Protein synthesis plays a pivotal role in determining the overall gene expression profile of the cell. The involvement of YchFs in translation has been hinted at in previous studies on bacterial, protozoan, and mammalian cells. In plant, YchF has been characterized as an unconventional P-loop GTPase that interacts with various ligands including rRNA. Here, using the model organism, Arabidopsis, we demonstrated the significance of ribosomal protein S7 (AtRPS7) binding by AtYchF1 on salt sensitivity. Polysome profiling suggested that AtYchF1 regulates translational efficiency in an AtRPS7-binding-depdenent manner. Translatomic and proteomic analyses together indicated that AtRPS7 regulates translation events at the heavy polysome through interacting with AtRPS7. A docking model was constructed and validated by site-directed mutagenesis and in vitro pull-down experiments to illustrate the molecular interactions between AtYchF1 and AtRPS7. Our study offers a structural framework for understanding the molecular basis of YchF proteins on translational regulation and stress responses.