Evidence map›Paper›PMID 18007656›Full record

ArticleEMBO reports2008

Saccharomyces cerevisiae Rad16 mediates ultraviolet-dependent histone H3 acetylation required for efficient global genome nucleotide-excision repair.

Yumin Teng, Hairong Liu, Hefin W Gill, Yachuan Yu, Raymond Waters, Simon H Reed

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Photoreactivation Activities of Rad5, Rad16A and Rad16B HelpJournal of fungi (Basel, Switzerland) · 2024
    Article
  2. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  3. Article
  4. Article
  5. Epigenetic Regulation of Nucleotide Excision Repair.Frontiers in cell and developmental biology · 2022
    Review
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  7. Article
  8. Article
  9. Review
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  11. Article
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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

6 authors at 1 institution in 1 country.

Yumin TengDepartment of Pathology, School of Medicine, Cardiff University, Heath Park, Cardiff, UK.
Hairong Liu
Hefin W Gill
Yachuan Yu
Raymond Waters
Simon H Reed
Cardiff University · GB

Funding

Medical Research Council G0400113Medical Research Council G9900118
6 · The paper itself

Abstract

In yeast, global genome nucleotide-excision repair (GG-NER) requires a protein complex containing Rad7 and Rad16. Rad16 is a member of the switch/sucrose nonfermentable superfamily, and it is presumed that chromatin remodelling is its primary function during repair. We show that RAD16 is required for ultraviolet-dependent hyperacetylation of histone H3 (Lys 9 and Lys 14) at the MFA2 promoter and throughout the genome. The yeast repressor complex Ssn6-Tup1 represses many genes including MFA2. TUP1 deletion results in constitutive hyperacetylation of histone H3, nucleosome disruption and derepression of gene transcription in Tup1-regulated genes. GG-NER in the MFA2 promoter proceeds more rapidly in tup1Delta alpha-cells compared with wild type, even when transcription is inhibited. We show that elevated histone H3 acetylation levels in the MFA2 promoter in tup1Delta alpha-cells result in Rad7- and Rad16-independent GG-NER, and that Rad16 mediates the ultraviolet-induced acetylation of histone H3, necessary for efficient GG-NER.

Indexed as

Ultraviolet RaysAcetylationAdenosine TriphosphatasesDNA-Binding ProteinsDNA RepairGene DeletionGene Expression Regulation, FungalGenes, FungalGenome, FungalHistonesLipoproteinsNuclear ProteinsPheromonesPyrimidine DimersRepressor ProteinsSaccharomyces cerevisiaeAdenosine TriphosphatasesDNA-Binding ProteinsHistonesLipoproteinsMFA2 protein, S cerevisiaeNuclear ProteinsPheromonesPyrimidine DimersRAD16 protein, S cerevisiaeRAD7 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae ProteinsTUP1 protein, S cerevisiae

Identifiers

PMID18007656
PMCPMC2246617
OpenAlexW2039502138

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.