Lys34 of translation elongation factor EF-P is hydroxylated by YfcM

Nat Chem Biol. 2012 Aug;8(8):695-7. doi: 10.1038/nchembio.1001. Epub 2012 Jun 17.


Lys34 of the conserved translation elongation factor P (EF-P) is post-translationally lysinylated by YjeK and YjeA--a modification that is critical for bacterial virulence. Here we show that the currently accepted Escherichia coli EF-P modification pathway is incomplete and lacks a final hydroxylation step mediated by YfcM, an enzyme distinct from deoxyhypusine hydroxylase that catalyzes the final maturation step of eukaryotic initiation factor 5A, the eukaryotic EF-P homolog.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chymotrypsin / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial / physiology*
  • Lysine / chemistry*
  • Mass Spectrometry
  • Mixed Function Oxygenases / genetics
  • Mixed Function Oxygenases / metabolism*
  • Molecular Structure
  • Peptide Elongation Factors / genetics
  • Peptide Elongation Factors / metabolism*
  • Protein Binding
  • Protein Processing, Post-Translational


  • Escherichia coli Proteins
  • Peptide Elongation Factors
  • factor EF-P
  • Mixed Function Oxygenases
  • YfcM protein, E coli
  • Chymotrypsin
  • Lysine