Evidence map›Paper›PMID 11564872›Full record

ArticleMolecular and cellular biology2001

Positive and negative TAF(II) functions that suggest a dynamic TFIID structure and elicit synergy with traps in activator-induced transcription.

M Guermah, Y Tao, R G Roeder

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. 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
2.9field-weighted citation impact, top 9% 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, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The TAFs of TFIID Bind and Rearrange the Topology of the TATA-LessInternational journal of molecular sciences · 2019
    Article
  7. Article
  8. Article
  9. The Mediator complex: a central integrator of transcription.Nature reviews. Molecular cell biology · 2015
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Core promoter binding by histone-like TAF complexes.Molecular and cellular biology · 2005
    Article
  19. 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

3 authors at 1 institution in 1 country.

M GuermahLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021, USA.
Y Tao
R G Roeder
Rockefeller University · US

Funding

BIOCHEMICAL MECHANISMS OF HIV TRANSCRIPTIONAL REGULATIONR01AI037327 · NIAID · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 1995 to 1999
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MOLECULAR BASIS OF CELL GROWTH AND TRANSFORMATIONR35CA042567 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 1986 to 1999
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NCI NIH HHS CA 42567NIAID NIH HHS AI 37327
6 · The paper itself

Abstract

Human transcription factor TFIID contains the TATA-binding protein (TBP) and several TBP-associated factors (TAF(II)s). To elucidate the structural organization and function of TFIID, we expressed and characterized the product of a cloned cDNA encoding human TAF(II)135 (hTAF(II)135). Comparative far Western blots have shown that hTAF(II)135 interacts strongly with hTAF(II)20, moderately with hTAF(II)150, and weakly with hTAF(II)43 and hTAF(II)250. Consistent with these observations and with sequence relationships of hTAF(II)20 and hTAF(II)135 to histones H2B and H2A, respectively, TFIID preparations that contain higher levels of hTAF(II)135 also contain higher levels of hTAF(II)20, and the interaction between hTAF(II)20 and hTAF(II)135 is critical for human TFIID assembly in vitro. From a functional standpoint, hTAF(II)135 has been found to interact strongly and directly with hTFIIA and (within a complex that also contains hTBP and hTAF(II)250) to specifically cooperate with TFIIA to relieve TAF(II)250-mediated repression of TBP binding and function on core promoters. Finally, we report a functional synergism between TAF(II)s and the TRAP/Mediator complex in activated transcription, manifested as hTAF(II)-mediated inhibition of basal transcription and a consequent TRAP requirement for both a high absolute level of activated transcription and a high and more physiological activated/basal transcription ratio. These results suggest a dynamic TFIID structure in which the switch from a basal hTAF(II)-enhanced repression state to an activator-mediated activated state on a promoter may be mediated in part through activator or coactivator interactions with hTAF(II)135.

Indexed as

TATA-Binding Protein Associated FactorsTranscription, GeneticBlotting, WesternChromatography, GelCloning, MolecularDeoxyribonuclease IDNA-Binding ProteinsDNA, ComplementaryHistone AcetyltransferasesHistonesHumansModels, GeneticNuclear ProteinsPromoter Regions, GeneticProtein BindingProtein Structure, TertiaryDeoxyribonuclease IDNA-Binding ProteinsDNA, ComplementaryHistone AcetyltransferasesHistonesNuclear ProteinsTAF4 protein, humanTATA-binding protein associated factor 250 kDaTATA-Binding Protein Associated FactorsTrans-ActivatorsTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIATranscription Factor TFIID

Identifiers

PMID11564872
PMCPMC99865
OpenAlexW2128907425

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.