PMID:16244456
| Citation |
Tanaka, T, Nagai, Y and Kikuchi, Y (2005) Substrate shape preference of Escherichia coli ribonuclease P ribozyme and holo enzyme using bottom-half part-shifting variants of pre-tRNA. Biosci. Biotechnol. Biochem. 69:1992-4 |
|---|---|
| Abstract |
We showed previously that the bacterial ribonuclease P (RNase P) ribozyme has substrate shape preference depending on the concentrations of catalytically important magnesium ions. The ribozyme discriminates a canonical cloverleaf precursor tRNA from a hairpin RNA with a CCA-tag sequence at low concentrations of magnesium ions. By detailed analysis of the shape preference using the bottom-half part-shifting variants of a tRNA precursor, we showed that the RNAs in a T-shape structure can be substrates for the ribozyme reactions even at low concentrations of magnesium ions, and that the RNA in a natural L-shape is the best substrate for both the ribozyme and the holo enzyme. The results also showed that the position of the bottom-half part did not affect the cleavage site selection of a substrate by the enzyme. Our results are the first kinetic evidence to show the importance of the bottom-half part of tRNA molecule, and our result also showed that the holo enzyme can discriminate substrate shape as well as the ribozyme at low concentrations of metal ions. |
| Links | |
| Keywords |
Escherichia coli Proteins/metabolism; Holoenzymes/metabolism; Kinetics; Magnesium; Nucleic Acid Conformation; RNA Precursors/chemistry; RNA Precursors/metabolism; RNA, Catalytic/metabolism; Ribonuclease P/metabolism; Substrate Specificity |
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