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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

1
Center for Integrated Protein Science Munich, Department of Biology I, Microbiology, Ludwig-Maximilians-Universität München, Munich, Germany.
2
Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany.
3
Department of Bioinformatics, Wissenschaftszentrum Weihenstephan, Technische Universität München, Freising, Germany.
4
St. Petersburg State Polytechnic University, Saint Petersburg, Russia.
5
Faculty of Biosciences, Collaboration for Joint PhD Degree Between EMBL and Heidelberg University, Heidelberg, Germany.
6
Molecular Enzymology Group, University of Groningen, Groningen, Netherlands.

Abstract

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.

KEYWORDS:

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

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