Evidence map›Paper›PMID 20189987›Full record

ArticleThe Journal of biological chemistry2010

Direct transactivator-transcription factor IID (TFIID) contacts drive yeast ribosomal protein gene transcription.

Justin H Layer, Scott G Miller, P Anthony Weil

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

33 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. DecodingbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. What do Transcription Factors Interact With?Journal of molecular biology · 2021
    Review
  10. Article
  11. The TAFs of TFIID Bind and Rearrange the Topology of the TATA-LessInternational journal of molecular sciences · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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 1 institution in 1 country.

Justin H LayerDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615.
Scott G MillerDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615.
P Anthony WeilDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615. Electronic address: tony.weil@vanderbilt.edu.
Vanderbilt University · US

Funding

MOLECULAR GENETIC ANALYSIS OF YEAST TAFSR01GM052461 · NIGMS · VANDERBILT UNIVERSITY · PI WEIL, PETER ANTHONY · 1995 to 2011
$6.2M
Molecular Genetic Analysis of Yeast TAFsR56GM052461 · NIGMS · VANDERBILT UNIVERSITY · PI WEIL, PETER ANTHONY · 2007 to 2007
$500k
NIGMS NIH HHS GM52461NIGMS NIH HHS R01 GM052461NIGMS NIH HHS R56 GM052461
6 · The paper itself

Abstract

Transcription factor IID (TFIID) plays a key role in regulating eukaryotic gene expression by directly binding promoters and enhancer-bound transactivator proteins. However, the precise mechanisms and outcomes of transactivator-TFIID interaction remain unclear. Transcription of yeast ribosomal protein genes requires TFIID and the DNA-binding transactivator Rap1. We have previously shown that Rap1 directly binds to the TFIID complex through interaction with its TATA-binding protein-associated factor (Taf) subunits Taf4, -5, and -12. Here, we identify and characterize the Rap1 binding domains (RBDs) of Taf4 and Taf5. These RBDs are essential for viability but dispensable for Taf-Taf interactions and TFIID stability. Cells expressing altered Rap1 binding domains exhibit conditional growth, synthetic phenotypes when expressed in combination or with altered Rap1, and are selectively defective in ribosomal protein gene transcription. Taf4 and Taf5 proteins with altered RBDs bind Rap1 with reduced affinity. We propose that collectively the Taf4, Taf5, and Taf12 subunits of TFIID represent the physical and functional targets for Rap1 interaction and, furthermore, that these interactions drive ribosomal protein gene transcription.

Indexed as

Transcription, GeneticBinding SitesFungal ProteinsPolymerase Chain ReactionProtein BindingRibosomal ProteinsTrans-ActivatorsTranscription Factor TFIIDFungal ProteinsRibosomal ProteinsTrans-ActivatorsTranscription Factor TFIID

Identifiers

PMID20189987
PMCPMC2865315
OpenAlexW2009654808

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.