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Updated: Aug 10, 2026

Studying RNA Interactors of Protein Kinase RNA-Activated during the Mammalian Cell Cycle
Published on: March 5, 2019
Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA
Yanglong Zhu1, Vilius Stribinskis, Kenneth S Ramos
1Department of Biochemistry and Molecular Biology, and Center for Genetics and Molecular Medicine, School of Medicine, University of Louisville, Kentucky 40202, USA.
Abstract:
RNase MRP is a eukaryote-specific endoribonuclease that generates RNA primers for mitochondrial DNA replication and processes precursor rRNA. RNase P is a ubiquitous endoribonuclease that cleaves precursor tRNA transcripts to produce their mature 5' termini. We found extensive sequence homology of catalytic domains and specificity domains between their RNA subunits in many organisms. In Candida glabrata, the internal loop of helix P3 is 100% conserved between MRP and P RNAs. The helix P8 of MRP RNA from microsporidia Encephalitozoon cuniculi is identical to that of P RNA. Sequence homology can be widely spread over the whole molecule of MRP RNA and P RNA, such as those from Dictyostelium discoideum. These conserved nucleotides between the MRP and P RNAs strongly support the hypothesis that the MRP RNA is derived from the P RNA molecule in early eukaryote evolution.
Insights
RNase P and RNase MRP RNAs share significant sequence homology, suggesting RNase MRP RNA evolved from RNase P RNA in early eukaryotes. This finding impacts our understanding of RNA enzyme evolution.
Area of Science:
- Molecular Biology
- RNA Biology
- Eukaryotic Evolution
Background:
- RNase MRP and RNase P are essential eukaryotic endoribonucleases with distinct functions in RNA processing and DNA replication.
- RNase MRP generates RNA primers for mitochondrial DNA replication and processes precursor ribosomal RNA.
- RNase P produces mature 5' termini of precursor transfer RNA transcripts.
Purpose of the Study:
- To investigate the evolutionary relationship between RNase MRP RNA and RNase P RNA.
- To identify conserved sequence elements and domains between the RNA subunits of RNase MRP and RNase P across various organisms.
Main Methods:
- Comparative sequence analysis of RNase MRP and RNase P RNA subunits.
- Identification and comparison of conserved catalytic and specificity domains.
- Examination of specific conserved nucleotide sequences in key structural regions.
Main Results:
- Extensive sequence homology was observed between the RNA subunits of RNase MRP and RNase P in numerous organisms.
- Specific regions, such as the internal loop of helix P3 in Candida glabrata and helix P8 in Encephalitozoon cuniculi, exhibit high conservation.
- Sequence homology was found to be widespread across the entire molecules in organisms like Dictyostelium discoideum.
Conclusions:
- The extensive and widespread sequence homology strongly supports the hypothesis that RNase MRP RNA is evolutionarily derived from RNase P RNA.
- This finding provides crucial insights into the early evolution of RNA-based enzymes in eukaryotes.
- The conserved elements highlight functional or structural importance in the divergence of these RNA molecules.
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