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

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.

Automated summary

The conserved protein RsfS plays a role in ribosome shutdown and cell survival during starvation, and is involved in the biogenesis of the large ribosomal subunit. In this study, the contribution of specific amino acid side chains at the interface between RsfS and uL14 in Staphylococcus aureus was investigated. The results suggest that the Y98 amino acid on RsfS surface may be a potential target for drug development and treatment of S. aureus infections.