ArticleProceedings of the National Academy of Sciences of the United States of America2008
p53 and TFIIEalpha share a common binding site on the Tfb1/p62 subunit of TFIIH.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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.
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.
Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Review
- Elf1 promotes transcription-coupled repair in yeast by using its C-terminal domain to bind TFIIH.Nature communications · 2024Article
- Structural polymorphism of the PH domain in TFIIH.Bioscience reports · 2023Article
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Three human RNA polymerases interact with TFIIH via a common RPB6 subunit.Nucleic acids research · 2022Article
- Structure of the p53/RNA polymerase II assembly.Communications biology · 2021Article
- Structural and dynamical insights into the PH domain of p62 in human TFIIH.Nucleic acids research · 2021Article
- High-resolution cryo-EM structures of TFIIH and their functional implications.Current opinion in structural biology · 2019Review
- Article
- The essential and multifunctional TFIIH complex.Protein science : a publication of the Protein Society · 2018Review
- Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways.Nucleic acids research · 2017Article
- Structural characterization of interactions between transactivation domain 1 of the p65 subunit of NF-κB and transcription regulatory factors.Nucleic acids research · 2017Article
- Structural visualization of the p53/RNA polymerase II assembly.Genes & development · 2016Article
- Dynamics of the Extended String-Like Interaction of TFIIE with the p62 Subunit of TFIIH.Biophysical journal · 2016Article
- Architecture of the Human and Yeast General Transcription and DNA Repair Factor TFIIH.Molecular cell · 2015Article
- A ΩXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- Structural and functional characterization of a complex between the acidic transactivation domain of EBNA2 and the Tfb1/p62 subunit of TFIIH.PLoS pathogens · 2014Article
- Structural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NER.Nucleic acids research · 2013Article
- Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2.Nucleic acids research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The general transcription factor IIH is recruited to the transcription preinitiation complex through an interaction between its p62/Tfb1 subunit and the alpha-subunit of the general transcription factor IIE (TFIIEalpha). We have determined that the acidic carboxyl terminus of TFIIEalpha (TFIIEalpha(336-439)) directly binds the amino-terminal PH domain of p62/Tfb1 with nanomolar affinity. NMR mapping and mutagenesis studies demonstrate that the TFIIEalpha binding site on p62/Tfb1 is identical to the binding site for the second transactivation domain of p53 (p53 TAD2). In addition, we demonstrate that TFIIEalpha(336-439) is capable of competing with p53 for a common binding site on p62/Tfb1 and that TFIIEalpha(336-439) and the diphosphorylated form (pS46/pT55) of p53 TAD2 have similar binding constants. NMR structural studies reveal that TFIIEalpha(336-439) contains a small domain (residues 395-433) folded in a novel betabetaalphaalphaalpha topology. NMR mapping studies demonstrate that two unstructured regions (residues 377-393 and residues 433-439) located on either side of the folded domain appear to be required for TFIIEalpha(336-439) binding to p62/Tfb1 and that these two unstructured regions are held close to each other in three-dimensional space by the novel structured domain. We also demonstrate that, like p53, TFIIEalpha(336-439) can activate transcription in vivo. These results point to an important interplay between the general transcription factor TFIIEalpha and the tumor suppressor protein p53 in regulating transcriptional activation that may be modulated by the phosphorylation status of p53.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.