PMID:10652227
| Citation |
Park, BH, Lee, JH, Kim, M and Lee, Y (2000) Effects of C5 protein on Escherichia coli RNase P catalysis with a precursor tRNA(Phe) bearing a single mismatch in the acceptor stem. Biochem. Biophys. Res. Commun. 268:136-40 |
|---|---|
| Abstract |
Escherichia coli RNase P, an RNA-processing enzyme that cleaves precursor tRNAs to generate the mature 5'-end, is composed of a catalytic component (M1 RNA) and a protein cofactor (C5 protein). In this study, effects of C5 protein on the RNase P catalysis with a precursor E. coli tRNA(Phe) having a single mismatch in the acceptor stem were examined. This mutant precursor unexpectedly generated upstream cleavage products at the -8 position as well as normal cleavage products at the +1 position. The cleavage at the -8 position was essentially effective only in the presence of C5 protein. Possible secondary structures for cleavage at the -8 position deviate significantly from the structures of the known RNase P substrates, implying that C5 protein can allow the enzyme to broaden the substrate specificity more than previously appreciated. |
| Links |
PubMed Online version:10.1006/bbrc.2000.2095 |
| Keywords |
Bacterial Proteins/metabolism; Base Sequence; Catalysis; DNA Primers/genetics; Endoribonucleases/metabolism; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; RNA Precursors/chemistry; RNA Precursors/genetics; RNA Precursors/metabolism; RNA Processing, Post-Transcriptional; RNA, Catalytic/metabolism; RNA, Transfer, Phe/chemistry; RNA, Transfer, Phe/genetics; RNA, Transfer, Phe/metabolism; Ribonuclease P; Substrate Specificity |
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