title: Unusual -1 ribosomal frameshift caused by stable RNA G-quadruplex in open reading frame.
abstract: Tertiary structures formed by mRNAs impact the efficiency of the translation reaction. Ribosomal frameshift is a well-characterized recoding process that occurs during translation elongation. Pseudoknot and stem-loop structures may stimulate frameshifting by causing a translational halt at a slippery sequence. In this study, we evaluated the efficiency of an unusual -1 frameshift caused by a noncanonical RNA G-quadruplex structure in mammalian cells. The reporter gene construct consisting of a fluorescent protein and Luciferase enabled evaluation of apparent and absolute values of the -1 frameshift efficiency and revealed significant increase of the efficiency by G-quadrupex forming potential sequence. In addition, berberine, a small molecule that binds to and stabilizes G-quadruplex structures, further increased the frameshift efficiency. These results indicate that the stable G-quadruplex structure stimulates the unusual -1 frameshift and has a potential to regulate the frameshift with its ligand.
authors.affiliation: Frontier Institute for Biomolecular Engineering Research (FIBER), Konan University , 7-1-20 Minatojima-minamimachi, Kobe 650-0047, Japan.
authors.forename: Tamaki
authors.initials: T
authors.lastname: Endoh
authors.forename: Naoki
authors.initials: N
authors.lastname: Sugimoto
mesh_terms: D001483:Base Sequence; D018965:Frameshifting, Ribosomal / Q000235:genetics*; D054856:G-Quadruplexes; D006801:Humans; D061986:MCF-7 Cells; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics*; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry* / Q000235:genetics*
chemical_list: D012313:RNA