Journal
NATURE CHEMICAL BIOLOGY
Volume 8, Issue 8, Pages 695-697Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1001
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Funding
- Deutsche Forschungsgemeinschaft [WI3285/1-1]
- Human Frontiers of Science Foundation [RGY88/2008]
- European Molecular Biology Organization young investigator program
- Estonian Science Foundation [9289]
- European Social Fund program Mobilitas [MJD144, MJD99]
- European Regional Development Fund through the Center of Excellence in Chemical Biology (Institute of Technology, University of Tartu)
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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.
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