ArticleRNA (New York, N.Y.)2009
RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway.
Article in RNA (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 57 citations in OpenAlex.
- Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex.Nature communications · 2026Article
- RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026Article
- Screening for non-invasive rsRNA biomarkers to assess embryo quality utilizing ultra-sensitive pandora sequencing combined with machine learning.Journal of assisted reproduction and genetics · 2025Article
- High resolution landscape of ribosomal RNA processing and surveillance.Nucleic acids research · 2024Article
- The novel pre-rRNA detection workflow "Riboprobing" allows simple identification of undescribed RNA species.RNA (New York, N.Y.) · 2024Article
- Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes.The Journal of biological chemistry · 2024Review
- RNA Polymerases I and III in development and disease.Seminars in cell & developmental biology · 2023Review
- Maize Shrek1 encodes a WD40 protein that regulates pre-rRNA processing in ribosome biogenesis.The Plant cell · 2022Article
- Increasing Complexity of Ribosomes and Their Biogenesis.International journal of molecular sciences · 2022Article
- A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA.International journal of molecular sciences · 2021Article
- Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.Nature communications · 2020Article
- The small and large ribosomal subunits depend on each other for stability and accumulation.Life science alliance · 2019Article
- Small Non-Coding RNAs Derived From Eukaryotic Ribosomal RNA.Non-coding RNA · 2019Review
- tRNA Processing and Subcellular Trafficking Proteins Multitask in Pathways for Other RNAs.Frontiers in genetics · 2019Review
- Trypanosoma brucei RRP44 is involved in an early stage of large ribosomal subunit RNA maturation.RNA biology · 2019Article
- The Yeast DNA Damage Checkpoint Kinase Rad53 Targets the Exoribonuclease, Xrn1.G3 (Bethesda, Md.) · 2018Article
- Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing.Genes & development · 2017Article
- Hypo- and Hyper-Assembly Diseases of RNA-Protein Complexes.Trends in molecular medicine · 2016Review
- Splicing-Mediated Autoregulation Modulates Rpl22p Expression in Saccharomyces cerevisiae.PLoS genetics · 2016Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase MRP is a nucleolar RNA-protein enzyme that participates in the processing of rRNA during ribosome biogenesis. Previous experiments suggested that RNase MRP makes a nonessential cleavage in the first internal transcribed spacer. Here we report experiments with new temperature-sensitive RNase MRP mutants in Saccharomyces cerevisiae that show that the abundance of all early intermediates in the processing pathway is severely reduced upon inactivation of RNase MRP. Transcription of rRNA continues unabated as determined by RNA polymerase run-on transcription, but the precursor rRNA transcript does not accumulate, and appears to be unstable. Taken together, these observations suggest that inactivation of RNase MRP blocks cleavage at sites A0, A1, A2, and A3, which in turn, prevents precursor rRNA from entering the canonical processing pathway (35S > 20S + 27S > 18S + 25S + 5.8S rRNA). Nevertheless, at least some cleavage at the processing site in the second internal transcribed spacer takes place to form an unusual 24S intermediate, suggesting that cleavage at C2 is not blocked. Furthermore, the long form of 5.8S rRNA is made in the absence of RNase MRP activity, but only in the presence of Xrn1p (exonuclease 1), an enzyme not required for the canonical pathway. We conclude that RNase MRP is a key enzyme for initiating the canonical processing of precursor rRNA transcripts, but alternative pathway(s) might provide a backup for production of small amounts of rRNA.
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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.