title: EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.
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.
authors.affiliation: Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany.
authors.forename: Lili K
authors.initials: LK
authors.lastname: Doerfel
authors.forename: Ingo
authors.initials: I
authors.lastname: Wohlgemuth
authors.forename: Christina
authors.initials: C
authors.lastname: Kothe
authors.forename: Frank
authors.initials: F
authors.lastname: Peske
authors.forename: Henning
authors.initials: H
authors.lastname: Urlaub
authors.forename: Marina V
authors.initials: MV
authors.lastname: Rodnina
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008969:Molecular Sequence Data; D010445:Peptide Elongation Factors / Q000378:metabolism*; D011392:Proline / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012270:Ribosomes / Q000378:metabolism*
chemical_list: D010445:Peptide Elongation Factors; C020746:factor EF-P; D011392:Proline; D008239:Lysine