Evidence map›Paper›PMID 12489984›Full record

ArticleThe Biochemical journal2003

Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7.

Julia Kzhyshkowska, Andre Rusch, Hans Wolf, Thomas Dobner

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Emerging Roles of BRD7 in Pathophysiology.International journal of molecular sciences · 2020
    Review
  7. Review
  8. Article
  9. Article
  10. BRD7: a novel tumor suppressor gene in different cancers.American journal of translational research · 2016
    Review
  11. Article
  12. Article
  13. U7 small nuclear ribonucleoprotein represses histone gene transcription in cell cycle-arrested cells.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  14. Article
  15. 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

4 authors at 2 institutions in 1 country.

Julia KzhyshkowskaUniversität Heidelberg, Uni-Klinikum Mannheim, Dermatologie, Theodor-Kutzer-Ufer 1-3, D-68167 Mannheim, Germany. julia.kzhyshkowska@haut.ma.uni-heidelberg.de
Andre Rusch
Hans Wolf
Thomas Dobner
University of Regensburg · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

E1B-AP5 was initially identified as a target of the early adenovirus E1B-55 kDa protein during the course of lytic infection. E1B-AP5 belongs to the heterogeneous nuclear ribonucleoprotein family and was demonstrated to be involved in mRNA processing and transport [Gabler, Schutt, Groitl, Wolf, Shenk and Dobner (1998) J. Virol. 72, 7960-7971]. In the present paper, we demonstrate that E1B-AP5 differentially regulates basic and ligand-dependent transcription. We found that E1B-AP5 represses basic transcription driven by several virus and cellular promoters, and mapped the repression activity to the N-terminal part of the protein. In contrast with basic repression, E1B-AP5 activated the glucocorticoid-dependent promoter in the absence of dexamethasone, but did not contribute to the dexamethasone-induced activation. Mutant analysis indicated the presence of an additional cellular factor that modulates E1B-AP5 transcriptional activity. Using yeast two-hybrid screening, we identified a novel chromatin-associated bromodomain-containing protein, BRD7, as an E1B-AP5 interaction partner. We confirmed E1B-AP5-BRD7 complex formation in vivo and in vitro. We found that, although BRD7 binds to histones H2A, H2B, H3 and H4 through its bromodomain, this domain was not necessary for the interaction with E1B-AP5. Indeed, the triple complex formation of E1B-AP5, BRD7 and histones was demonstrated. Disruption of the E1B-AP5-BRD7 complex increased E1B-AP5 repression activity for basic transcription and converted it from being an activator of the hormone-dependent promoter into being a strong repressor. We conclude that complex formation between BRD7 and E1B-AP5 links chromatin events with mRNA processing at the level of transcriptional regulation.

Indexed as

Nuclear ProteinsTranscription, GeneticAnimalsBromodomain Containing ProteinsCell LineChromosomal Proteins, Non-HistoneGene Expression RegulationGenes, ReporterHeterogeneous-Nuclear RibonucleoproteinsHumansMammary Tumor Virus, MouseMiceMolecular Sequence DataPromoter Regions, GeneticRecombinant Fusion ProteinsRNA, MessengerBRD7 protein, humanBrd7 protein, mouseBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneHeterogeneous-Nuclear RibonucleoproteinsHNRNPUL1 protein, humanNuclear ProteinsRecombinant Fusion ProteinsRNA, MessengerTranscription Factors

Identifiers

PMID12489984
PMCPMC1223277
OpenAlexW1969905300

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.