Abstract
The substrate shape specificity of the Escherichia coli ribonuclease P (RNase P) ribozyme depends on the concentration of magnesium ion. At 10 mM or more, it can cleave a hairpin substrate as well as a cloverleaf pre-transfer RNA (tRNA). The results showed, however, that the holo enzyme cleaved the hairpin substrate at low concentrations of magnesium ion. Considering that the homologous E. coli tRNAs are resistant to internal cleavage by the RNase P, the phenomena suggest that this catalytic activity might take part in the removing the mis-folded RNAs in the cell.
| Original language | English |
|---|---|
| Pages (from-to) | 2294-2296 |
| Number of pages | 3 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 67 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 2003 Oct |
| Externally published | Yes |
Keywords
- Escherichia coli
- Holo enzyme
- Ribonuclease P
- Ribozyme
- Specificity
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology
- Chemistry (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology
- Bioengineering