ArticleRNA (New York, N.Y.)2010
Comparison of mitochondrial and nucleolar RNase MRP reveals identical RNA components with distinct enzymatic activities and protein components.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 37 citations in OpenAlex.
- Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus.Molecular cell · 2026Review
- Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components.Cell reports · 2025Article
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- Post-transcriptional diversity in riboproteins and RNAs in aging and cancer.Seminars in cancer biology · 2021Review
- Non-coding RNA Regulated Cross-Talk Between Mitochondria and Other Cellular Compartments.Frontiers in cell and developmental biology · 2021Review
- Chance and necessity in the evolution of RNase P.RNA (New York, N.Y.) · 2018Article
- Non-coding RNAs: the dark side of nuclear-mitochondrial communication.The EMBO journal · 2017Review
- Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.RNA (New York, N.Y.) · 2015Article
- The dichotomy of p53 regulation by noncoding RNAs.Journal of molecular cell biology · 2014Review
- The impairment of MAGMAS function in human is responsible for a severe skeletal dysplasia.PLoS genetics · 2014Article
- Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
- Global identification of new substrates for the yeast endoribonuclease, RNase mitochondrial RNA processing (MRP).The Journal of biological chemistry · 2012Article
- Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.RNA (New York, N.Y.) · 2012Article
- Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNA (New York, N.Y.) · 2011Article
- Binding and cleavage of unstructured RNA by nuclear RNase P.RNA (New York, N.Y.) · 2011Article
- Substrate recognition by ribonucleoprotein ribonuclease MRP.RNA (New York, N.Y.) · 2011Article
- Role of RNase MRP in viral RNA degradation and RNA recombination.Journal of virology · 2011Article
- Archaeal/eukaryal RNase P: subunits, functions and RNA diversification.Nucleic acids research · 2010Review
- Functional characterization of the Drosophila MRP (mitochondrial RNA processing) RNA gene.RNA (New York, N.Y.) · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RNase MRP is a ribonucleoprotein endoribonuclease found in three cellular locations where distinct substrates are processed: the mitochondria, the nucleolus, and the cytoplasm. Cytoplasmic RNase MRP is the nucleolar enzyme that is transiently relocalized during mitosis. Nucleolar RNase MRP (NuMRP) was purified to homogeneity, and we extensively purified the mitochondrial RNase MRP (MtMRP) to a single RNA component identical to the NuMRP RNA. Although the protein components of the NuMRP were identified by mass spectrometry successfully, none of the known NuMRP proteins were found in the MtMRP preparation. Only trace amounts of the core NuMRP protein, Pop4, were detected in MtMRP by Western blot. In vitro activity of the two enzymes was compared. MtMRP cleaved only mitochondrial ORI5 substrate, while NuMRP cleaved all three substrates. However, the NuMRP enzyme cleaved the ORI5 substrate at sites different than the MtMRP enzyme. In addition, enzymatic differences in preferred ionic strength confirm these enzymes as distinct entities. Magnesium was found to be essential to both enzymes. We tested a number of reported inhibitors including puromycin, pentamidine, lithium, and pAp. Puromycin inhibition suggested that it binds directly to the MRP RNA, reaffirming the role of the RNA component in catalysis. In conclusion, our study confirms that the NuMRP and MtMRP enzymes are distinct entities with differing activities and protein components but a common RNA subunit, suggesting that the RNA must be playing a crucial role in catalytic activity.
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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.