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RNase P--a 'Scarlet Pimpernel'
1Department of Microbiology, Biomedical Centre, Uppsala, Sweden.
Molecular Microbiology
|August 1, 1995
Summary
The catalytic subunit of Escherichia coli RNase P (M1 RNA) and its protein subunit (C5) select tRNA cleavage sites. Watson-Crick base-pairing with the precursor
Area of Science:
- Molecular Biology
- Biochemistry
- Enzymology
Background:
- Ribonuclease P (RNase P) is essential for tRNA 5' end maturation.
- RNase P must accurately recognize diverse precursor molecules.
- Understanding cleavage-site selection is key to RNase P function.
Purpose of the Study:
- To review current knowledge on Escherichia coli RNase P (M1 RNA and C5) in cleavage-site selection.
- To elucidate the mechanism of substrate recognition and cleavage site exposure.
Main Methods:
- Genetic analysis
- Biochemical assays
- Structural modeling of M1 RNA-substrate complexes
Main Results:
- Watson-Crick base-pairing between precursor CCA and enzyme identifies cleavage sites.
- This interaction promotes unfolding of the amino acid acceptor stem.
- Additional M1 RNA-substrate contact points have been identified.
Conclusions:
- A mechanistic model for RNase P cleavage site selection is emerging.
- Structural data provide a foundation for understanding the catalytic mechanism.
- Further research will clarify the function of M1 RNA and C5 subunits.