The Protein Component of Bacterial Ribonuclease P Flickers the Metal Ion Response to the Substrate Shape Preference of the Ribozyme

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...

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Bibliographic Details
Published in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2003-10, Vol.67 (10), p.2294-2296
Main Authors: ANDO, Tomoaki, TANAKA, Terumichi, KIKUCHI, Yo
Format: Article
Language:English
Subjects:
Biological and medical sciences
Catalysis
Escherichia coli
Escherichia coli Proteins
Fundamental and applied biological sciences. Psychology
holo enzyme
Magnesium
Nucleic Acid Conformation
ribonuclease P
Ribonuclease P - metabolism
ribozyme
RNA Stability
RNA, Catalytic - metabolism
RNA, Transfer - chemistry
RNA, Transfer - metabolism
specificity
Substrate Specificity
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Summary: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.
ISSN:0916-8451
1347-6947
DOI:10.1271/bbb.67.2294