Evidence map›Paper›PMID 12514098›Full record

ArticleGenes & development2003

Phosphorylation of histone H3 during transcriptional activation depends on promoter structure.

Mariano Labrador, Victor G Corces

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Upregulated SMYD3 promotes bladder cancer progression by targeting BCLAF1 and activating autophagy.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  6. Article
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  8. Article
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  10. Article
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  13. Article
  14. Regulation of chromatin structure by histone H3S10 phosphorylation.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2006
    Review
  15. Occupancy of the Drosophila hsp70 promoter by a subset of basal transcription factors diminishes upon transcriptional activation.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  16. Article
  17. Article
  18. Article
  19. Histone H3.3 is enriched in covalent modifications associated with active chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  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.

Mariano LabradorDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Victor G Corces
Johns Hopkins University · US

Funding

MOLECULAR BASIS OF SUPPRESSION IN DROSOPHILAR01GM035463 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CORCES, VICTOR G. · 1986 to 2020
$10.7M
NIGMS NIH HHS GM35463NIGMS NIH HHS R01 GM035463
6 · The paper itself

Abstract

Covalent modifications of histone N-terminal tails are required for the proper assembly and activation of the general transcription factors at promoters. Here, we analyze histone acetylation and phosphorylation in Drosophila transgenes activated by the yeast Gal4 transcriptional activator in the context of different promoters. We show that, independent of the promoter, transcription does not correlate with acetylation of either H3-Lys 14 or H4-Lys 8. Histone H3 associated with the DNA of Gal4-induced transcribing transgenes driven by the Drosophila Hsp70 promoter is hyperphosphorylated at Ser 10 during transcription. Surprisingly, histone H3 at Gal4-induced transgenes driven by the P element Transposase promoter is not hyperphosphorylated. The data suggest that transcription occurs without acetylated H4 and H3 in both transgenes in Drosophila polytene chromosomes. Instead, phosphorylation of H3 is linked to transcription and can be modulated by the structure of the promoter.

Indexed as

Promoter Regions, GeneticProtein Processing, Post-TranslationalTranscriptional ActivationAcetylationAnimalsAnimals, Genetically ModifiedDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsHistonesHSP70 Heat-Shock ProteinsNucleosomesPhosphorylationSaccharomyces cerevisiae ProteinsTATA BoxTATA-Box Binding ProteinDNA-Binding ProteinsDrosophila ProteinsGAL4 protein, S cerevisiaeHistonesHSP70 Heat-Shock ProteinsNucleosomesSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTransposases

Identifiers

PMID12514098
PMCPMC195963
OpenAlexW2117950771

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.