Abstract
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
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Research Support, Non-U.S. Gov't
MeSH terms
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Chymotrypsin / chemistry
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Gene Expression Regulation, Bacterial / physiology*
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Lysine / chemistry*
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Mass Spectrometry
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Mixed Function Oxygenases / genetics
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Mixed Function Oxygenases / metabolism*
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Molecular Structure
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Peptide Elongation Factors / genetics
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Peptide Elongation Factors / metabolism*
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Protein Binding
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Protein Processing, Post-Translational
Substances
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Escherichia coli Proteins
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Peptide Elongation Factors
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factor EF-P
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Mixed Function Oxygenases
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YfcM protein, E coli
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Chymotrypsin
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Lysine