Evidence map›Paper›PMID 11691931›Full record

ArticleNucleic acids research2001

Altering the GTP binding site of the DNA/RNA-binding protein, Translin/TB-RBP, decreases RNA binding and may create a dominant negative phenotype.

V M Chennathukuzhi, Y Kurihara, J D Bray, J Yang, N B Hecht

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Human RAS superfamily proteins and related GTPases.Science's STKE : signal transduction knowledge environment · 2004
    Review
  10. 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

5 authors at 1 institution in 1 country.

V M ChennathukuzhiCenter for Research on Reproduction and Women's Health and Department of Obstetrics and Gynecology, University of Pennsylvania School of Medicine, 1310 Biomedical Research Building II/III, 421 Curie Boulevard, Philadelphia, PA 19104-6142, USA.
Y Kurihara
J D Bray
J Yang
N B Hecht
University of Pennsylvania · US

Funding

GENE EXPRESSION DURING SPERMATOGENESISR01HD028832 · NICHD · UNIVERSITY OF PENNSYLVANIA · PI HECHT, NORMAN B · 1991 to 2006
$1.8M
RESEARCH AND TRAINING IN REPRODUCTIVE BIOLOGYT32HD007305 · NICHD · UNIVERSITY OF PENNSYLVANIA · PI COUTIFARIS, CHRISTOS · 1986 to 2010
$1.8M
NICHD NIH HHS HD 28832NICHD NIH HHS R01 HD028832NICHD NIH HHS T32 HD007305NICHD NIH HHS T32 HD07305
6 · The paper itself

Abstract

The DNA/RNA-binding protein, Translin/Testis Brain RNA-binding protein (Translin/TB-RBP), contains a putative GTP binding site in its C-terminus which is highly conserved. To determine if guanine nucleotide binding to this site functionally alters nucleic acid binding, electrophoretic mobility shift assays were performed with RNA and DNA binding probes. GTP, but not GDP, reduces RNA binding by approximately 50% and the poorly hydrolyzed GTP analog, GTPgammaS, reduces binding by >90% in gel shift and immunoprecipitation assays. No similar reduction of DNA binding is seen. When the putative GTP binding site of TB-RBP, amino acid sequence VTAGD, is altered to VTNSD by site directed mutagenesis, GTP will no longer bind to TB-RBP(GTP) and TB-RBP(GTP) no longer binds to RNA, although DNA binding is not affected. Yeast two-hybrid assays reveal that like wild-type TB-RBP, TB-RBP(GTP) will interact with itself, with wild-type TB-RBP and with Translin associated factor X (Trax). Transfection of TB-RBP(GTP) into NIH 3T3 cells leads to a marked increase in cell death suggesting a dominant negative function for TB-RBP(GTP) in cells. These data suggest TB-RBP is an RNA-binding protein whose activity is allosterically controlled by nucleotide binding.

Indexed as

3T3 CellsAllosteric RegulationAllosteric SiteAmino Acid SequenceAnimalsCarrier ProteinsCell DeathDimerizationDNADNA-Binding ProteinsGenes, DominantGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateHumansMaleCarrier ProteinsDNADNA-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateNuclear ProteinsRNARNA-Binding ProteinsTSNAX protein, humanTsnax protein, mouseTSN protein, humanTsn protein, mouse

Identifiers

PMID11691931
PMCPMC60198
OpenAlexW2080328112

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.