title: Anticodon-independent aminoacylation of an RNA minihelix with valine.
abstract: Minihelices mimicking the amino acid acceptor and anticodon branches of yeast tRNA(Val) have been synthesized by in vitro transcription of synthetic templates. It is shown that a minihelix corresponding to the amino acid acceptor branch and containing solely a valine-specific identity nucleotide can be aminoacylated by yeast valyl-tRNA synthetase. Its charging ability is lost after mutating this nucleotide. This ability is stimulated somewhat by the addition of a second hairpin helix that mimicks the anticodon arm, which suggests that information originating from the anticodon stem-loop can be transmitted to the active site of the enzyme by the core of the protein.
authors.affiliation: Laboratoire de Biochimie, Centre National de la Recherche Scientifique, Strasbourg, France.
authors.forename: M
authors.initials: M
authors.lastname: Frugier
authors.forename: C
authors.initials: C
authors.lastname: Florentz
authors.forename: R
authors.initials: R
authors.lastname: Giegé
mesh_terms: D000926:Anticodon; D001483:Base Sequence; D006860:Hydrogen Bonding; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D012366:RNA, Transfer, Val / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae; D013329:Structure-Activity Relationship; D046249:Transfer RNA Aminoacylation; D014637:Valine-tRNA Ligase / Q000378:metabolism*
chemical_list: D000926:Anticodon; D012366:RNA, Transfer, Val; D014637:Valine-tRNA Ligase