Binding of misacylated tRNAs to the ribosomal a site

Taraka Dale, Olke C. Uhlenbeck*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


To test whether the ribosome displays specificity for the esterified amino acid and the tRNA body of an aminoacyl-tRNA (aa-tRNA), the stabilities of 4 correctly acylated and 12 misacylated tRNAs in the ribosomal A site were determined. By introducing the GAC (valine) anticodon into each tRNA, a constant anticodon·codon interaction was maintained, thus removing concern that different anticodon·codon strengths might affect the binding of the different aa-tRNAs to the A site. Surprisingly, all 16 aa-tRNAs displayed similar dissociation rate constants from the A site. These results suggest that either the ribosome is not specific for different amino acids and tRNA bodies when intact aa-tRNAs are used or the specificity for the amino acid side chain and tRNA body is masked by a conformational change upon aa-tRNA release. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)1610-1615
Number of pages6
Issue number11
StatePublished - Nov 2005


  • A site
  • Misacylated tRNA
  • Ribosome
  • Ribosome binding
  • Uniformity
  • tRNA

ASJC Scopus subject areas

  • Molecular Biology


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