title: Regulation of bacterial RNase P ribozyme reaction by divalent cation and guide DNA.
abstract: The RNA subunit of bacterial ribonuclease P (RNase P) is a ribozyme which can cleave a canonical cloverleaf tRNA precursor and a hairpin RNA with a CCA-3' tag sequence as its substrate. With high concentration of Mg ion, the ribozyme as well as holo enzyme internally cleaves certain tRNAs in vitro. We denoted this unusual reaction as hyperprocessing. By controlling magnesium ion concentration for the reaction and also by forcing the RNA shape with external guide DNAs, we could regulate the hyperprocessing reaction by the bacterial RNase P enzymes. These techniques will lead the RNase P ribozyme to more designable and more applicable RNA-cleaving enzyme.
authors.affiliation: Division of Bioscience and Biotechnology, Department of Ecological Engineering, Toyohashi University of Technology, Tempakucho, 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: Yoshiaki
authors.initials: Y
authors.lastname: Hori
authors.forename: Yo
authors.initials: Y
authors.lastname: Kikuchi
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001483:Base Sequence; D002413:Cations, Divalent; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004722:Endoribonucleases / Q000378:metabolism*; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry / Q000378:metabolism*; D043262:Ribonuclease P
chemical_list: D002413:Cations, Divalent; D016337:RNA, Catalytic; D004247:DNA; D004722:Endoribonucleases; D043262:Ribonuclease P