Evidence map›Paper›PMID 9171077›Full record

ArticleNucleic acids research1997

NonO enhances the association of many DNA-binding proteins to their targets.

Y S Yang, M C Yang, P W Tucker, J D Capra

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.0field-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

25 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
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  13. Article
  14. Article
  15. Crystallization of a paraspeckle protein PSPC1-NONO heterodimer.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  16. Article
  17. Review
  18. Article
  19. Complex assembly on the human CYP17 promoter.Molecular and cellular endocrinology · 2009
    Review
  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

4 authors at 1 institution in 1 country.

Y S YangMolecular Immunology Center, Department of Microbiology, The University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, TX 75235-9140, USA.
M C Yang
P W Tucker
J D Capra
The University of Texas Southwestern Medical Center · US

Funding

XERODERMA PIGMENTOSUM VARIANT--GENETIC ANALYSIS AND GENE MAPPINGP30AR041940 · NIAMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI BERGSTRESSER, PAUL R · 1992 to 2005
$3.7M
IMMUNOGLOBULIN V REGION STRUCTURES: GENETIC IMPLICATIONR01AI012127 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI CAPRA, J DONALD · 1985 to 2003
$1.2M
NUCLEIC ACID STUDIES OF ANTIARSONATE HYBRIDOMASR01AI018499 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI TUCKER, PHILIP W. · 1985 to 1996
–
IMMUNOGLOBULIN V REGION STRUCTURES;GENETIC IMPLICATIONSR37AI012127 · NIAID · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI CAPRA, J DONALD · 1987 to 1997
–
NIAID NIH HHS AI-12127NIAID NIH HHS AI-18499NIAMS NIH HHS AR-41940
6 · The paper itself

Abstract

NonO is an unusual nucleic acid binding protein not only in that it binds both DNA and RNA but that it does so via functionally separable domains. Here we document that NonO enhances the binding of some (E47, OTF-1 and OTF-2) but not all (PEA3) conventional sequence-specific transcription factors to their recognition sites in artificial substrates as well as in an immunoglobulin VHpromoter. We also show that NonO induces the binding of the Ku complex to DNA ends. Ku has no known DNA sequence specificity. These enhancement of binding effects are NonO concentration dependent. Using the E box activity of E47 as a model, kinetic studies demonstrate that the association rate of the protein-DNA complex increases in the presence of NonO while the dissociation rate remains the same, thereby increasing the sum total of the interaction. Oligo competition experiments indicate that NonO does not contact the target DNA in order to enhance the binding activity of DNA binding proteins. Rather, methylation interference analysis reveals that the induced E47 binding-activity has the same DNA-binding sequence specificity as the normal binding. This result suggests that one of the effects of NonO is to induce a true protein-DNA interaction. In this way, it might be possible for NonO to play a crucial role in gene regulation.

Indexed as

Antigens, NuclearDNA HelicasesSaccharomyces cerevisiae ProteinsBinding SitesCyclin D1DNADNA-Binding ProteinsDNA MethylationGene Expression RegulationGenes, ImmunoglobulinGlutathione TransferaseHost Cell Factor C1Immunoglobulin Heavy ChainsImmunoglobulin Variable RegionKineticsKu AutoantigenAntigens, NuclearCyclin D1DNADNA-Binding ProteinsDNA HelicasesGlutathione Transferasehigh affinity DNA-binding factor, S cerevisiaeHost Cell Factor C1Immunoglobulin Heavy ChainsImmunoglobulin Variable RegionKu AutoantigenNuclear ProteinsOctamer Transcription Factor-1Oligonucleotide ProbesProto-Oncogene ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsXRCC5 protein, humanXrcc6 protein, human

Identifiers

PMID9171077
PMCPMC146775
OpenAlexW2143573846

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.