Acceptor stem and anticodon RNA hairpin helix interactions with glutamine tRNA synthetase

D. J. Wright, S. A. Martinis, M. Jahn, D. Söll, P. Schimmel

Research output: Contribution to journalArticlepeer-review


The class I glutamine (Gln) tRNA synthetase interacts with the anticodon and acceptor stem of glutamine tRNA. RNA hairpin helices were designed to probe acceptor stem and anticodon stem-loop contacts. A seven-base pair RNA microhelix derived from the acceptor stem of tRNAGln was aminoacylated by Gln tRNA synthetase. Variants of the glutamine acceptor stem microhelix implicated the discriminator base as a major identity element for glutaminylation of the RNA helix. A second RNA microhelix representing the anticodon stem-loop competitively inhibited tRNAGln charging. However, the anticodon stem-loop microhelix did not enhance aminoacylation of the acceptor stem microhelix. Thus, transduction of the anticodon identity signal may require covalent continuity of the tRNA chain to trigger efficient aminoacylation.

Original languageEnglish (US)
Pages (from-to)1041-1049
Number of pages9
Issue number12
StatePublished - 1993
Externally publishedYes


  • RNA recognition
  • aminoacyl tRNA synthetases
  • evolution of coding
  • genetic code
  • tRNA identity

ASJC Scopus subject areas

  • Biochemistry


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