Evidence map›Paper›PMID 12052880›Full record

ArticleMolecular and cellular biology2002

Proteomics of the eukaryotic transcription machinery: identification of proteins associated with components of yeast TFIID by multidimensional mass spectrometry.

Steven L Sanders, Jennifer Jennings, Adrian Canutescu, Andrew J Link, P Anthony Weil

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
10.3field-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

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 292 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Frontiers in epigenetics and epigenomics · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  14. The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  15. The SAGA continues: The rise of cis- and trans-histone crosstalk pathways.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

80 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

5 authors at 1 institution in 1 country.

Steven L SandersDepartment of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615, USA.
Jennifer Jennings
Adrian Canutescu
Andrew J Link
P Anthony Weil
Vanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
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
NCI NIH HHS 5P30CA68485NCI NIH HHS P30 CA068485NIGMS NIH HHS GM52461NIGMS NIH HHS R01 GM052461NIGMS NIH HHS R56 GM052461
6 · The paper itself

Abstract

The general transcription factor TFIID is a multisubunit complex of TATA-binding protein (TBP) and 14 distinct TBP-associated factors (TAFs). Although TFIID constituents are required for transcription initiation of most mRNA encoding genes, the mechanism of TFIID action remains unclear. To gain insight into TFIID function, we sought to generate a proteomic catalogue of proteins specifically interacting with TFIID subunits. Toward this end, TFIID was systematically immunopurified by using polyclonal antibodies directed against each subunit, and the constellation of TBP- and TAF-associated proteins was directly identified by coupled multidimensional liquid chromatography and tandem mass spectrometry. A number of novel protein-protein associations were observed, and several were characterized in detail. These interactions include association between TBP and the RSC chromatin remodeling complex, the TAF17p-dependent association of the Swi6p transactivator protein with TFIID, and the identification of three novel subunits of the SAGA acetyltransferase complex, including a putative ubiquitin-specific protease component. Our results provide important new insights into the mechanisms of mRNA gene transcription and demonstrate the feasibility of constructing a complete proteomic interaction map of the eukaryotic transcription apparatus.

Indexed as

TATA-Binding Protein Associated FactorsChromatography, LiquidDNA-Binding ProteinsFungal ProteinsImmunochemistryMass SpectrometryMutationProteomeReproducibility of ResultsSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIDYeastsDNA-Binding ProteinsFungal ProteinsProteomeSaccharomyces cerevisiae ProteinsSAGA protein, Emericella nidulansSWI6 protein, S cerevisiaeTAF9 protein, S cerevisiaeTATA-Binding Protein Associated FactorsTATA-Box Binding ProteinTranscription FactorsTranscription Factors, TFIITranscription Factor TFIID

Identifiers

PMID12052880
PMCPMC133885
OpenAlexW2167653615

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.