ArticleRNA biology2013
RNase P enzymes: divergent scaffolds for a conserved biological reaction.
Article in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
26 citing papers in PubMed, 37 citations in OpenAlex.
- Constructing Drive-and-Process (DAP) CRISPR Guide RNA Arrays for Multiplexed Base- and Prime-Editing.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Article
- RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024Review
- RNA Epigenetics in Chronic Lung Diseases.Genes · 2022Review
- Disease-associated mutations in mitochondrial precursor tRNAs affect binding, m1R9 methylation, and tRNA processing by mtRNase P.RNA (New York, N.Y.) · 2021Article
- RNA modifications and cancer.RNA biology · 2020Review
- Interplay between substrate recognition, 5' end tRNA processing and methylation activity of human mitochondrial RNase P.RNA (New York, N.Y.) · 2019Article
- Both kinds of RNase P in all domains of life: surprises galore.RNA (New York, N.Y.) · 2019Article
- Distributive enzyme binding controlled by local RNA context results in 3' to 5' directional processing of dicistronic tRNA precursors by Escherichia coli ribonuclease P.Nucleic acids research · 2019Article
- Biochemical Studies Provide Insights into the Necessity for Multiple Arabidopsis thaliana Protein-Only RNase P Isoenzymes.Journal of molecular biology · 2019Article
- TheRNA (New York, N.Y.) · 2018Article
- Structural insight into the human mitochondrial tRNA purine N1-methyltransferase and ribonuclease P complexes.The Journal of biological chemistry · 2018Article
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Molecular recognition of pre-tRNA byRNA (New York, N.Y.) · 2017Article
- Use of chemical modification and mass spectrometry to identify substrate-contacting sites in proteinaceous RNase P, a tRNA processing enzyme.Nucleic acids research · 2016Article
- The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions.Biomolecules · 2016Review
- Differential substrate recognition by isozymes of plant protein-only Ribonuclease P.RNA (New York, N.Y.) · 2016Article
- Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.Nucleic acids research · 2016Article
- Nuclear Protein-Only Ribonuclease P2 Structure and Biochemical Characterization Provide Insight into the Conserved Properties of tRNA 5' End Processing Enzymes.Journal of molecular biology · 2016Article
- Mechanistic Studies Reveal Similar Catalytic Strategies for Phosphodiester Bond Hydrolysis by Protein-only and RNA-dependent Ribonuclease P.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Ribonuclease P (RNase P) catalyzes the maturation of the 5' end of precursor-tRNAs (pre-tRNA) and is conserved in all domains of life. However, the composition of RNase P varies from bacteria to archaea and eukarya, making RNase P one of the most diverse enzymes characterized. Most known RNase P enzymes contain a large catalytic RNA subunit that associates with one to 10 proteins. Recently, a protein-only form of RNase P was discovered in mitochondria and chloroplasts of many higher eukaryotes. This proteinaceous RNase P (PRORP) represents a new class of metallonucleases. Here we discuss our recent crystal structure of PRORP1 from Arabidopsis thaliana and speculate on the reasons for the replacement of catalytic RNA by a protein catalyst. We conclude, based on an analysis of the catalytic efficiencies of ribonucleoprotein (RNP) and PRORP enzymes, that the need for greater catalytic efficiency is most likely not the driving force behind the replacement of the RNA with a protein catalyst. The emergence of a protein-based RNase P more likely reflects the increasing complexity of the biological system, including difficulties in importation into organelles and vulnerability of organellar RNAs to cleavage.
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What OpenQuestion holds
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.