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Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors

DOI: 10.1126/sciadv.aap9714 DOI Help

Authors: Ariel Talavera (Universiteit Brussel; VIB) , Jelle Hendrix (University of Leuven; Hasselt University) , Wim Versees (Vrije Universiteit Brussel; VIB) , Dukas Jurėnas (Université Libre de Bruxelles) , Katleen Van Nerom (Université Libre de Bruxelles) , Niels Vandenberk (University of Leuven) , Ranjan Kumar Singh (Vrije Universiteit Brussel; VIB) , Albert Konijnenberg (Vrije Universiteit Brussel; VIB; University of Antwerp) , Steven De Gieter (Vrije Universiteit Brussel; VIB) , Daniel Castro-Roa (Newcastle University) , Anders Barth (Ludwig-Maximilians-Universität München) , Henri De Greve (Vrije Universiteit Brussel; VIB) , Frank Sobott (University of Antwerp; University of Leeds) , Johan Hofkens (University of Leuven; University of Copenhagen) , Nikolay Zenkin (Newcastle University) , Remy Loris (Vrije Universiteit Brussel; VIB) , Abel Garcia-Pino (Université Libre de Bruxelles)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science Advances , VOL 4

State: Published (Approved)
Published: March 2018
Diamond Proposal Number(s): 17150

Open Access Open Access

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 β-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.

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: BM29 at ESRF; SWING at Soleil

Added On: 26/03/2018 10:28

Discipline Tags:

Life Sciences & Biotech Structural biology

Technical Tags:

Diffraction Macromolecular Crystallography (MX)