Evidence map›Paper›PMID 12391174›Full record

ArticleMolecular and cellular biology2002

Subnuclear localization of Ku protein: functional association with RNA polymerase II elongation sites.

Xianming Mo, William S Dynan

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

36 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. The Role of Ku70 as a Cytosolic DNA Sensor in Innate Immunity and Beyond.Frontiers in cellular and infection microbiology · 2021
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Transcription-induced DNA double strand breaks: both oncogenic force and potential therapeutic target?Clinical cancer research : an official journal of the American Association for Cancer Research · 2011
    Article
  20. 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

2 authors.

Xianming MoInstitute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, Georgia 30912, USA.
William S Dynan

Funding

MOLECULAR MECHANISM OF TRANSCRIPTIONAL ACTIVATIONR01GM035866 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI DYNAN, WILLIAM S · 1986 to 2004
$1.1M
NIGMS NIH HHS GM 35866NIGMS NIH HHS R01 GM035866
6 · The paper itself

Abstract

Ku is an abundant nuclear protein with an essential function in the repair of DNA double-strand breaks. Various observations suggest that Ku also interacts with the cellular transcription machinery, although the mechanism and significance of this interaction are not well understood. In the present study, we investigated the subnuclear distribution of Ku in normally growing human cells by using confocal microscopy, chromatin immunoprecipitation, and protein immunoprecipitation. All three approaches indicated association of Ku with RNA polymerase II (RNAP II) elongation sites. This association occurred independently of the DNA-dependent protein kinase catalytic subunit and was highly selective. There was no detectable association with the initiating isoform of RNAP II or with the general transcription initiation factors. In vitro protein-protein interaction assays demonstrated that the association of Ku with elongation proteins is mediated, in part, by a discrete C-terminal domain in the Ku80 subunit. Functional disruption of this interaction with a dominant-negative mutant inhibited transcription in vitro and in vivo and suppressed cell growth. These results suggest that association of Ku with transcription sites is important for maintenance of global transcription levels. Tethering of double-strand break repair proteins to defined subnuclear structures may also be advantageous in maintenance of genome stability.

Indexed as

Antigens, NuclearDNA HelicasesTranscription, GeneticAmino Acid SequenceAnimalsCell-Free SystemCell LineChromatinDNA-Binding ProteinsDNA RepairHumansImmunohistochemistryIsoenzymesKu AutoantigenMolecular Sequence DataNuclear ProteinsAntigens, NuclearChromatinDNA-Binding ProteinsDNA HelicasesIsoenzymesKu AutoantigenNuclear ProteinsRecombinant Fusion ProteinsRNA Polymerase IITranscription FactorsXRCC5 protein, humanXrcc6 protein, human

Identifiers

PMID12391174
PMCPMC134733

What OpenQuestion holds

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Registered trials

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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.