Evidence map›Paper›PMID 12215531›Full record

ArticleMolecular and cellular biology2002

The Ccr4-not complex and yTAF1 (yTaf(II)130p/yTaf(II)145p) show physical and functional interactions.

Cécile Deluen, Nicole James, Laurent Maillet, Miguel Molinete, Grégory Theiler, Marc Lemaire, Nicole Paquet, Martine A Collart

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 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

44 citing papers in PubMed, 69 citations in OpenAlex.

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  6. Def1 interacts with TFIIH and modulates RNA polymerase II transcription.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

8 authors at 1 institution in 1 country.

Cécile DeluenDépartement de Biochimie Médicale, CMU, 1211 Geneva 4, Switzerland.
Nicole James
Laurent Maillet
Miguel Molinete
Grégory Theiler
Marc Lemaire
Nicole Paquet
Martine A Collart
Bio-Medical Science (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Saccharomyces cerevisiae Ccr4-Not complex is a global regulator of transcription that is thought to regulate TATA binding protein (TBP) function at certain promoters specifically. In this paper, we show interactions between the essential domain of Not1p, which interacts with Not4p and Not5p, and the N-terminal domain of yTAF1. We isolated a temperature-sensitive nonsense allele of TAF1, taf1-4, which is synthetically lethal at the permissive temperature when combined with not4 and not5 mutants and which produces high levels of a C-terminally truncated yTAF1 derivative. Overexpression of C-terminally truncated yTAF1 is toxic in not4 or not5 mutants, whereas overexpression of full-length yTAF1 suppresses not4. Furthermore, mutations in the autoinhibitory N-terminal TAND domain of yTAF1 suppress not5, and the overexpression of similar mutants does not suppress not4. We find that, like Not5p, yTAF1 acts as a repressor of stress response element-dependent transcription. Finally, we have evidence for stress-regulated occupancy of promoter DNA by Not5p and for Not5p-dependent regulation of yTAF1 association with promoter DNA. Taken together with our finding that Not1p copurifies with glutathione S-transferase-yTaf1 in large complexes, these results provide the first molecular evidence that the Ccr4-Not complex might interact with yTAF1 to regulate its association at promoters, a function that might in turn regulate the autoinhibitory N-terminal domain of yTAF1.

Indexed as

TATA-Binding Protein Associated FactorsCell Cycle ProteinsDNA-Binding ProteinsFungal ProteinsGene Expression Regulation, FungalMacromolecular SubstancesMutagenesis, Site-DirectedProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRepressor ProteinsRibonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureTranscription FactorsCCR4 protein, S cerevisiaeCDC39 protein, S cerevisiaeCell Cycle ProteinsDNA-Binding ProteinsFungal ProteinsMacromolecular SubstancesMOT2 protein, S cerevisiaeNOT5 protein, S cerevisiaeRecombinant Fusion ProteinsRepressor ProteinsRibonucleasesSaccharomyces cerevisiae ProteinsTAF1 protein, S cerevisiaeTATA-Binding Protein Associated FactorsTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIDUbiquitin-Protein Ligases

Identifiers

PMID12215531
PMCPMC134042
OpenAlexW2097207357

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.