Evidence map›Paper›PMID 11406595›Full record

ArticleThe EMBO journal2001

UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation.

M Brand, J G Moggs, M Oulad-Abdelghani, F Lejeune, F J Dilworth, J Stevenin, G Almouzni, L Tora

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

94 citing papers in PubMed, 207 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Review
  12. Chronicles of the human SAGA co-activator complex.Nature structural & molecular biology · 2021
    Article
  13. Structure of the human SAGA coactivator complex.Nature structural & molecular biology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. The SF3b complex: splicing and beyond.Cellular and molecular life sciences : CMLS · 2020
    Review
  18. Review
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

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.

M BrandInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Department of 'Transcriptional and post-transcriptional control of gene regulation', CNRS/INSERM/ULP, BP 163, 67404 Illkirch Cedex, CU de Strasbourg.
J G Moggs
M Oulad-Abdelghani
F Lejeune
F J Dilworth
J Stevenin
G Almouzni
L Tora
Inserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initiation of transcription of protein-encoding genes by RNA polymerase II (Pol II) was thought to require transcription factor TFIID, a complex comprised of the TATA box-binding protein (TBP) and TBP-associated factors (TAF(II)s). In the presence of TBP-free TAF(II) complex (TFTC), initiation of Pol II transcription can occur in the absence of TFIID. TFTC containing the GCN5 acetyltransferase acetylates histone H3 in a nucleosomal context. We have identified a 130 kDa subunit of TFTC (SAP130) that shares homology with the large subunit of UV-damaged DNA-binding factor. TFTC preferentially binds UV-irradiated DNA, UV-damaged DNA inhibits TFTC-mediated Pol II transcription and TFTC is recruited in parallel with the nucleotide excision repair protein XP-A to UV-damaged DNA. TFTC preferentially acetylates histone H3 in nucleosomes assembled on UV-damaged DNA. In agreement with this, strong histone H3 acetylation occurs in intact cells after UV irradiation. These results suggest that the access of DNA repair machinery to lesions within chromatin may be facilitated by TFTC via covalent modification of chromatin. Thus, our experiments reveal a molecular link between DNA damage recognition and chromatin modification.

Indexed as

DNA DamageRNA-Binding ProteinsAcetylationAmino Acid SequenceDNA-Binding ProteinsDNA RepairHeLa CellsHistonesHumansMolecular Sequence DataNucleosomesPhosphoproteinsRibonucleoprotein, U2 Small NuclearRNA SplicingRNA Splicing FactorsTemplates, GeneticDNA-Binding ProteinsHistonesNucleosomesPhosphoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA Splicing FactorsSF3B1 protein, humanSf3b1 protein, mouseSF3B3 protein, humanXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID11406595
PMCPMC150203
OpenAlexW2008738118

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.