Send to

Choose Destination
Front Microbiol. 2019 May 24;10:1148. doi: 10.3389/fmicb.2019.01148. eCollection 2019.

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

Author information

Center for Integrated Protein Science Munich, Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany.
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
Department of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität München, Freising, Germany.
St. Petersburg State Polytechnic University, Saint Petersburg, Russia.
Faculty of Biosciences, Collaboration for Joint PhD Degree Between EMBL and Heidelberg University, Heidelberg, Germany.
Molecular Enzymology Group, University of Groningen, Groningen, Netherlands.


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.


EpmA; EarP; IF5A; NleB; Pseudomonas aeruginosa; TDP-rhamnose; bacterial two-hybrid; glycosylation

Supplemental Content

Full text links

Icon for Frontiers Media SA Icon for PubMed Central
Loading ...
Support Center