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 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.
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi, Aichi, Japan.
Tomoaki
T
Ando
Terumichi
T
Tanaka
Yo
Y
Kikuchi
D002384:Catalysis; D029968:Escherichia coli Proteins; D008274:Magnesium; D009690:Nucleic Acid Conformation; D020871:RNA Stability; D016337:RNA, Catalytic / Q000378:metabolism; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D043262:Ribonuclease P / Q000378:metabolism*; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D016337:RNA, Catalytic; D012343:RNA, Transfer; D043262:Ribonuclease P; D008274:Magnesium