ArticleNucleic acids research2012
Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.
Article in Nucleic acids research, 2012. 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.
- Cartilage-hair hypoplasia: A comprehensive review.Journal of human immunity · 2025Review
- In vitro reconstitution and analysis of eukaryotic RNase P RNPs.Nucleic acids research · 2018Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Detection of RNA-Protein Interactions in Living Cells with SHAPE.Biochemistry · 2015Article
- Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.RNA (New York, N.Y.) · 2015Article
- Uncovering the stoichiometry of Pyrococcus furiosus RNase P, a multi-subunit catalytic ribonucleoprotein complex, by surface-induced dissociation and ion mobility mass spectrometry.Angewandte Chemie (International ed. in English) · 2014Article
- Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
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Authors and funding
5 authors.
Funding
Abstract
Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleoprotein enzymes, which process RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some mRNAs, for RNase MRP. The structures of RNase P and RNase MRP have not yet been solved, so it is unclear how the proteins contribute to the structure of the complexes and how substrate specificity is determined. Using electron microscopy and image processing we show that eukaryotic RNase P and RNase MRP have a modular architecture, where proteins stabilize the RNA fold and contribute to cavities, channels and chambers between the modules. Such features are located at strategic positions for substrate recognition by shape and coordination of the cleaved-off sequence. These are also the sites of greatest difference between RNase P and RNase MRP, highlighting the importance of the adaptation of this region to the different substrates.
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Registered trials
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