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

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

doi:10.3390/ijms231810931

Open AccessArticle

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

by

Bulat Fatkhullin

^1,2,

Alexander Golubev

^3,4,

Natalia Garaeva

^3,4,

Shamil Validov

³,

Azat Gabdulkhakov

¹

and

Marat Yusupov

^2,3,*

¹

Institute of Protein Research, Russian Academy of Science, 142290 Pushchino, Russia

²

Department of Integrated Structural Biology, Institute of Genetics and Molecular and Cellular Biology, INSERM, U964, CNRS, UMR7104, University of Strasbourg, 67400 Illkirch Graffenstaden, France

³

Laboratory for Structural Analysis of Biomacromolecules, Kazan Scientific Center of Russian Academy of Sciences, 420111 Kazan, Russia

⁴

Laboratory of Structural Biology, Institute of Fundamental Medicine and Biology, Kazan Federal University, 420021 Kazan, Russia

^*

Author to whom correspondence should be addressed.

Int. J. Mol. Sci. 2022, 23(18), 10931; https://doi.org/10.3390/ijms231810931

Submission received: 19 August 2022 / Revised: 8 September 2022 / Accepted: 15 September 2022 / Published: 18 September 2022

(This article belongs to the Section Molecular Biology)

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Abstract

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 subunit. RsfS binds to the uL14 ribosomal protein on the large ribosomal subunit and prevents its association with the small subunit. Here, we estimated the contribution of RsfS amino acid side chains at the interface between RsfS and uL14 to RsfS anti-association function in Staphylococcus aureus through in vitro experiments: centrifugation in sucrose gradient profiles and an S. aureus cell-free system assay. The detected critical Y98 amino acid on the RsfS surface might become a new potential target for pharmacological drug development and treatment of S. aureus infections.

Keywords: ribosome; maturation factor; hibernation factor; RsfS; Staphylococcus aureus

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MDPI and ACS Style

Fatkhullin, B.; Golubev, A.; Garaeva, N.; Validov, S.; Gabdulkhakov, A.; Yusupov, M. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus. Int. J. Mol. Sci. 2022, 23, 10931. https://doi.org/10.3390/ijms231810931

AMA Style

Fatkhullin B, Golubev A, Garaeva N, Validov S, Gabdulkhakov A, Yusupov M. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus. International Journal of Molecular Sciences. 2022; 23(18):10931. https://doi.org/10.3390/ijms231810931

Chicago/Turabian Style

Fatkhullin, Bulat, Alexander Golubev, Natalia Garaeva, Shamil Validov, Azat Gabdulkhakov, and Marat Yusupov. 2022. "Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus" International Journal of Molecular Sciences 23, no. 18: 10931. https://doi.org/10.3390/ijms231810931

APA Style

Fatkhullin, B., Golubev, A., Garaeva, N., Validov, S., Gabdulkhakov, A., & Yusupov, M. (2022). Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus. International Journal of Molecular Sciences, 23(18), 10931. https://doi.org/10.3390/ijms231810931

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

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