Substrate shape preference of Escherichia coli ribonuclease P ribozyme and holo enzyme using bottom-half part-shifting variants of pre-tRNA

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 conce...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005-10, Vol.69 (10), p.1992-1994, Article 1992
Main Authors: Tanaka, T.(Toyohashi Univ. of Technology, Aichi (Japan)), Nagai, Y, Kikuchi, Y
Format: Article
Language:English
Subjects:
ARN
Biological and medical sciences
CHEMICAL COMPOSITION
CHEMICAL STRUCTURE
cloverleaf
COMPOSICION QUIMICA
COMPOSITION CHIMIQUE
CONCEPTION
DESIGN
DISENO
ENZIMAS
ENZYME
ENZYMES
ESCHERICHIA COLI
Escherichia coli Proteins - metabolism
ESTRUCTURA QUIMICA
Fundamental and applied biological sciences. Psychology
hairpin RNA
Holoenzymes - metabolism
ION
IONES
IONS
Kinetics
MAGNESIO
MAGNESIUM
METAL
METALES
METALS
Nucleic Acid Conformation
RIBONUCLEASAS
RIBONUCLEASE
ribonuclease P
Ribonuclease P - metabolism
RIBONUCLEASES
RNA
RNA Precursors - chemistry
RNA Precursors - metabolism
RNA, Catalytic - metabolism
STRUCTURE CHIMIQUE
Substrate Specificity
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Summary: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 Tshape 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.
ISSN:0916-8451
1347-6947
1347-6947
DOI:10.1271/bbb.69.1992