The Disordered -Terminus of the Chaperone DnaK Increases the Competitive Fitness of and Facilitates the Toxicity of GraT.

Chaperone proteins are crucial for proper protein folding and quality control, especially when cells encounter stress caused by non-optimal temperatures. DnaK is one of such essential chaperones in bacteria. Although DnaK has been well characterized, the function of its intrinsically disordered -terminus has remained enigmatic as the deletion of this region has been shown to either enhance or reduce its protein folding ability. We have shown previously that DnaK interacts with toxin GraT of the GraTA toxin-antitoxin system in . Interestingly, the -terminal truncation of DnaK was shown to alleviate GraT-caused growth defects. Here, we aim to clarify the importance of DnaK in GraT activity. We show that DnaK increases GraT toxicity, and particularly important is the negatively charged motif in the DnaK -terminus. Given that GraT has an intrinsically disordered -terminus, the assistance of DnaK is probably needed for re-modelling the toxin structure. We also demonstrate that the DnaK -terminal negatively charged motif contributes to the competitive fitness of at both high and optimal growth temperatures. Thus, our data suggest that the disordered -terminal end of DnaK enhances the chaperone functionality.