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Updated: Jul 13, 2026

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
Published on: September 21, 2017
A view of RNase P.
1Department of Molecular, Cellular and Developmental Biology, Yale University, 266 Whitney Avenue, CT 06511, USA. sidney.altman@yale.edu
Ribonuclease P (RNase P) studies show bacterial catalytic subunits via crystallography and eukaryotic catalytic activity. New substrates in bacteria and yeast highlight an "RNA-protein world" over a "protein world".
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Ribonuclease P (RNase P) is crucial for tRNA maturation.
- Understanding RNase P's catalytic mechanisms is key to cellular processes.
- Recent advances have shed light on its diverse roles.
Purpose of the Study:
- To review major progress in RNase P research.
- To highlight advances in understanding RNase P's structure and function.
- To discuss the implications of new findings for molecular biology.
Main Methods:
- Crystallographic studies of bacterial RNase P catalytic subunits.
- Biochemical assays to identify eukaryotic RNase P catalytic activity.
- Substrate identification studies in bacteria and yeast.
Main Results:
- Crystallography elucidated the structure of bacterial RNase P catalytic subunits.
- Catalytic activity of RNase P was discovered in eukaryotes.
- Novel substrates for RNase P were identified in bacteria and yeast.
Conclusions:
- RNase P is a ribozyme with significant roles in both prokaryotes and eukaryotes.
- The discovery of eukaryotic catalytic activity expands our understanding of RNA-based catalysis.
- Current biological systems represent an
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