ArticleCell reports2025
Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components.
Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- TRNAU1AP and PRPF39 establish integrated control over processing of most abundant human non-coding RNAs.Nature communications · 2026Article
- Structural and evolutionary insights into the eukaryotic RNase MRP ribonucleoprotein complex.Nature communications · 2026Article
- Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus.Molecular cell · 2026Review
- RNase MRP subunit composition and role in 40S ribosome biogenesis.Nature structural & molecular biology · 2026Article
- Cartilage-hair hypoplasia: A comprehensive review.Journal of human immunity · 2025Review
- Composition and RNA binding specificity of metazoan RNase MRP.Nucleic acids research · 2025Article
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6 authors.
Funding
Abstract
Human RNase MRP is a ribonucleoprotein (RNP) enzyme that processes precursor rRNA (pre-rRNA) at ITS1 site 2 and may have additional activities. It is an endonuclease related to RNase P, which processes pre-tRNAs and pre-tRNA-like substrates. In Saccharomyces cerevisiae, these two RNPs utilize distinct catalytic RNAs with eight shared and one or two specific protein subunits. However, the human RNase MRP-specific protein subunits remain unidentified. Our genome-wide forward genetic screening identifies two poorly characterized human genes, which we name ribonuclease MRP subunit P24 (RMP24) and RMP64. We show that Rmp24 and Rmp64 are required for pre-rRNA ITS1 site 2 processing and associate with MRP RNA but are not required for RNase P activity and do not associate with RNase P-specific H1 RNA. Despite limited sequence homology, Rmp24 and Rmp64 exhibit predicted structural similarities to two RNase MRP-specific components in S. cerevisiae. Collectively, our functional screening and validation reveal two protein components unique to human nuclear RNase MRP.
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