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. Author manuscript; available in PMC: 2025 Apr 18.
Published in final edited form as: Cell Chem Biol. 2024 Mar 15;31(4):729–742.e13. doi: 10.1016/j.chembiol.2024.02.008

Figure 5. PfHsp90 increases proteasome substrate hydrolysis in vitro.

Figure 5.

(A) Time-course measurements of the relative hydrolysis of the proteasomal substrate Suc-LLVY-AMC in P. falciparum lysate. Compared to DMSO (white fill square), addition of PfHsp90 (3 μM; blue fill circle) increased total hydrolysis whereas the proteosome inhibitor bortezomib (25 μM; orange fill square) decreased total hydrolysis over an 180 minute incubation. Data shown as means ± SEM, n = 3–4; ****<0.0001; one-way ANOVA, Dunnett’s multiple comparison. (B) The relative rate of Suc-LLVY-AMC hydrolysis upon DMSO, bortezomib (25 μM), and PfHsp90 (3 μM) treatments. Relative rate determinations were made by comparing the linear slope of Suc-LLVY-AMC hydrolysis, excluding values before the 30 min time-point (A, dashed line). Concurrent chemical inhibition with BX-2819 (BX; 10 – 100 μM) negated the increased rate (~150%) of substrate hydrolysis upon PfHsp90 addition relative to the DMSO control. Data shown as means ± SEM, n = 3–4; not significant (ns)>0.05, **<0.01, ***<0.001, ****<0.0001; one-way ANOVA, Dunnett’s multiple comparison.