title: Regulation of ribozyme activity by engineered protein switch.
abstract: Previously, we showed that the P3 domain of the Escherichia coli ribonuclease P ribozyme can be truncated and replaced in vitro. In this study, we prepared a P3-replaced variant of the E. coli ribozyme that has HIV TAR sequence as the engineered P3 domain. The mutant ribozyme demonstrated the ribonuclease P activity and was inhibited in the presence of the HIV tat protein fragment. Our results showed that the P3 domain of this enzyme can be engineered, and addition of some heterologous protein subunits can also be done to this domain.
authors.affiliation: Division of Bioscience and Biotechnology, Department of ecological Engineering, Toyohashi University of Technology, Tempakucho, Toyohashi, Aichi 441-8580, Japan.
authors.forename: Terumichi
authors.initials: T
authors.lastname: Tanaka
authors.forename: Naomi
authors.initials: N
authors.lastname: Kanda
authors.forename: Yo
authors.initials: Y
authors.lastname: Kikuchi
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D015696:Gene Products, tat / Q000378:metabolism; D005818:Genetic Engineering; D016325:HIV Long Terminal Repeat; D043262:Ribonuclease P / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; D015696:Gene Products, tat; D043262:Ribonuclease P; C470865:ribonuclease P, E coli