANISMS OF TRANSCRIPTIONAL REGULATION IN CHROMATINR01GM047867 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI WORKMAN, JERRY L · 1992 to 2014
$1.5M
NIGMS NIH HHS R01 GM047867NIGMS NIH HHS R01GM04867
6 · The paper itself

Abstract

Set2-mediated methylation of histone H3 at Lys 36 (H3K36me) is a co-transcriptional event that is necessary for the activation of the Rpd3S histone deacetylase complex, thereby maintaining the coding region of genes in a hypoacetylated state. In the absence of Set2, H3K36 or Rpd3S acetylated histones accumulate on open reading frames (ORFs), leading to transcription initiation from cryptic promoters within ORFs. Although the co-transcriptional deacetylation pathway is well characterized, the factors responsible for acetylation are as yet unknown. Here we show that, in yeast, co-transcriptional acetylation is achieved in part by histone exchange over ORFs. In addition to its function of targeting and activating the Rpd3S complex, H3K36 methylation suppresses the interaction of H3 with histone chaperones, histone exchange over coding regions and the incorporation of new acetylated histones. Thus, Set2 functions both to suppress the incorporation of acetylated histones and to signal for the deacetylation of these histones in transcribed genes. By suppressing spurious cryptic transcripts from initiating within ORFs, this pathway is essential to maintain the accuracy of transcription by RNA polymerase II.

Indexed as

AcetylationCell Cycle ProteinsGenes, FungalHistonesLysineMethylationMethyltransferasesMolecular ChaperonesOpen Reading FramesPhenotypeRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticASF1 protein, S cerevisiaeCell Cycle ProteinsHistonesLysineMethyltransferasesMolecular ChaperonesRNA Polymerase IISaccharomyces cerevisiae ProteinsSet2 protein, S cerevisiae

Identifiers

PMID22914091
OpenAlexW1984436755

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.