henhaobio
Sign in

bioRxivMolecular BiologyPreprint

Molecular determinants of RNase MRP specificity and function

Eric M. SmithiD, Jimmy LyiD, Sofia Haug, Iain M. CheesemaniD

PDFDOI

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 protein, C18orf21/RMRPP1. RMRPP1 and Rpp21 display significant structural homology, but we identify specific regions that drive interactions with their respective complexes. Additionally, we reveal that RNase MRP is required for 40S, but not 60S, ribosome biogenesis uncovering an alternative pathway for ribosome assembly. Finally, we identify Nepro as an essential rRNA processing factor that associates with the RNase MRP complex. Together, our findings elucidate the molecular determinants of RNase MRP function and underscore its critical role in ribosome biogenesis.

Citations
2

Reproducibility ledger

Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.

Sign in to file a reproducibility report.

Similarity Map
SelectedSame fieldCross-field
THISLiu '25Che '25Perederina '20Liu '19Best '22Liao '22
83% semantic matchMolecular Biology
Yuan Liu, Shiyang He, Kawon Pyo+7 more·Nucleic Acids Research·Aug 8, 2025· 7 citations