at Google ScholarTitle data
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:
Switching the Post-translational Modification of Translation Elongation Factor EF-P.
In: Frontiers in Microbiology.
Vol. 10
(2019)
.
- 1148.
ISSN 1664-302X
DOI: https://doi.org/10.3389/fmicb.2019.01148
Abstract in another language
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.