ArticleNucleic acids research2009
The PKR-binding domain of adenovirus VA RNAI exists as a mixture of two functionally non-equivalent structures.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Differential assembly of RNP granules via activation of distinct dsRNA sensors by adenovirus mutants.PLoS pathogens · 2026Article
- Differential assembly of RNP granules via activation of distinct dsRNA sensors by adenovirus mutants.bioRxiv : the preprint server for biology · 2026Article
- Review
- Crystal structure of an adenovirus virus-associated RNA.Nature communications · 2019Article
- The search for a PKR code-differential regulation of protein kinase R activity by diverse RNA and protein regulators.RNA (New York, N.Y.) · 2019Review
- PKR: A Kinase to Remember.Frontiers in molecular neuroscience · 2018Review
- Impact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition.PloS one · 2017Article
- Structural analysis of adenovirus VAI RNA defines the mechanism of inhibition of PKR.Biophysical journal · 2015Article
- Identification of RISC-associated adenoviral microRNAs, a subset of their direct targets, and global changes in the targetome upon lytic adenovirus 5 infection.Journal of virology · 2015Article
- Conserved sequence-specific lincRNA-steroid receptor interactions drive transcriptional repression and direct cell fate.Nature communications · 2014Article
- Dissection of the adenoviral VA RNAI central domain structure reveals minimum requirements for RNA-mediated inhibition of PKR.The Journal of biological chemistry · 2014Article
- Domain interactions in adenovirus VAI RNA mediate high-affinity PKR binding.Journal of molecular biology · 2014Article
- Long non-coding RNAs (lncRNAs) and viral infections.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2013Article
- Article
- Regulation of innate immunity through RNA structure and the protein kinase PKR.Current opinion in structural biology · 2011Review
- Analysis of PKR activation using analytical ultracentrifugation.Macromolecular bioscience · 2010Article
- Adenovirus and miRNAs.Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
VA RNA(I) is a non-coding adenoviral transcript that counteracts the host cell anti-viral defenses such as immune responses mediated via PKR. We investigated potential alternate secondary structure conformations within the PKR-binding domain of VA RNA(I) using site-directed mutagenesis, RNA UV-melting analysis and enzymatic RNA secondary structure probing. The latter data clearly indicated that the wild-type VA RNA(I) apical stem can adopt two different conformations and that it exists as a mixed population of these two structures. In contrast, in two sequence variants we designed to eliminate one of the possible structures, while leaving the other intact, each formed a unique secondary structure. This clarification of the apical stem pairing also suggests a small alteration to the apical stem-loop secondary structure. The relative ability of the two apical stem conformations to bind PKR and inhibit kinase activity was measured by isothermal titration calorimetry and PKR autophosphorylation inhibition assay. We found that the two sequence variants displayed markedly different activities, with one being a significantly poorer binder and inhibitor of PKR. Whether the presence of the VA RNA(I) conformation with reduced PKR inhibitory activity is directly beneficial to the virus in the cell for some other function requires further investigation.
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Registered trials
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.