EF-P Is Essential for Rapid Synthesis of Proteins Containing Consecutive Proline Residues

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Science  13 Dec 2012:
DOI: 10.1126/science.1229017

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Elongation factor P (EF-P) is a translation factor of unknown function which 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-tRNA 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.

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