Abstract
We prepared several mutants of the J3/4 and P4 domains of Escherichia coli ribonuclease P (RNase P): A62G, A62U, G63C/G64C, A65G, A67G, U69A, U69G, U69C, U69Δ, and U69UU. Comparison of the ribozyme and holo enzyme reactions at various concentrations of magnesium ions showed that the presence of a bulge at U69 in the P4 domain was important in the holo enzyme. The results also showed that the conserved bases G63 and G64 in the J3/4 domain were important for efficient ribozyme reactions but were replaceable in the presence of the protein component. Our data showed that the bases in the J3/4 and P4 domains displayed different responses to the metal ions that were affected by the presence of the protein component.
| Original language | English |
|---|---|
| Pages (from-to) | 1388-1392 |
| Number of pages | 5 |
| Journal | Bioscience, Biotechnology and Biochemistry |
| Volume | 68 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2004 Jun |
| Externally published | Yes |
Keywords
- C5 protein
- Escherichia coli
- M1 RNA
- Ribonuclease P (RNase P)
- Ribozyme
ASJC Scopus subject areas
- Food Science
- Applied Microbiology and Biotechnology
- Chemistry (miscellaneous)
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology