Evidence map›Paper›PMID 23613755›Full record

ArticlePloS one2013

A DNA damage response system associated with the phosphoCTD of elongating RNA polymerase II.

Tiffany Sabin Winsor, Bartlomiej Bartkowiak, Craig B Bennett, Arno L Greenleaf

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  3. Article
  4. Multiple roles of CTDK-I throughout the cell.Cellular and molecular life sciences : CMLS · 2019
    Review
  5. Review
  6. Article
  7. Shaping the cellular landscape with Set2/SETD2 methylation.Cellular and molecular life sciences : CMLS · 2017
    Review
  8. Article
  9. Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
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

4 authors at 2 institutions in 1 country.

Tiffany Sabin WinsorDepartment of Biochemistry, Duke Center for RNA Biology, Duke University Medical Center, Durham, North Carolina, United States of America.
Bartlomiej Bartkowiak
Craig B Bennett
Arno L Greenleaf
Duke Medical Center · USDuke University Hospital · US

Funding

TRANSCRIPTASE KINASES FROM YEAST AND DROSOPHILAR01GM040505 · NIGMS · DUKE UNIVERSITY · PI GREENLEAF, ARNO L. · 1988 to 2014
$5.1M
NIGMS NIH HHS GM040505NIGMS NIH HHS R01 GM040505
6 · The paper itself

Abstract

RNA polymerase II translocates across much of the genome and since it can be blocked by many kinds of DNA lesions, detects DNA damage proficiently; it thereby contributes to DNA repair and to normal levels of DNA damage resistance. However, the components and mechanisms that respond to polymerase blockage are largely unknown, except in the case of UV-induced damage that is corrected by nucleotide excision repair. Because elongating RNAPII carries with it numerous proteins that bind to its hyperphosphorylated CTD, we tested for effects of interfering with this binding. We find that expressing a decoy CTD-carrying protein in the nucleus, but not in the cytoplasm, leads to reduced DNA damage resistance. Likewise, inducing aberrant phosphorylation of the CTD, by deleting CTK1, reduces damage resistance and also alters rates of homologous recombination-mediated repair. In line with these results, extant data sets reveal a remarkable, highly significant overlap between phosphoCTD-associating protein genes and DNA damage-resistance genes. For one well-known phosphoCTD-associating protein, the histone methyltransferase Set2, we demonstrate a role in DNA damage resistance, and we show that this role requires the phosphoCTD binding ability of Set2; surprisingly, Set2's role in damage resistance does not depend on its catalytic activity. To explain all of these observations, we posit the existence of a CTD-Associated DNA damage Response (CAR) system, organized around the phosphoCTD of elongating RNAPII and comprising a subset of phosphoCTD-associating proteins.

Indexed as

DNA DamageMitosisPhosphorylationRNA Polymerase IIRNA Polymerase II

Identifiers

PMID23613755
PMCPMC3629013
OpenAlexW2040942628

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.