Evidence map›Paper›PMID 20007604›Full record

ArticleNucleic acids research2010

Rad26p, a transcription-coupled repair factor, is recruited to the site of DNA lesion in an elongating RNA polymerase II-dependent manner in vivo.

Shivani Malik, Priyasri Chaurasia, Shweta Lahudkar, Geetha Durairaj, Abhijit Shukla, Sukesh R Bhaumik

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

40 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. Photoreactivation Activities of Rad5, Rad16A and Rad16B HelpJournal of fungi (Basel, Switzerland) · 2024
    Article
  3. DNA Repair in Nucleosomes: Insights from Histone Modifications and Mutants.International journal of molecular sciences · 2024
    Review
  4. Article
  5. The Paf1 complex is required for RNA polymerase II removal in response to DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Article
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  11. Molecular basis of chromatin remodeling by Rhp26, a yeast CSB ortholog.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Article
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  19. Review
  20. Regulation of the Rhp26ERCC6/CSB chromatin remodeler by a novel conserved leucine latch motif.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 1 institution in 1 country.

Shivani MalikDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, 1245 Lincoln Drive, Carbondale, IL-62901, USA.
Priyasri Chaurasia
Shweta Lahudkar
Geetha Durairaj
Abhijit Shukla
Sukesh R Bhaumik
Southern Illinois University School of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rad26p, a yeast homologue of human Cockayne syndrome B with an ATPase activity, plays a pivotal role in stimulating DNA repair at the coding sequences of active genes. On the other hand, DNA repair at inactive genes or silent areas of the genome is not regulated by Rad26p. However, how Rad26p recognizes DNA lesions at the actively transcribing genes to facilitate DNA repair is not clearly understood in vivo. Here, we show that Rad26p associates with the coding sequences of genes in a transcription-dependent manner, but independently of DNA lesions induced by 4-nitroquinoline-1-oxide in Saccharomyces cerevisiae. Further, histone H3 lysine 36 methylation that occurs at the active coding sequence stimulates the recruitment of Rad26p. Intriguingly, we find that Rad26p is recruited to the site of DNA lesion in an elongating RNA polymerase II-dependent manner. However, Rad26p does not recognize DNA lesions in the absence of active transcription. Together, these results provide an important insight as to how Rad26p is delivered to the damage sites at the active, but not inactive, genes to stimulate repair in vivo, shedding much light on the early steps of transcription-coupled repair in living eukaryotic cells.

Indexed as

DNA DamageTranscription, GeneticAdenosine TriphosphatasesBinding SitesHistonesMethylationRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesHistonesRAD26 protein, S cerevisiaeRNA Polymerase IISaccharomyces cerevisiae Proteins

Identifiers

PMID20007604
PMCPMC2836574
OpenAlexW2007986017

What OpenQuestion holds

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LicenceCC BY-NC
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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.