Anticodon-independent aminoacylation of an RNA minihelix with valine.
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.
Frugier
M
M
Laboratoire de Biochimie, Centre National de la Recherche Scientifique, Strasbourg, France.
Florentz
C
C
Giegé
R
R
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*
D000926:Anticodon; D012366:RNA, Transfer, Val; D014637:Valine-tRNA Ligase