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

Title 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) . - No. 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.

Further data

Item Type: Article in a journal
Refereed: Yes
Keywords: EpmA; EarP; IF5A; NleB; Pseudomonas aeruginosa; TDP-rhamnose; bacterial two-hybrid; glycosylation
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry - Univ.-Prof. Dr. Janosch Hennig
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry with an Emphasis on Biophysical Chemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 06 Oct 2021 11:25
Last Modified: 24 Nov 2022 07:18
URI: https://eref.uni-bayreuth.de/id/eprint/67211