The balance between pre- and post-transfer editing in tRNA synthetases

Susan A. Martinis, Michal T. Boniecki

Research output: Contribution to journalReview articlepeer-review


The fidelity of tRNA aminoacylation is dependent in part on amino acid editing mechanisms. A hydrolytic activity that clears mischarged tRNAs typically resides in an active site on the tRNA synthetase that is distinct from its synthetic aminoacylation active site. A second pre-transfer editing pathway that hydrolyzes the tRNA synthetase aminoacyl adenylate intermediate can also be activated. Pre- and post-transfer editing activities can co-exist within a single tRNA synthetase resulting in a redundancy of fidelity mechanisms. However, in most cases one pathway appears to dominate, but when compromised, the secondary pathway can be activated to suppress tRNA synthetase infidelities.

Original languageEnglish (US)
Pages (from-to)455-459
Number of pages5
JournalFEBS Letters
Issue number2
StatePublished - Jan 21 2010


  • Amino acid editing
  • Aminoacylation
  • Fidelity
  • Protein synthesis

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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