PMID:12951523
| Citation |
Ando, T, Tanaka, T and Kikuchi, Y (2003) Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes. Biosci. Biotechnol. Biochem. 67:1825-7 |
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| Abstract |
Previously, we reported that the substrate shape recognition of the Escherichia coli ribonuclease (RNase) P ribozyme depends on the concentration of magnesium ion in vitro. We additionally examined the Bacillus subtilis RNase P ribozyme and found that the B. subtilis enzyme also required high magnesium ion, above 10 mM, for cleavage of a hairpin substrate. The results of kinetic studies showed that the metal ion concentration affected both the catalysis and the affinity of the ribozymes toward a hairpin RNA substrate. |
| Links | |
| Keywords |
Bacillus subtilis/enzymology; Escherichia coli/enzymology; Humans; Kinetics; Magnesium/chemistry; Magnesium/metabolism; Nucleic Acid Conformation; RNA Precursors/chemistry; RNA Precursors/metabolism; RNA, Transfer, Tyr/chemistry; RNA, Transfer, Tyr/metabolism; Ribonuclease P/metabolism; Substrate Specificity |
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