10.3389/fmicb.2019.01148.s002 Wolfram Volkwein Wolfram Volkwein Ralph Krafczyk Ralph Krafczyk Pravin Kumar Ankush Jagtap Pravin Kumar Ankush Jagtap Marina Parr Marina Parr Elena Mankina Elena Mankina Jakub Macošek Jakub Macošek Zhenghuan Guo Zhenghuan Guo Maximilian Josef Ludwig Johannes Fürst Maximilian Josef Ludwig Johannes Fürst Miriam Pfab Miriam Pfab Dmitrij Frishman Dmitrij Frishman Janosch Hennig Janosch Hennig Kirsten Jung Kirsten Jung Jürgen Lassak Jürgen Lassak Data_Sheet_2_Switching the Post-translational Modification of Translation Elongation Factor EF-P.pdf Frontiers 2019 IF5A EarP EpmA bacterial two-hybrid glycosylation TDP-rhamnose Pseudomonas aeruginosa NleB 2019-05-24 14:42:13 Dataset https://frontiersin.figshare.com/articles/dataset/Data_Sheet_2_Switching_the_Post-translational_Modification_of_Translation_Elongation_Factor_EF-P_pdf/8182244 <p>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.</p>