Fiche publication
Date publication
avril 2020
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat
,
Dr YUSUPOVA Gulnara
Tous les auteurs :
Khusainov I, Fatkhullin B, Pellegrino S, Bikmullin A, Liu WT, Gabdulkhakov A, Shebel AA, Golubev A, Zeyer D, Trachtmann N, Sprenger GA, Validov S, Usachev K, Yusupova G, Yusupov M
Lien Pubmed
Résumé
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.
Référence
Nat Commun. 2020 Apr 3;11(1):1656
