10.3389/fmicb.2019.01148.s002
Wolfram Volkwein
Wolfram
Volkwein
Ralph Krafczyk
Ralph
Krafczyk
Pravin Kumar Ankush Jagtap
Pravin Kumar Ankush
Jagtap
Marina Parr
Marina
Parr
Elena Mankina
Elena
Mankina
Jakub Macošek
Jakub
Macošek
Zhenghuan Guo
Zhenghuan
Guo
Maximilian Josef Ludwig Johannes Fürst
Maximilian Josef Ludwig Johannes
Fürst
Miriam Pfab
Miriam
Pfab
Dmitrij Frishman
Dmitrij
Frishman
Janosch Hennig
Janosch
Hennig
Kirsten Jung
Kirsten
Jung
Jürgen Lassak
Jürgen
Lassak
Data_Sheet_2_Switching the Post-translational Modification of Translation Elongation Factor EF-P.pdf
Frontiers
2019
IF5A
EarP
EpmA
bacterial two-hybrid
glycosylation
TDP-rhamnose
Pseudomonas aeruginosa
NleB
2019-05-24 14:42:13
Dataset
https://frontiersin.figshare.com/articles/dataset/Data_Sheet_2_Switching_the_Post-translational_Modification_of_Translation_Elongation_Factor_EF-P_pdf/8182244
<p>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.</p>