PMID:23239624

Citation	Doerfel, LK, Wohlgemuth, I, Kothe, C, Peske, F, Urlaub, H and Rodnina, MV (2013) EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339:85-8
Abstract	Elongation factor P (EF-P) is a translation factor of unknown function that has been implicated in a great variety of cellular processes. Here, we show that EF-P prevents ribosome from stalling during synthesis of proteins containing consecutive prolines, such as PPG, PPP, or longer proline strings, in natural and engineered model proteins. EF-P promotes peptide-bond formation and stabilizes the peptidyl-transfer RNA in the catalytic center of the ribosome. EF-P is posttranslationally modified by a hydroxylated β-lysine attached to a lysine residue. The modification enhances the catalytic proficiency of the factor mainly by increasing its affinity to the ribosome. We propose that EF-P and its eukaryotic homolog, eIF5A, are essential for the synthesis of a subset of proteins containing proline stretches in all cells.
Links	PubMed Online version:10.1126/science.1229017
Keywords	Amino Acid Sequence; Escherichia coli/genetics; Escherichia coli/metabolism; Lysine/metabolism; Molecular Sequence Data; Peptide Elongation Factors/metabolism; Proline/genetics; Proline/metabolism; Protein Biosynthesis; Protein Processing, Post-Translational; Ribosomes/metabolism
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