Fig. 2: Co-chaperone actions are influenced by the modifications.
From: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
a, c ATP turnover of the WT and the different mutants in the presence of the co-chaperone Aha1. b, d The binding of the different Hsp90 constructs to Aha1 was analyzed by analytical ultracentrifugation. dc/dt plots are shown for Aha1-FAM (purple) and the mixtures of Aha1-FAM with the indicated Hsp90 constructs. e Normalized ATPase activity of the WT and the mutants in the presence of the inhibitory protein p23/Sba1. f The binding of the different Hsp90 mutants to p23/Sba1 was analyzed by analytical ultracentrifugation. dc/dt plots are shown for p23/Sba1-Atto488 (purple) and its mixtures with the indicated mutants.
