Evidence map›Paper›PMID 8665858›Full record

ArticleThe EMBO journal1996

Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.

M Vettese-Dadey, P A Grant, T R Hebbes, C Crane- Robinson, C D Allis, J L Workman

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 166 papers.

0numbers the graph read from it
0cells of the map it votes in
166citing papers in PubMed
14.6field-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

166 citing papers in PubMed, 473 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Effect of Culture Supernatant ofInternational journal of molecular sciences · 2024
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Histone mutations in cancer.Biochemical Society transactions · 2023
    Article
  16. Review
  17. Role of D(-)-Lactic Acid in Prevention ofPathogens (Basel, Switzerland) · 2023
    Article
  18. Article
  19. Article
  20. Article

106 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 at 1 institution in 1 country.

M Vettese-DadeyDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, PA 16802-4500, USA.
P A Grant
T R Hebbes
C Crane- Robinson
C D Allis
J L Workman
Pennsylvania State University · US

Funding

Wellcome Trust
6 · The paper itself

Abstract

Core histones isolated from normal and butyrate-treated HeLa cells have been reconstituted into nucleosome cores in order to analyze the role of histone acetylation in enhancing transcription factor binding to recognition sites in nucleosomal DNA. Moderate stimulation of nucleosome binding was observed for the basic helix-loop-helix factor USF and the Zn cluster DNA binding domain factor GAL4-AH using heterogeneously acetylated histones. However, by coupling novel immunoblotting techniques to a gel retardation assay, we observed that nucleosome cores containing the most highly acetylated forms of histone H4 have the highest affinity for these two transcription factors. Western analysis of gel-purified USF-nucleosome and GAL4-AH-nucleosome complexes demonstrated the predominant presence of acetylated histone H4 relative to acetylated histone H3. Immunoprecipitation of USF-nucleosome complexes with anti-USF antibodies also demonstrated that these complexes were enriched preferentially in acetylated histone H4. These data show that USF and GAL4-AH preferentially interact with nucleosome cores containing highly acetylated histone H4. Acetylation of histone H4 thus appears to play a primary role in the structural changes that mediate enhanced binding of transcription factors to their recognition sites within nucleosomes.

Indexed as

DNA-Binding ProteinsProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsAcetylationBase SequenceButyratesButyric AcidDNAFungal ProteinsHeLa CellsHelix-Loop-Helix MotifsHistonesHumansMolecular Sequence DataNucleosomesProtein BindingButyratesButyric AcidDNADNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeHistonesNucleosomesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsUpstream Stimulatory FactorsUSF1 protein, human

Identifiers

PMID8665858
PMCPMC450183
OpenAlexW1540264737

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.