Switching the post-translational modification of translation elongation factor EF-P

• Verfasst von: Volkwein, Wolfram [VerfasserIn]
• Verfasst von: Jagtap, Pravin Kumar Ankush [VerfasserIn]
• Verfasst von: Macošek, Jakub [VerfasserIn]
• Verfasst von: Hennig, Janosch [VerfasserIn]
• Titel: Switching the post-translational modification of translation elongation factor EF-P
• Verf.angabe: Wolfram Volkwein, Ralph Krafczyk, Pravin Kumar Ankush Jagtap, Marina Parr, Elena Mankina, Jakub Macošek, Zhenghuan Guo, Maximilian Josef Ludwig Johannes Fürst, Miriam Pfab, Dmitrij Frishman, Janosch Hennig, Kirsten Jung and Jürgen Lassak
• E-Jahr: 2019
• Jahr: 24 May 2019
• Umfang: 16 S.
• Fussnoten: Gesehen am 20.04.2020
• Titel Quelle: Enthalten in: Frontiers in microbiology
• Ort Quelle: Lausanne : Frontiers Media, 2010
• Jahr Quelle: 2019
• Band/Heft Quelle: 10(2019) Artikel-Nummer 1148, 16 Seiten
• ISSN Quelle: 1664-302X
• DOI: doi:10.3389/fmicb.2019.01148
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Bacterial two-hybrid
• Sach-SW: EARP
• Sach-SW: EPMA
• Sach-SW: Glycosylation
• Sach-SW: IF5A
• Sach-SW: Luminescence
• Sach-SW: NleB
• Sach-SW: Post-tranlational modification of arginine
• Sach-SW: Pseudomonas aeruginosa
• Sach-SW: TDP-rhamnose
• Sach-SW: YjeA
• K10plus-PPN: 1695011791

Abstract

Tripeptides with two consecutive prolines are the shortest and most frequent sequences causing ribosome stalling. The bacterial translation elongation factor P (EF-P) relieves this arrest, allowing protein biosynthesis to continue. A seven amino acids long loop between beta-strands β3/β4 is crucial for EF-P function and modified at its tip by lysylation of lysine or rhamnosylation of arginine. Phylogenetic analyses unveiled an invariant proline in the -2 position of the modification site in EF Ps that utilize lysine modifications such as Escherichia coli. Bacteria with the arginine modification like Pseudomonas putida on the contrary have selected against it. Focusing on the EF-Ps from these two model organisms we demonstrate the importance of the β3/β4 loop composition for functionalization by chemically distinct modifications. Ultimately, we show that only two amino acid changes in E. coli EF P are needed for switching the modification strategy from lysylation to rhamnosylation.