Fig. 4: Changes at the position of the conserved lysine affect client activation.
From: A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
a Yeast strains were exposed to the indicated dosage of UV light and subsequently analyzed for their ability to induce the Hsp90 dependent nucleotide excision repair. b The activation of the Hsp90 client v-src was tested by a lethality assay. Survival implies the inability of Hsp90 to activate v-src. c The activity of the glucocorticoid receptor (GR), which is dependent on Hsp90 was measured in a ß-galactosidase assay. Activities were normalized to ß-galactosidase activity of wt Hsp90. The error bars for the activity represent s.d. from three biological replicates (n = 3). Statistical significance was assessed using a two-sample t-test and a level of significance of 0.05 (*), 0.01 (**), and 0.001 (***). d The binding of the different Hsp90 constructs to the ligand binding domain of the glucocorticoid receptor (GR-LBD) was analyzed by analytical ultracentrifugation. dc/dt plots are shown for GR-LBD-Atto 488 (purple) and the mixtures of GR-LBDm-Atto 488 with the indicated Hsp90 mutants. Source data are provided as a Source Data file.
