ReviewRNA biology
RNase P: increased versatility through protein complexity?
Review in RNA biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Three-metal-ion catalysis by ribonuclease P holoenzyme: a new mechanistic insight into transfer RNA maturation.Research square · 2026Article
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
- The conformational space of RNase P RNA in solution.Nature · 2025Article
- Article
- Determining structures of individual RNA conformers using atomic force microscopy images and deep neural networks.Research square · 2023Article
- Identification of theFrontiers in microbiology · 2018Article
- External guide sequence technology: a path to development of novel antimicrobial therapeutics.Annals of the New York Academy of Sciences · 2015Review
- Playing RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme forms.PLoS genetics · 2014Article
- Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
- PPR proteins shed a new light on RNase P biology.RNA biology · 2013Review
- RNase MRP RNA and RNase P activity in plants are associated with a Pop1p containing complex.Nucleic acids research · 2012Article
- Nuclear RNase P of Trypanosoma brucei: a single protein in place of the multicomponent RNA-protein complex.Cell reports · 2012Article
- Fidelity of tRNA 5'-maturation: a possible basis for the functional dependence of archaeal and eukaryal RNase P on multiple protein cofactors.Nucleic acids research · 2012Article
- A two-piece derivative of a group I intron RNA as a platform for designing self-assembling RNA templates to promote Peptide ligation.Journal of nucleic acids · 2012Article
- Solution structure of RNase P RNA.RNA (New York, N.Y.) · 2011Article
- Unexpected diversity of RNase P, an ancient tRNA processing enzyme: challenges and prospects.FEBS letters · 2010Review
- An overview of RNAs with regulatory functions in gram-positive bacteria.Cellular and molecular life sciences : CMLS · 2010Review
- Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Ribonuclease P (RNase P) is an essential enzyme that catalyzes the 5' endonucleolytic cleavage of precursor transfer RNAs (pretRNAs). It is found in all phylogenetic domains: bacteria, archaea and eukaryotes. The bacterial enzyme consists of a single, catalytic RNA subunit and one small protein, while the archaeal and eukaryotic enzymes have 4-10 proteins in addition to a similar RNA subunit. The bacterial RNA acts as a ribozyme at high salt in vitro; however the added protein optimizes kinetics and makes specific contacts with the pre-tRNA substrate. The bacterial protein subunit also appears to be required for the processing of non-tRNA substrates by broadening recognition tolerance. In addition, the immense increase in protein content in the eukaryotic enzymes suggests substantially enlarged capacity for recognition of additional substrates. Recently intron-encoded box C/D snoRNAs were shown to be likely substrates for RNase P, with several lines of evidence suggesting that the nuclear holoenzyme binds tightly to, and can cleave single-stranded RNA in a sequence dependent fashion. The possible involvement of RNase P in additional RNA processing or turnover pathways would be consistent with previous findings that RNase MRP, a variant of RNase P that has evolved to participate in ribosomal RNA processing, is also involved in turnover of specific messenger RNAs. Here, involvement of RNase P in multiple RNA processing pathways is discussed.
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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.