%0 Generic %A Volkwein, Wolfram %A Krafczyk, Ralph %A Jagtap, Pravin Kumar Ankush %A Parr, Marina %A Mankina, Elena %A Macošek, Jakub %A Guo, Zhenghuan %A Fürst, Maximilian Josef Ludwig Johannes %A Pfab, Miriam %A Frishman, Dmitrij %A Hennig, Janosch %A Jung, Kirsten %A Lassak, Jürgen %D 2019 %T Data_Sheet_3_Switching the Post-translational Modification of Translation Elongation Factor EF-P.fasta %U https://frontiersin.figshare.com/articles/dataset/Data_Sheet_3_Switching_the_Post-translational_Modification_of_Translation_Elongation_Factor_EF-P_fasta/8182247 %R 10.3389/fmicb.2019.01148.s003 %2 https://frontiersin.figshare.com/ndownloader/files/15250631 %K IF5A %K EarP %K EpmA %K bacterial two-hybrid %K glycosylation %K TDP-rhamnose %K Pseudomonas aeruginosa %K NleB %X

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.

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