title: Comparative analyses of hairpin substrate recognition by Escherichia coli and Bacillus subtilis ribonuclease P ribozymes.
abstract: 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.
authors.affiliation: Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi, Aichi 441-8580, Japan.
authors.forename: Tomoaki
authors.initials: T
authors.lastname: Ando
authors.forename: Terumichi
authors.initials: T
authors.lastname: Tanaka
authors.forename: Yo
authors.initials: Y
authors.lastname: Kikuchi
mesh_terms: 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
chemical_list: D012322:RNA Precursors; D012365:RNA, Transfer, Tyr; C030449:pre-tRNA(Tyr); D043262:Ribonuclease P; D008274:Magnesium