ArticleNucleic acids research2016
Substrate recognition and cleavage-site selection by a single-subunit protein-only RNase P.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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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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Who cites it
27 citing papers in PubMed, 38 citations in OpenAlex.
- 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
- Substrate and enzyme determinants for recognition by human mitochondrial RNase P.Nucleic acids research · 2025Article
- Bacterial/archaeal protein-only RNase P: complementation inRNA (New York, N.Y.) · 2025Article
- Mitochondrial protein synthesis quality control.Human molecular genetics · 2024Review
- Discovery, structure, mechanisms, and evolution of protein-only RNase P enzymes.The Journal of biological chemistry · 2024Review
- tRFUniverse: A comprehensive resource for the interactive analyses of tRNA-derived ncRNAs in human cancer.iScience · 2024Article
- A tRNA-modifying enzyme facilitates RNase P activity in Arabidopsis nuclei.Nature plants · 2023Article
- Cleavage kinetics of human mitochondrial RNase P and contribution of its non-nuclease subunits.Nucleic acids research · 2023Article
- Importance of residue 248 in Escherichia coli RNase P RNA mediated cleavage.Scientific reports · 2023Article
- Mitochondrion-targeted RNA therapies as a potential treatment strategy for mitochondrial diseases.Molecular therapy. Nucleic acids · 2022Review
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- Synthetic riboswitches for the analysis of tRNA processing by eukaryotic RNase P enzymes.RNA (New York, N.Y.) · 2022Article
- Structural basis of RNA processing by human mitochondrial RNase P.Nature structural & molecular biology · 2021Article
- Article
- Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA.Nucleic acids research · 2020Article
- Interplay between substrate recognition, 5' end tRNA processing and methylation activity of human mitochondrial RNase P.RNA (New York, N.Y.) · 2019Article
- Identification of tRNA-derived ncRNAs in TCGA and NCI-60 panel cell lines and development of the public database tRFexplorer.Database : the journal of biological databases and curation · 2019Article
- An RNase P-Based Assay for Accurate Determination of the 5'-Deoxy-5'-azidoguanosine-Modified Fraction of in Vitro-Transcribed RNAs.Chembiochem : a European journal of chemical biology · 2018Article
- Genetic editing and interrogation with Cpf1 and caged truncated pre-tRNA-like crRNA in mammalian cells.Cell discovery · 2018Article
- Molecular recognition of pre-tRNA byRNA (New York, N.Y.) · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
RNase P is the enzyme that removes 5' extensions from tRNA precursors. With its diversity of enzyme forms-either protein- or RNA-based, ranging from single polypeptides to multi-subunit ribonucleoproteins-the RNase P enzyme family represents a unique model system to compare the evolution of enzymatic mechanisms. Here we present a comprehensive study of substrate recognition and cleavage-site selection by the nuclear single-subunit proteinaceous RNase P PRORP3 from Arabidopsis thaliana. Compared to bacterial RNase P, the best-characterized RNA-based enzyme form, PRORP3 requires a larger part of intact tRNA structure, but little to no determinants at the cleavage site or interactions with the 5' or 3' extensions of the tRNA. The cleavage site depends on the combined dimensions of acceptor stem and T domain, but also requires the leader to be single-stranded. Overall, the single-subunit PRORP appears mechanistically more similar to the complex nuclear ribonucleoprotein enzymes than to the simpler bacterial RNase P. Mechanistic similarity or dissimilarity among different forms of RNase P thus apparently do not necessarily reflect molecular composition or evolutionary relationship.
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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.