Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes.
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.
Ando
Tomoaki
T
Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan.
Tanaka
Terumichi
T
Kikuchi
Yo
Y
D001412:Bacillus subtilis / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism; D009690:Nucleic Acid Conformation; D012322:RNA Precursors / Q000737:chemistry / Q000378:metabolism*; D012365:RNA, Transfer, Tyr / Q000737:chemistry / Q000378:metabolism*; D043262:Ribonuclease P / Q000378:metabolism*; D013379:Substrate Specificity
D012322:RNA Precursors; D012365:RNA, Transfer, Tyr; C030449:pre-tRNA(Tyr); D043262:Ribonuclease P; D008274:Magnesium