Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach

Iskander Khusainov (), Bulat Fatkhullin, Simone Pellegrino, Aydar Bikmullin, Wen-ti Liu, Azat Gabdulkhakov, Amr Al Shebel, Alexander Golubev, Denis Zeyer, Natalie Trachtmann, Georg A. Sprenger, Shamil Validov, Konstantin Usachev, Gulnara Yusupova () and Marat Yusupov ()
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Iskander Khusainov: Kazan Federal University
Bulat Fatkhullin: Kazan Federal University
Simone Pellegrino: University of Strasbourg
Aydar Bikmullin: Kazan Federal University
Wen-ti Liu: NovAliX, BioParc
Azat Gabdulkhakov: Institute of Protein Research, Russian Academy of Sciences
Amr Al Shebel: Kazan Federal University
Alexander Golubev: Kazan Federal University
Denis Zeyer: NovAliX, BioParc
Natalie Trachtmann: Kazan Federal University
Georg A. Sprenger: University of Stuttgart
Shamil Validov: Kazan Federal University
Konstantin Usachev: Kazan Federal University
Gulnara Yusupova: University of Strasbourg
Marat Yusupov: Kazan Federal University

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract For the sake of energy preservation, bacteria, upon transition to stationary phase, tone down their protein synthesis. This process is favored by the reversible binding of small stress-induced proteins to the ribosome to prevent unnecessary translation. One example is the conserved bacterial ribosome silencing factor (RsfS) that binds to uL14 protein onto the large ribosomal subunit and prevents its association with the small subunit. Here we describe the binding mode of Staphylococcus aureus RsfS to the large ribosomal subunit and present a 3.2 Å resolution cryo-EM reconstruction of the 50S-RsfS complex together with the crystal structure of uL14-RsfS complex solved at 2.3 Å resolution. The understanding of the detailed landscape of RsfS-uL14 interactions within the ribosome shed light on the mechanism of ribosome shutdown in the human pathogen S. aureus and might deliver a novel target for pharmacological drug development and treatment of bacterial infections.

Date: 2020
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DOI: 10.1038/s41467-020-15517-0

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