ArticleThe Journal of biological chemistry2013
The antiprion compound 6-aminophenanthridine inhibits the protein folding activity of the ribosome by direct competition.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- RNA-seq analyses reveal the relevance of RNAs involved in ribosomal complex to induce mammalian prion protein aggregation and phase separationRNA biology · 2025Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- Chaperna: linking the ancient RNA and protein worlds.RNA biology · 2021Review
- Ribosomal RNA Modulates Aggregation of theInternational journal of molecular sciences · 2020Article
- RNA modulates aggregation of the recombinant mammalian prion protein by direct interaction.Scientific reports · 2019Article
- Molecular targets for modulating the protein translation vital to proteostasis and neuron degeneration in Parkinson's disease.Translational neurodegeneration · 2019Review
- Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.The Journal of biological chemistry · 2017Article
- Regulation of PfEMP1-VAR2CSA translation by a Plasmodium translation-enhancing factor.Nature microbiology · 2017Article
- The double life of the ribosome: When its protein folding activity supports prion propagation.Prion · 2017Review
- Sequestration of Ribosome during Protein Aggregate Formation: Contribution of ribosomal RNA.Scientific reports · 2017Article
- Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation.Scientific reports · 2016Article
- Article
- Prion 2016 Oral Abstracts.Prion · 2016Article
- M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.RNA biology · 2015Article
- Review
- G-quadruplexes within prion mRNA: the missing link in prion disease?Nucleic acids research · 2014Article
- Impact of P-Site tRNA and antibiotics on ribosome mediated protein folding: studies using the Escherichia coli ribosome.PloS one · 2014Article
- Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Domain V of the 23S/25S/28S rRNA of the large ribosomal subunit constitutes the active center for the protein folding activity of the ribosome (PFAR). Using in vitro transcribed domain V rRNAs from Escherichia coli and Saccharomyces cerevisiae as the folding modulators and human carbonic anhydrase as a model protein, we demonstrate that PFAR is conserved from prokaryotes to eukaryotes. It was shown previously that 6-aminophenanthridine (6AP), an antiprion compound, inhibits PFAR. Here, using UV cross-linking followed by primer extension, we show that the protein substrates and 6AP interact with a common set of nucleotides on domain V of 23S rRNA. Mutations at the interaction sites decreased PFAR and resulted in loss or change of the binding pattern for both the protein substrates and 6AP. Moreover, kinetic analysis of human carbonic anhydrase refolding showed that 6AP decreased the yield of the refolded protein but did not affect the rate of refolding. Thus, we conclude that 6AP competitively occludes the protein substrates from binding to rRNA and thereby inhibits PFAR. Finally, we propose a scheme clarifying the mechanism by which 6AP inhibits PFAR.
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