КФУ. Карточка публикации. 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

Форма представления

Статьи в зарубежных журналах и сборниках

Год публикации

2022

Язык

английский

Авторы, сотрудники КФУ

Гараева Наталия Сергеевна, автор

Библиографическое описание на языке оригинала

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

Аннотация

International Journal of Molecular Sciences

Ключевые слова

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

Название журнала

International Journal of Molecular Sciences

URL

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

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https://repository.kpfu.ru/?p_id=272393

Полная запись метаданных

Поле DC	Значение	Язык
dc.contributor.author	Гараева Наталия Сергеевна	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/?p_id=272393	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	Статьи в зарубежных журналах и сборниках	ru_RU