Publication
Title
Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors
Author
Abstract
Bacterial protein synthesis is intricately connected to metabolic rate. One of the ways in which bacteria respond to environmental stress is through posttranslational modifications of translation factors. Translation elongation factor Tu (EF-Tu) is methylated and phosphorylated in response to nutrient starvation upon entering stationary phase, and its phosphorylation is a crucial step in the pathway toward sporulation. We analyze how phosphorylation leads to inactivation of Escherichia coli EF-Tu. We provide structural and biophysical evidence that phosphorylation of EF-Tu at T382 acts as an efficient switch that turns off protein synthesis by decoupling nucleotide binding from the EF-Tu conformational cycle. Direct modifications of the EF-Tu switch I region or modifications in other regions stabilizing the beta-hairpin state of switch I result in an effective allosteric trap that restricts the normal dynamics of EF-Tu and enables the evasion of the control exerted by nucleotides on G proteins. These results highlight stabilization of a phosphorylation-induced conformational trap as an essential mechanism for phosphoregulation of bacterial translation and metabolism. We propose that this mechanism may lead to the multisite phosphorylation state observed during dormancy and stationary phase.
Language
English
Source (journal)
Science Advances
Publication
2018
ISSN
2375-2548
Volume/pages
4 :3 (2018) , 14 p.
Article Reference
eaap9714
ISI
000427892700026
Pubmed ID
29546243
Medium
E-only publicatie
Full text (Publisher's DOI)
UAntwerpen
Faculty/Department
Research group
Project info
4D Protein Structure.
Publication type
Subject
Affiliation
Publications with a UAntwerp address
External links
Web of Science
Record
Identification
Creation 04.05.2018
Last edited 21.09.2021
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