Evidence map›Paper›PMID 22373916›Full record

ArticleNucleic acids research2012

Structural and functional characterization of interactions involving the Tfb1 subunit of TFIIH and the NER factor Rad2.

Julien Lafrance-Vanasse, Geneviève Arseneault, Laurent Cappadocia, Hung-Ta Chen, Pascale Legault, James G Omichinski

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Photoreactivation Activities of Rad5, Rad16A and Rad16B HelpJournal of fungi (Basel, Switzerland) · 2024
    Article
  5. Article
  6. Review
  7. Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. XPG: a multitasking genome caretaker.Cellular and molecular life sciences : CMLS · 2022
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. 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 · 2015
    Article
  15. Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015
    Review
  16. Article
  17. Review
  18. 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

6 authors at 2 institutions in 2 countries.

Julien Lafrance-VanasseDépartement de Biochimie, Université de Montréal, C.P. 6128, Succursale Centre-Ville, Montréal, QC H3C 3J7, Canada.
Geneviève Arseneault
Laurent Cappadocia
Hung-Ta Chen
Pascale Legault
James G Omichinski
Université de Montréal · CAInstitute of Molecular Biology, Academia Sinica · TW

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

The general transcription factor IIH (TFIIH) plays crucial roles in transcription as part of the pre-initiation complex (PIC) and in DNA repair as part of the nucleotide excision repair (NER) machinery. During NER, TFIIH recruits the 3'-endonuclease Rad2 to damaged DNA. In this manuscript, we functionally and structurally characterized the interaction between the Tfb1 subunit of TFIIH and Rad2. We show that deletion of either the PH domain of Tfb1 (Tfb1PH) or several segments of the Rad2 spacer region yield yeast with enhanced sensitivity to UV irradiation. Isothermal titration calorimetry studies demonstrate that two acidic segments of the Rad2 spacer bind to Tfb1PH with nanomolar affinity. Structure determination of a Rad2-Tfb1PH complex indicates that Rad2 binds to TFIIH using a similar motif as TFIIEα uses to bind TFIIH in the PIC. Together, these results provide a mechanistic bridge between the role of TFIIH in transcription and DNA repair.

Indexed as

Amino Acid SequenceBinding SitesDNA-Binding ProteinsEndodeoxyribonucleasesModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryProtein SubunitsRadiation ToleranceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence DeletionTranscription Factors, TFIITumor Suppressor Protein p53Ultraviolet RaysDNA-Binding ProteinsEndodeoxyribonucleasesProtein SubunitsRAD2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTFB1 protein, S cerevisiaeTranscription Factors, TFIItranscription factor TFIIETumor Suppressor Protein p53

Identifiers

PMID22373916
PMCPMC3384317
OpenAlexW2082682714

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.