ArticleNature structural & molecular biology2026
RNase MRP subunit composition and role in 40S ribosome biogenesis.
Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Updated guide to RNA quantification by RNA sequencing and reverse transcription-qPCR.Molecules and cells · 2026Article
- 5' UTR length shapes alternative N-terminal protein isoforms across cancers and in rare disease.EMBO reports · 2026Article
- Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex.Nature communications · 2026Article
- 5' UTR length regulates alternative N-terminal protein isoform production in health and disease.bioRxiv : the preprint server for biology · 2026Article
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4 authors.
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Abstract
RNase MRP and RNase P are evolutionarily related complexes that facilitate rRNA and tRNA biogenesis, respectively. The two enzymes share nearly all protein subunits and have evolutionarily related catalytic RNAs. Notably, RNase P includes a unique subunit, RPP21, whereas no RNase MRP-specific proteins have been found in humans, limiting molecular analyses of RNase MRP function. Here, we identify the RNase MRP-specific proteins, C18orf21 (RMP24) and NEPRO (RMP64). C18orf21/RMP24 and RPP21 display significant structural homology, but we identify specific regions that drive interactions with their respective complexes. By targeting these RNase MRP-specific subunits, our functional analysis reveals that RNase MRP is essential for rRNA processing and preferentially required for 40S ribosome biogenesis. Finally, we determine that disease-associated mutations in RMP64 impair its association with RNase MRP subunits. Together, our findings elucidate the molecular determinants of RNase MRP function and underscore its critical role in ribosome biogenesis and disease.
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