ArticleProceedings of the National Academy of Sciences of the United States of America2006
Functional reconstitution and characterization of Pyrococcus furiosus RNase P.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 95 citations in OpenAlex.
- Crystal structures of type T archaeal ribonuclease P Rpp30, Rpp30/Pop5, and L7Ae provide insights into a reduced RNase P.Nucleic acids research · 2026Article
- Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025Review
- RNase P cleavage of pseudoknot substrates reveals differences in active site architecture that depend on residue N-1 in the 5' leader.RNA biology · 2025Article
- Comprehensive datasets for RNA design, machine learning, and beyond.Scientific reports · 2025Article
- 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
- RNAs undergo phase transitions with lower critical solution temperatures.Nature chemistry · 2023Article
- Importance of residue 248 in Escherichia coli RNase P RNA mediated cleavage.Scientific reports · 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
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- Protein cofactors and substrate influence Mg2+-dependent structural changes in the catalytic RNA of archaeal RNase P.Nucleic acids research · 2021Article
- RNA polymerase III and antiviral innate immune response.Transcription · 2021Review
- Purification, reconstitution, and mass analysis of archaeal RNase P, a multisubunit ribonucleoprotein enzyme.Methods in enzymology · 2021Article
- Piece by piece: Building a ribozyme.The Journal of biological chemistry · 2020Review
- Biogenesis of RNase P RNA from an intron requires co-assembly with cognate protein subunits.Nucleic acids research · 2019Article
- Cryo-electron microscopy structure of an archaeal ribonuclease P holoenzyme.Nature communications · 2019Article
- rPredictorDB: a predictive database of individual secondary structures of RNAs and their formatted plots.Database : the journal of biological databases and curation · 2019Article
- In vitro reconstitution and analysis of eukaryotic RNase P RNPs.Nucleic acids research · 2018Article
- Critical domain interactions for type A RNase P RNA catalysis with and without the specificity domain.PloS one · 2018Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
RNase P, which catalyzes the magnesium-dependent 5'-end maturation of tRNAs in all three domains of life, is composed of one essential RNA and a varying number of protein subunits depending on the source: at least one in bacteria, four in archaea, and nine in eukarya. To address why multiple protein subunits are needed for archaeal/eukaryal RNase P catalysis, in contrast to their bacterial relative, in vitro reconstitution of these holoenzymes is a prerequisite. Using recombinant subunits, we have reconstituted in vitro the RNase P holoenzyme from the thermophilic archaeon Pyrococcus furiosus (Pfu) and furthered our understanding regarding its functional organization and assembly pathway(s). Whereas Pfu RNase P RNA (RPR) alone is capable of multiple turnover, addition of all four RNase P protein (Rpp) subunits to Pfu RPR results in a 25-fold increase in its k(cat) and a 170-fold decrease in K(m). In fact, even in the presence of only one of two specific pairs of Rpps, the RPR displays activity at lower substrate and magnesium concentrations. Moreover, a pared-down, mini-Pfu RNase P was identified with an RPR deletion mutant. Results from our kinetic and footprinting studies on Pfu RNase P, together with insights from recent structures of bacterial RPRs, provide a framework for appreciating the role of multiple Rpps in archaeal RNase P.
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