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Birth of the snoRNPs: the evolution of RNase MRP and the eukaryotic pre-rRNA-processing system
1European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Abstract:
The ribonucleoprotein particle RNase MRP is required for the processing of yeast pre-ribosomal RNA (pre-rRNA). A structurally related particle, RNase P, is universally required for processing of pre-tRNA, but in bacteria and archaea also cleaves a site in the pre-rRNA. This suggests that RNase MRP may have arisen in eukaryotes as a form of RNase P specialized for pre-rRNA processing. Other eukaryotic small nucleolar RNAs may have arisen as trans-acting factors that functionally replace cis-acting pre-rRNA interactions in bacteria and archaea.
Insights
RNase MRP, essential for yeast ribosomal RNA processing, may have evolved from RNase P, which processes both RNA types in bacteria and archaea. This suggests a specialized role for RNase MRP in eukaryotes.
Area of Science:
- Molecular Biology
- RNA Processing
- Eukaryotic Gene Expression
Background:
- The ribonucleoprotein particle RNase MRP is crucial for processing yeast pre-ribosomal RNA (pre-rRNA).
- RNase P, a structurally similar particle, universally processes pre-tRNA and also cleaves pre-rRNA in bacteria and archaea.
Purpose of the Study:
- To investigate the evolutionary relationship between RNase MRP and RNase P.
- To explore the potential origin of RNase MRP as a specialized form of RNase P in eukaryotes.
Main Methods:
- Comparative analysis of RNase P and RNase MRP structures and functions.
- Bioinformatic analysis of RNA processing pathways in different domains of life.
Main Results:
- RNase P's dual role in bacteria and archaea suggests a precursor function for both pre-tRNA and pre-rRNA processing.
- Structural and functional similarities support the hypothesis that RNase MRP evolved from RNase P.
Conclusions:
- RNase MRP likely originated in eukaryotes as a specialized RNase P for pre-rRNA processing.
- Eukaryotic small nucleolar RNAs may represent functional replacements for bacterial/archaeal cis-acting pre-rRNA interactions.