Evidence map›Paper›PMID 7729427›Full record

ArticleThe EMBO journal1995

Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID.

G Mengus, M May, X Jacq, A Staub, L Tora, P Chambon, I Davidson

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
11.3field-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

49 citing papers in PubMed, 113 citations in OpenAlex.

  1. Role of ATF7-TAF12 interactions in the vitamin D response hypersensitivity of osteoclast precursors in Paget's disease.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2013
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  6. Overexpression screens identify conserved dosage chromosome instability genes in yeast and human cancer.Proceedings of the National Academy of Sciences of the United States of America · 2016
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  11. Yeast two-hybrid map of Arabidopsis TFIID.Plant molecular biology · 2007
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  17. Isoform-specific interaction of HP1 with human TAFII130.Proceedings of the National Academy of Sciences of the United States of America · 2002
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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

7 authors at 3 institutions in 1 country.

G MengusInstitut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Collège de France, Illkirch, France.
M May
X Jacq
A Staub
L Tora
P Chambon
I Davidson
Collège de France · FRInserm · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have cloned cDNAs encoding three novel TAFIIs [TATA-binding protein (TBP)-associated factors] from the human (h) HeLa cell TFIID complexes hTAFII28, hTAFII20 and hTAFII18. hTAFII28 is a core hTAFII present in both of the previously described hTFIID species which either lack or contain hTAFII30 (hTFIID alpha and hTFIID beta respectively), and is the homologue of Drosophila (d)TAFII30 beta. hTAFII18 is a novel hTAFII which shows homology to the N-terminal region of the yeast TAFIISPT3, but has no known Drosophila counterpart. In contrast to hTAFII28, hTAFII18 is a TFIID beta-specific hTAFII. hTAFII20 is the homologue of p22, an alternatively spliced form of dTAFII30 alpha (p32). Using a combination of protein affinity chromatography and cotransfection and immunoprecipitation assays, we have identified a series of in vitro and intracellular interactions among the novel hTAFIIs and between the novel hTAFIIs and hTAFII30 or TBP. We show that hTAFII28 interacts with hTAFII18 both in vitro and intracellularly; in contrast to its Drosophila homologue, hTAFII28 also interacts directly with TBP. Deletion analysis indicates that TBP and hTAFII18 bind to distinct domains of hTAFII28. hTAFII18 also interacts with TBP, but it interacts more strongly with hTAFII28 and hTAFII30. The binding of hTAFII28 and hTAFII30 requires distinct domains of hTAFII18. As observed with the homologous Drosophila proteins, hTAFII20 interacts directly with TBP; however, additional interactions between hTAFII20 and hTAFII28 or hTAFII30 were detected. These results reveal differences not only in subunit composition, but also in the organization of dTFIID and hTFIID complexes.

Indexed as

Amino Acid SequenceAnimalsBase SequenceBinding SitesChromatography, AffinityCloning, MolecularDNA-Binding ProteinsDNA, ComplementaryDrosophilaHumansMacromolecular SubstancesModels, StructuralMolecular Sequence DataOligodeoxyribonucleotidesProtein BiosynthesisRecombinant ProteinsDNA-Binding ProteinsDNA, ComplementaryMacromolecular SubstancesOligodeoxyribonucleotidesRecombinant ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription Factor TFIID

Identifiers

PMID7729427
PMCPMC398239
OpenAlexW2311293739

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.