Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.
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.
Institute of Technology, University of Tartu, Tartu, Estonia.
Lauri
L
Peil
Agata L
AL
Starosta
Kai
K
Virumäe
Gemma C
GC
Atkinson
Tanel
T
Tenson
Jaanus
J
Remme
Daniel N
DN
Wilson
D002918:Chymotrypsin / Q000737:chemistry; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D008239:Lysine / Q000737:chemistry*; D013058:Mass Spectrometry; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism*; D015394:Molecular Structure; D010445:Peptide Elongation Factors / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011499:Protein Processing, Post-Translational
D029968:Escherichia coli Proteins; D010445:Peptide Elongation Factors; C020746:factor EF-P; D006899:Mixed Function Oxygenases; C575986:YfcM protein, E coli; D002918:Chymotrypsin; D008239:Lysine