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

Autor: 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, Marat Yusupov

Publikováno v: Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)

Upon transition to stationary phase or upon stress, bacteria limit protein synthesis through small inhibitory proteins that bind the ribosome. Here the authors decipher the interaction mode of the bacterial ribosome silencing factor (RsfS) at atomic

Externí odkaz: https://doaj.org/article/1ad738db839640ba9241f8a79ce45330

Abstract OR-15: Structural and Functional Studies of the Staphylococcus aureus Ribosome Hibernation

Autor: Konstantin Usachev, Iskander Khusainov, Bulat Fatkhullin, Shamil Validov, Marat Yusupov

Publikováno v: International Journal of Biomedicine, Vol 9, Iss Suppl_1, Pp S11-S12 (2019)

Background: In bacteria, diminishing of protein synthesis is often accompanied with the formation of ribosomal dimers (or disomes). This process might be particularly important for pathogenic bacteria whose successful survival is a key factor for suc

Externí odkaz: https://doaj.org/article/e9a5b601c25f4988ba229a787fc8807c

Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in

Autor: Bulat, Fatkhullin, Alexander, Golubev, Natalia, Garaeva, Shamil, Validov, Azat, Gabdulkhakov, Marat, Yusupov

Publikováno v: International journal of molecular sciences. 23(18)

Ribosomal silencing factor S (RsfS) is a conserved protein that plays a role in the mechanisms of ribosome shutdown and cell survival during starvation. Recent studies demonstrated the involvement of RsfS in the biogenesis of the large ribosomal subu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::22062b933865d35b286a255cd11bc2a4
https://pubmed.ncbi.nlm.nih.gov/36142845

Cryo‐EM structure of the ribosome functional complex of the human pathogen Staphylococcus aureus at 3.2 Å resolution

Autor: Bulat Fatkhullin, Marat Yusupov, Shamil Validov, Azat Gabdulkhakov, Iskander Khusainov, Konstantin S. Usachev, Lasse Jenner, Alexander Golubev, Gulnara Yusupova

Publikováno v: FEBS Letters
FEBS Letters, Wiley, 2020, ⟨10.1002/1873-3468.13915⟩
FEBS Letters, 2020, 594 (21), pp.3551-3567. ⟨10.1002/1873-3468.13915⟩
FEBS Letters, Wiley, 2020, 594 (21), pp.3551-3567. ⟨10.1002/1873-3468.13915⟩

International audience; Staphylococcus aureus is a bacterial pathogen and one of the leading causes of healthcare-acquired infections in the world. The growing antibiotic resistance of S. aureus obliges us to search for new drugs Accepted Article Thi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d61a32e4cd3048d03f5c2abdd6090f2
https://hal.archives-ouvertes.fr/hal-02997677

The key role of E418 carboxyl group in the formation of Nt.BspD6I nickase active site: Structural and functional properties of Nt.BspD6I E418A mutant

Autor: Boris P. Atanasov, A. K. Yunusova, L. A. Zheleznaya, T. A. Perevyazova, R.I. Artyukh, Bulat Fatkhullin, Galina S. Kachalova, Alexander Popov, Azat Gabdulkhakov

Publikováno v: Journal of structural biology. 210(3)

The mutated nickase Nt.BspD6I E418A has been obtained by site-directed mutagenesis. The purified protein has been crystallized, and its spatial structure has been determined at 2.45 A resolution. An analysis of the crystal structures of the wild-type

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d46b87294537906ba6ff66ae9870b08
https://pubmed.ncbi.nlm.nih.gov/32298813