ArticleNucleic acids research2018
In vitro reconstitution and analysis of eukaryotic RNase P RNPs.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Structural basis for protein-free catalysis by ribonuclease P ribozyme.Nature communications · 2026Article
- Divergent molecular assembly and catalytic mechanisms between bacterial and archaeal RNase P in pre-tRNA cleavage.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P.RNA biology · 2023Article
- Elucidation of structure-function relationships in Methanocaldococcus jannaschii RNase P, a multi-subunit catalytic ribonucleoprotein.Nucleic acids research · 2022Article
- The many faces of RNA-based RNase P, an RNA-world relic.Trends in biochemical sciences · 2021Review
- Protein cofactors and substrate influence Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P.Nucleic acids research · 2021Article
- Analysis of Tagged Proteins Using Tandem Affinity-Buffer Exchange Chromatography Online with Native Mass Spectrometry.Biochemistry · 2021Article
- Analysis of RNA-protein networks with RNP-MaP defines functional hubs on RNA.Nature biotechnology · 2021Article
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme.Methods in enzymology · 2021Article
- Exploring the Complexity of Protein-Level Dosage Compensation that Fine-Tunes Stoichiometry of Multiprotein Complexes.PLoS genetics · 2020Article
- Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.Nature communications · 2020Article
- Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP.Nature communications · 2020Article
- Biogenesis of RNase P RNA from an intron requires co-assembly with cognate protein subunits.Nucleic acids research · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RNase P is a ubiquitous site-specific endoribonuclease primarily responsible for the maturation of tRNA. Throughout the three domains of life, the canonical form of RNase P is a ribonucleoprotein (RNP) built around a catalytic RNA. The core RNA is well conserved from bacteria to eukaryotes, whereas the protein parts vary significantly. The most complex and the least understood form of RNase P is found in eukaryotes, where multiple essential proteins playing largely unknown roles constitute the bulk of the enzyme. Eukaryotic RNase P was considered intractable to in vitro reconstitution, mostly due to insolubility of its protein components, which hindered its studies. We have developed a robust approach to the in vitro reconstitution of Saccharomyces cerevisiae RNase P RNPs and used it to analyze the interplay and roles of RNase P components. The results eliminate the major obstacle to biochemical and structural studies of eukaryotic RNase P, identify components required for the activation of the catalytic RNA, reveal roles of proteins in the enzyme stability, localize proteins on RNase P RNA, and demonstrate the interdependence of the binding of RNase P protein modules to the core RNA.
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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.