title: Cis and trans reactions of hairpin ribozymes derived from the negative strand of arabis mosaic virus satellite RNA.
abstract: We have previously shown that the hairpin ribozyme-like structure of the negative strand of the satellite RNA of arabis mosaic virus [(- )sArMV] has indeed ribozyme activity. However, some mutagenesis analyses revealed surprisingly that the wild type ribozyme was less active than almost all the other mutant ribozymes tested. These results were derived from a trans-acting system. Here we tested this ribozyme activity in a cis-acting system. We show that the (-)s ArMV hairpin ribozyme has different target-site specificities between cis and trans cleavages. The wild type ribozyme has the highest self-cleaving activity among the ribozyme variants tested.
authors.affiliation: Mitsubishi Kasei Institute of Life Sciences, Tokyo, Japan.
authors.forename: R
authors.initials: R
authors.lastname: Tomita
authors.forename: Y
authors.initials: Y
authors.lastname: Morikawa
authors.forename: S
authors.initials: S
authors.lastname: Hisamatsu
authors.forename: K
authors.initials: K
authors.lastname: Suzuki-Fujita
authors.forename: T
authors.initials: T
authors.lastname: Tanaka
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; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017860:Nepovirus / Q000201:enzymology* / Q000235:genetics; D009690:Nucleic Acid Conformation; D016337:RNA, Catalytic / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019244:RNA, Satellite / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013237:Stereoisomerism
chemical_list: D016337:RNA, Catalytic; D019244:RNA, Satellite