EF-P is essential for rapid synthesis of proteins containing consecutive proline residues
2013 | journal article
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Doerfel, Lili K., Ingo Wohlgemuth, Christina Kothe, Frank Peske, Henning Urlaub, and Marina V. Rodnina. "EF-P is essential for rapid synthesis of proteins containing consecutive proline residues." Science 339, no. 6115 (2013): 85-88. https://doi.org/10.1126/science.1229017.
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- Authors
- Doerfel, Lili K. ; Wohlgemuth, Ingo ; Kothe, Christina ; Peske, Frank ; Urlaub, Henning ; Rodnina, Marina V.
- 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.
- Issue Date
- 2013
- Journal
- Science
- eISSN
- 1095-9203
- Language
- English