Fig. 3: 2H compromised the chaperone activities of purified Msi3 protein.
From: A first-in-class inhibitor of Hsp110 molecular chaperones of pathogenic fungi
a The holdase activity of Msi3 assayed using OD readings at 320 nm (OD320). Purified firefly luciferase was used as a substrate. The OD320 values were recorded during incubation at 42 °C. Increased OD320 values represent the aggregation of luciferase. Data are presented as mean values + /- SEM (n = 3 independent experiments). b The effect of 2H on the holdase activity of Msi3 (red circles) and Hsp105 (green squares). The substrate is firefly luciferase. The activity in the absence of 2H was set as 100%. Data are presented as mean values + /- SEM (n = 7 independent experiments). c Refolding activity of the Ssa1 chaperone machinery. Firefly luciferase was used as a substrate. After denaturation, the refolding of luciferase in the presence of different combinations of chaperones was measured over time. Chaperones included Ssa1 (A), Msi3 (M), and Ydj1 (Y). The activity of luciferase before denaturation was set as 100%. Data are presented as mean values + /- SEM (n = 3 independent experiments). Source data are provided as a Source Data file for all the panels.
