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

Author

Listed:
  • Iskander Khusainov

    (Kazan Federal University
    University of Strasbourg
    Department of Molecular Sociology, Max Planck Institute of Biophysics)

  • Bulat Fatkhullin

    (Kazan Federal University
    Institute of Protein Research, Russian Academy of Sciences)

  • Simone Pellegrino

    (University of Strasbourg
    University of Cambridge)

  • 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
    University of Strasbourg)

  • Denis Zeyer

    (NovAliX, BioParc)

  • Natalie Trachtmann

    (Kazan Federal University
    University of Stuttgart)

  • 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
    University of Strasbourg)

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.

Suggested Citation

  • 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 , 2020. "Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-15517-0
    DOI: 10.1038/s41467-020-15517-0
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    Cited by:

    1. Iskander Khusainov & Natalie Romanov & Camille Goemans & Beata Turoňová & Christian E. Zimmerli & Sonja Welsch & Julian D. Langer & Athanasios Typas & Martin Beck, 2024. "Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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