Evidence map›Paper›PMID 17081996›Full record

ArticleMolecular cell2006

RSC exploits histone acetylation to abrogate the nucleosomal block to RNA polymerase II elongation.

Michael Carey, Bing Li, Jerry L Workman

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

108 citing papers in PubMed, 184 citations in OpenAlex.

  1. Review
  2. Article
  3. How does CHD4 slide nucleosomes?Biochemical Society transactions · 2024
    Review
  4. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  5. Frontiers in epigenetics and epigenomics · 2024
    Article
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  7. Article
  8. Review
  9. Review
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  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

48 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 2 institutions in 1 country.

Michael CareyStowers Medical Research Institute, 1000 East 50th Street, Kansas City, Missouri 64110, USA.
Bing Li
Jerry L Workman
Stowers Institute for Medical Research · USUniversity of California, Los Angeles · US

Funding

Interplay Between Chromatin and Co-Activator ComplexesR01GM074701 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CAREY, MICHAEL F · 2005 to 2025
$6.7M
Mechanisms of Transcriptional Regulation in ChromatinR37GM047867 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI WORKMAN, JERRY L · 2001 to 2010
$3.4M
MECHANISMS OF TRANSCRIPTIONAL REGULATION IN CHROMATINR01GM047867 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI WORKMAN, JERRY L · 1992 to 2014
$1.5M
NIGMS NIH HHS GM047867NIGMS NIH HHS GM074701NIGMS NIH HHS R01 GM074701NIGMS NIH HHS R37 GM047867
6 · The paper itself

Abstract

The coordinated action of histone acetyltransferases (HATs) and ATP-dependent chromatin remodeling enzymes in promoter-dependent transcription initiation represents a paradigm for how epigenetic information regulates gene expression. However, little is known about how such enzymes function during transcription elongation. Here, we investigated the role of RSC, a bromodomain-containing ATPase, in nucleosome transcription in vitro. Purified S. cerevisiae RNA polymerase II (Pol II) arrests at two primary locations on a positioned mononucleosome. RSC stimulates passage of Pol II through these sites. The function of RSC in elongation requires the energy of ATP hydrolysis. Moreover, the SAGA and NuA4 HATs strongly stimulated RSC's effect on elongation. The stimulation correlates closely with acetyl-CoA-dependent recruitment of RSC to nucleosomes. Thus, RSC can recognize acetylated nucleosomes and facilitate passage of Pol II through them. These data support the view that histone modifications regulate accessibility of the coding region to Pol II.

Indexed as

AcetylationAcetyltransferasesAdenosine TriphosphateAnimalsChromatin Assembly and DisassemblyDNA-Binding ProteinsHistone AcetyltransferasesHistonesNucleosomesProtein BindingRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsXenopus laevisAcetyltransferasesAdenosine TriphosphateDNA-Binding ProteinsHistone AcetyltransferasesHistonesNuA4 protein, S cerevisiaeNucleosomesRNA Polymerase IIRSC complex, S cerevisiaeSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeTrans-ActivatorsTranscription Factors

Identifiers

PMID17081996
PMCPMC1847601
OpenAlexW2008284328

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.