Evidence map›Paper›PMID 25998385›Full record

ArticleBiochemical and biophysical research communications2015

Characterization of DNA binding and pairing activities associated with the native SFPQ·NONO DNA repair protein complex.

Durga Udayakumar, William S Dynan

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 at 2 institutions in 1 country.

Durga UdayakumarInstitute of Molecular Medicine and Genetics, Georgia Regents University, Augusta, GA 30912, USA.
William S DynanInstitute of Molecular Medicine and Genetics, Georgia Regents University, Augusta, GA 30912, USA; Departments of Radiation Oncology and Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: wdynan@emory.edu.
Augusta University Health · USGeorgia Regents Medical Center · US

Funding

Regulation of DNA Double-Strand Break RepairR01CA098239 · NCI · MEDICAL COLLEGE OF GEORGIA (MCG) · PI DYNAN, WILLIAM S. · 2004 to 2013
$2.1M
NCI NIH HHS R01 CA098239
6 · The paper itself

Abstract

Nonhomologous end joining (NHEJ) is a major pathway for repair of DNA double-strand breaks. We have previously shown that a complex of SFPQ (PSF) and NONO (p54(nrb)) cooperates with Ku protein at an early step of NHEJ, forming a committed preligation complex and stimulating end-joining activity by 10-fold or more. SFPQ and NONO show no resemblance to other repair factors, and their mechanism of action is uncertain. Here, we use an optimized microwell-based assay to characterize the in vitro DNA binding behavior of the native SFPQ·NONO complex purified from human (HeLa) cells. SFPQ·NONO and Ku protein bind independently to DNA, with little evidence of cooperativity and only slight mutual interference at high concentration. Whereas Ku protein requires free DNA ends for binding, SFPQ·NONO does not. Both Ku and SFPQ·NONO have pairing activity, as measured by the ability of DNA-bound protein to capture a second DNA fragment in a microwell-based assay. Additionally, SFPQ·NONO stimulates DNA-dependent protein kinase autophosphorylation, consistent with the ability to promote formation of a synaptic complex formation without occluding the DNA termini proper. These findings suggest that SFPQ·NONO promotes end joining by binding to internal DNA sequences and cooperating with other repair proteins to stabilize a synaptic pre-ligation complex.

Indexed as

DNA RepairDNADNA-Binding ProteinsDNA End-Joining RepairDNA HelicasesHeLa CellsHumansKu AutoantigenNuclear Matrix-Associated ProteinsOctamer Transcription FactorsRNA-Binding ProteinsDNADNA-Binding ProteinsDNA HelicasesKu AutoantigenNONO protein, humanNuclear Matrix-Associated ProteinsOctamer Transcription FactorsRNA-Binding ProteinsXRCC5 protein, humanDNA bindingDNA repairNonhomologous end joiningNONOSFPQ

Identifiers

PMID25998385
PMCPMC4497844
OpenAlexW235945138

What OpenQuestion holds

Textmetadata
LicenceTDM
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.