ArticleNature communications2020
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Crystal structures of type T archaeal ribonuclease P Rpp30, Rpp30/Pop5, and L7Ae provide insights into a reduced RNase P.Nucleic acids research · 2026Article
- 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
- Molecular characterization of endosomal self RNA Rmrp-engaged TLR3 dimerization to prime innate activation.Cell research · 2025Article
- Exploring GNRA tetraloop-like motifs in nucleic acid 3D structures.Scientific reports · 2025Article
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
- Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components.Cell reports · 2025Article
- RNA Polymerase III-Transcribed RNAs in Health and Disease: Mechanisms, Dysfunction, and Future Directions.International journal of molecular sciences · 2025Review
- Transcriptome-wide RNA accessibility mapping reveals structured RNA elements and pervasive conformational rearrangements under stress.bioRxiv : the preprint server for biology · 2025Article
- The graphene-based affinity cryo-EM grid for the endogenous protein structure determination.bioRxiv : the preprint server for biology · 2025Article
- Molecular determinants of RNase MRP specificity and function.bioRxiv : the preprint server for biology · 2025Article
- RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024Review
- Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes.The Journal of biological chemistry · 2024Review
- TREX reveals proteins that bind to specific RNA regions in living cells.Nature methods · 2024Article
- Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- How does RNA fold dynamically?Journal of molecular biology · 2022Review
- How RNases Shape Mitochondrial Transcriptomes.International journal of molecular sciences · 2022Review
- A disease-linked lncRNA mutation in RNase MRP inhibits ribosome synthesis.Nature communications · 2022Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
RNase MRP is an essential eukaryotic ribonucleoprotein complex involved in the maturation of rRNA and the regulation of the cell cycle. RNase MRP is related to the ribozyme-based RNase P, but it has evolved to have distinct cellular roles. We report a cryo-EM structure of the S. cerevisiae RNase MRP holoenzyme solved to 3.0 Å. We describe the structure of this 450 kDa complex, interactions between its components, and the organization of its catalytic RNA. We show that some of the RNase MRP proteins shared with RNase P undergo an unexpected RNA-driven remodeling that allows them to bind to divergent RNAs. Further, we reveal how this RNA-driven protein remodeling, acting together with the introduction of new auxiliary elements, results in the functional diversification of RNase MRP and its progenitor, RNase P, and demonstrate structural underpinnings of the acquisition of new functions by catalytic RNPs.
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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.