Andrea N. Kravats

TL;DR: It is shown that yeast Hsp90 (Hsp82) and Hsp70 (Ssa1) directly interact in vitro in the absence of yeast Hop (Sti1) and a region in the middle domain of yeast HSp90 that is important for interaction with Hsp 70 is identified, suggesting that collaboration between HSp70 and HSP90 in protein remodeling may be modulated through competition between Hsp50 and H Sp90 cochaperones for the interaction surface.

TL;DR: The collaboration between Escherichia coli Hsp90 and DnaK is explored and it is found that the two chaperones form a complex that is stabilized by client protein binding.

TL;DR: Insight is provided into the molecular mechanism of collaboration between the DnaK/ Hsp70 system and ClpB/Hsp104 for protein disaggregation and homologous substitutions in subdomains IB and IIB of Ssa1 caused defects in collaboration between SSA1 and Hsp104.

TL;DR: The mutants provide insight into how the anti-adaptors perturb RssB response regulator function and activation and bears similarity to constitutively activated mutants found in a very different PP2C protein.

TL;DR: This work uses coarse-grained simulations to elucidate allostery-driven mechanisms of unfolding and translocation of a tagged four-helix bundle protein by the ClpY ATPase and finds that the resulting nonnative conformation is competent for translocation, which proceeds on a different time scale than unfolding and involves sharp stepped transitions.