Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence
Fig 6
The J-domain from PFA66 stimulates the ATPase activity of HsHSP70, HsHSC70 and PfHSP70-X.
A) Single turn-over ATP hydrolysis of HsHSP70 in the presence of a peptide substrate (red circles) or PFAJDS (blue circles). Note that in contrast to Daniyan et al. 2016 [39], we clearly observe a stimulation of the hydrolysis of ATP by HsHsp70 (HSPA1A) in the presence of PFAJDS B) Single turn-over ATPase rates for HsHSC70, HsHsp70 and PfHSP70-X in the absence of any substrates or JDPs (black circles), in the presence of the substrate peptide (red circles) or in the presence of PFAJDH (blue circles). Shown are individual data points and standard deviation of independent experiments (n = 3 to 8). *, p < 0.05; **, p<0.001 (ANOVA with Holm-Sidak’s multiple comparison test).