ArticleNucleic acids research2025
Composition and RNA binding specificity of metazoan RNase MRP.
Article in Nucleic acids research, 2025. 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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4 citing papers in PubMed.
- R-loop disruption triggers irreversible topoisomerase 1-DNA cleavage complex formation during AID-dependent IgH gene diversification.Proceedings of the National Academy of Sciences of the United States of America · 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
- Next-generation RNA sequencing of spatially mapped material from human body donors for testing the impact of fetal environments on the liver transcriptome.Scientific reports · 2025Article
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10 authors.
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Abstract
Ribonuclease (RNase) MRP is a conserved RNA-based enzyme best known for its essential role in the maturation of ribosomal RNA (rRNA) in eukaryotes. However, the composition and RNA substrate specificity of this multisubunit ribonucleoprotein complex in higher eukaryotes remain a mystery. Here, we identify NEPRO and C18ORF21 (which we renamed RMP64 and RMP24, respectively) as constitutive subunits of metazoan RNase MRP. These proteins are unique to RNase MRP and absent from the closely related RNase P, which processes transfer RNA (tRNA) precursors and tRNA-like substrates. We find that RMP64 and RMP24 are integral subunits of RNase MRP, stabilize its catalytic RNA, and are required for rRNA maturation and cell proliferation. Leveraging these discoveries, we identify a broad suite of in vivo RNA-binding targets of each enzyme, including potential cleavage sites at nucleotide resolution. Our findings identify the first metazoan RNase MRP-specific protein subunits and define the RNA-targeting repertoire of this essential enzyme in mammalian cells.
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