Substrate selection by aminoacyl-tRNA synthetases.

M. Ibba, H. U. Thomann, K. W. Hong, J. M. Sherman, I. Weygand-Durasevic, S. Sever, N. Stange-Thomann, M. Praetorius, D. Söll

Research output: Contribution to journalReview articlepeer-review

7 Scopus citations


The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.

Original languageEnglish (US)
Pages (from-to)40-42
Number of pages3
JournalNucleic acids symposium series
Issue number33
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • General Medicine


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