title: Acquirement of hairpin ribozyme activity by the long substrate-binding site.
abstract: Three hairpin ribozymes were designed to cleave Escherichia coli beta-glucuronidase (GUS) mRNA at a target site. Two of the designed ribozymes (HG10L and HG10L2) had long substrate binding sites and the other (HG10) had short substrate binding site. All three ribozymes cleaved the substrate, and HG10L and HG10L2 cleaved it efficiently. However, HG10 had very low activity. Effect of length of substrate binding site of the ribozyme will be discussed.
authors.affiliation: College of Environmental Health, Azabu University, Kanagawa, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Hisamatsu
authors.forename: S
authors.initials: S
authors.lastname: Sonoki
authors.forename: Y
authors.initials: Y
authors.lastname: Kikuchi
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D004926:Escherichia coli / Q000201:enzymology; D005966:Glucuronidase / Q000378:metabolism; D008969:Molecular Sequence Data; D017860:Nepovirus / Q000235:genetics; D009690:Nucleic Acid Conformation; D012329:RNA, Bacterial / Q000378:metabolism*; D016337:RNA, Catalytic / Q000378:metabolism*; D012333:RNA, Messenger / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism*
chemical_list: D012329:RNA, Bacterial; D016337:RNA, Catalytic; D012333:RNA, Messenger; D012367:RNA, Viral; D005966:Glucuronidase