ArticleProceedings of the National Academy of Sciences of the United States of America2007
Eukaryotic RNase P RNA mediates cleavage in the absence of protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 94 papers.
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Who cites it
94 citing papers in PubMed, 184 citations in OpenAlex.
- Stuck on you Giardia.Nature microbiology · 2026Article
- A GTP synthase ribozyme with increased GTP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis for protein-free catalysis by ribonuclease P ribozyme.Nature communications · 2026Article
- Resurrecting the Activity of the RNA Subunit of Human RNase P.Chembiochem : a European journal of chemical biology · 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
- Use of a small molecule microarray screen to identify inhibitors of the catalytic RNA subunit of Methanobrevibacter smithii RNase P.Nucleic acids research · 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
- The West Nile virus genome harbors essential riboregulatory elements with conserved and host-specific functional roles.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Human RNase P exhibits and controls distinct ribonucleolytic activities required for ordered maturation of tRNA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Importance of residue 248 in Escherichia coli RNase P RNA mediated cleavage.Scientific reports · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Human RNase P: overview of a ribonuclease of interrelated molecular networks and gene-targeting systems.RNA (New York, N.Y.) · 2023Review
- Inhibition of lncRNA RPPH1 activity decreases tumor proliferation and metastasis through down-regulation of inflammation-related oncogenes.American journal of translational research · 2023Article
- Hydrophobic-cationic peptides modulate RNA polymerase ribozyme activity by accretion.Nature communications · 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
- Functional Roles of Chelated Magnesium Ions in RNA Folding and Function.Biochemistry · 2021Article
- RNA polymerase III and antiviral innate immune response.Transcription · 2021Review
34 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The universally conserved ribonucleoprotein RNase P is involved in the processing of tRNA precursor transcripts. RNase P consists of one RNA and, depending on its origin, a variable number of protein subunits. Catalytic activity of the RNA moiety so far has been demonstrated only for bacterial and some archaeal RNase P RNAs but not for their eukaryotic counterparts. Here, we show that RNase P RNAs from humans and the lower eukaryote Giardia lamblia mediate cleavage of four tRNA precursors and a model RNA hairpin loop substrate in the absence of protein. Compared with bacterial RNase P RNA, the rate of cleavage (k(obs)) was five to six orders of magnitude lower, whereas the affinity for the substrate (appK(d)) was reduced approximately 20- to 50-fold. We conclude that the RNA-based catalytic activity of RNase P has been preserved during evolution. This finding opens previously undescribed ways to study the role of the different proteins subunits of eukaryotic RNase P.
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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.