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Updated: Aug 2, 2025

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Proteins Rpr2 and Pop3 increase the activity and thermal stability of yeast RNase P
Anna Perederina1, Igor Berezin1, Andrey S Krasilnikov1
1Department of Biochemistry and Molecular Biology, Center for RNA Biology, Pennsylvania State University, University Park, PA, USA.
Abstract:
RNA-based enzyme RNase P is a ribonucleoprotein complex responsible primarily for 5'-maturation of tRNAs. S. cerevisiae RNase P comprises a catalytic RNA component and nine proteins. The assembly and maturation of S. cerevisiae RNase P involves an abundant and catalytically active precursor form, which includes all components except for proteins Rpr2 and Pop3. Rpr2 and Pop3 are essential proteins, but their roles in RNase P were not clear. Here we use a step-wise in vitro assembly of yeast RNase P to show that the addition of proteins Rpr2 and Pop3 increases the activity and thermal stability of the RNase P complex, similar to the effects previously observed for archaeal RNases P.
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