Switching the Post-translational Modification of Translation Elongation Factor EF-P

• Published in: Frontiers in microbiology 2019-05, Vol.10, p.1148-1148
• Main Authors: Volkwein, Wolfram, Krafczyk, Ralph, Jagtap, Pravin Kumar Ankush, Parr, Marina, Mankina, Elena, Macošek, Jakub, Guo, Zhenghuan, Fürst, Maximilian Josef Ludwig Johannes, Pfab, Miriam, Frishman, Dmitrij, Hennig, Janosch, Jung, Kirsten, Lassak, Jürgen
• Format: Article
• Language: English
• Subjects: bacterial two-hybrid; EarP; EpmA; glycosylation; IF5A; Microbiology; TDP-rhamnose
• ISSN: 1664-302X; 1664-302X
• DOI: 10.3389/fmicb.2019.01148

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 . Bacteria with the arginine modification like 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 EF-P are needed for switching the modification strategy from lysylation to rhamnosylation.