KFU. Card publication. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus

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Y98 MUTATION LEADS TO THE LOSS OF RSFS ANTI-ASSOCIATION ACTIVITY IN STAPHYLOCOCCUS AUREUS

Form of presentation

Articles in international journals and collections

Year of publication

2022

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Authors, employees of KFU

Garaeva Nataliya Sergeevna, author

Bibliographic description in the original language

Fatkhullin B. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus/ Bulat Fatkhullin, Alexander Golubev, Natalia Garaeva, Shamil Validov, Azat Gabdulkhakov, Marat Yusupov// International Journal of Molecular Sciences. - 2022.- V.23. - P. 10931-10942

Annotation

International Journal of Molecular Sciences

Keywords

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

The name of the journal

International Journal of Molecular Sciences

URL

https://www.mdpi.com/1422-0067/23/18/10931/review_report

Please use this ID to quote from or refer to the card

https://repository.kpfu.ru/eng/?p_id=272393&p_lang=2

Full metadata record

Field DC	Value	Language
dc.contributor.author	Garaeva Nataliya Sergeevna	ru_RU
dc.date.accessioned	2022-01-01T00:00:00Z	ru_RU
dc.date.available	2022-01-01T00:00:00Z	ru_RU
dc.date.issued	2022	ru_RU
dc.identifier.citation	Fatkhullin B. Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus/ Bulat Fatkhullin, Alexander Golubev, Natalia Garaeva, Shamil Validov, Azat Gabdulkhakov, Marat Yusupov// International Journal of Molecular Sciences. - 2022.- V.23. - P. 10931-10942	ru_RU
dc.identifier.uri	https://repository.kpfu.ru/eng/?p_id=272393&p_lang=2	ru_RU
dc.description.abstract	International Journal of Molecular Sciences	ru_RU
dc.description.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.	ru_RU
dc.language.iso	ru	ru_RU
dc.subject		ru_RU
dc.title	Y98 Mutation Leads to the Loss of RsfS Anti-Association Activity in Staphylococcus aureus	ru_RU
dc.type	Articles in international journals and collections	ru_RU