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

• Autores: Ingo Wohlgemuth, Christina Kothe, Frank Peske
• Localización: Science, ISSN 0036-8075, Vol. 339, Nº 6115, 2013, págs. 86-88
• Idioma: inglés
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• Resumen

  • 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.