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

Fiche publication

Date publication

septembre 2022

Journal

International journal of molecular sciences

Auteurs

Membres identifiés du Cancéropôle Est :
Dr YUSUPOV Marat

Tous les auteurs :
Fatkhullin B, Golubev A, Garaeva N, Validov S, Gabdulkhakov A, Yusupov M

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/36142845

Résumé

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 through in vitro experiments: centrifugation in sucrose gradient profiles and an 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 infections.