ArticleNucleic acids research2000
A new double-stranded RNA-binding protein that interacts with PKR.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Proteomics-based determination of double-stranded RNA interactome reveals known and new factors involved in Sindbis virus infection.RNA (New York, N.Y.) · 2023Article
- Identification ofFrontiers in oncology · 2020Article
- Staufen1 promotes HCV replication by inhibiting protein kinase R and transporting viral RNA to the site of translation and replication in the cells.Nucleic acids research · 2016Article
- The RNA binding complexes NF45-NF90 and NF45-NF110 associate dynamically with the c-fos gene and function as transcriptional coactivators.The Journal of biological chemistry · 2015Article
- 'Black sheep' that don't leave the double-stranded RNA-binding domain fold.Trends in biochemical sciences · 2014Review
- Staufen1-mediated mRNA decay induces Requiem mRNA decay through binding of Staufen1 to the Requiem 3'UTR.Nucleic acids research · 2014Article
- NF90 in posttranscriptional gene regulation and microRNA biogenesis.International journal of molecular sciences · 2013Review
- Nuclear Factor 90, a cellular dsRNA binding protein inhibits the HIV Rev-export function.Retrovirology · 2006Article
- RNA binding and intramolecular interactions modulate the regulation of gene expression by nuclear factor 110.RNA (New York, N.Y.) · 2003Article
- The RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cells.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have identified a 74 kDa double-stranded (ds)RNA-binding protein that shares extensive homology with the mouse spermatid perinuclear RNA-binding (Spnr) protein. p74 contains two dsRNA-binding motifs (dsRBMs) that are essential for preferential binding to dsRNA. Previously, dsRNA-binding proteins were shown to undergo homo- and heterodimerization, raising the possibility that regulation of activity could be controlled by interactions between different family members. Homodimerization is required to activate the dsRNA-dependent protein kinase PKR, whereas hetero-dimerization between PKR and other dsRNA-binding proteins can inhibit kinase activity. We have found that p74 also interacts with PKR, both the wild-type enzyme and a catalytically defective mutant (K296R). While co-expression of p74 and wild-type PKR in the yeast Saccharomyces cerevisiae did not alter PKR activity, co-expression of p74 and the catalytically defective K296R mutant surprisingly resulted in abnormal morphology and cell death in transformants that maintained a high level of p74 expression. These transformants could be rescued by overexpression of the alpha-subunit of wild-type eukaryotic translation initiation factor 2 (eIF2alpha), one of the known substrates for PKR. We hypothesize that competing heterodimers between p74-K296R PKR and eIF2alpha-K296R PKR may control cell growth such that stabilization of the p74-K296R PKR heterodimer induces abnormal morphology and cell death.
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Registered trials
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