RNase MRP subunit composition and role in 40S ribosome biogenesis

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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Publication Details

Journal
Nature Structural & Molecular Biology
Published
2025-10-24
DOI
https://doi.org/10.1038/s41594-025-01690-7
Citations
2
Primary Topic
RNA and protein synthesis mechanisms
Type
article
Field-Weighted Citation Impact
1.61
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article

RNase MRP subunit composition and role in 40S ribosome biogenesis

Jimmy Ly, Iain M. Cheeseman, Eric M. Smith, S. Haug
2 citations
Nature Structural & Molecular Biology
RNA and protein synthesis mechanisms
1.61
article

RNase MRP subunit composition and role in 40S ribosome biogenesis

Jimmy Ly, Iain M. Cheeseman, Eric M. Smith, S. Haug
article en
2 citations

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.

Nature Structural & Molecular BiologyVol. 33(1)
Whitehead Institute for Biomedical Research (US), Massachusetts Institute of Technology (US)
Openalex Percentile: Top 14%
RNA and protein synthesis mechanisms
1.61
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