The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

Nat Chem Biol. 2011 Aug 14;7(10):667-9. doi: 10.1038/nchembio.632.


The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts containing non-α-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of β-lysine, a substrate also predicted by genomic analyses. EF-P was efficiently functionally modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Lysine / analogs & derivatives*
  • Lysine / chemistry
  • Lysine / metabolism
  • Lysine-tRNA Ligase / chemistry
  • Lysine-tRNA Ligase / metabolism*
  • Models, Molecular
  • Molecular Structure
  • Peptide Elongation Factors / chemistry
  • Peptide Elongation Factors / metabolism*
  • Stereoisomerism


  • Peptide Elongation Factors
  • factor EF-P
  • beta-lysine
  • Lysine-tRNA Ligase
  • Lysine