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. 2012 Nov 14;7(11):e49322. doi: 10.1371/journal.pone.0049322

Figure 6. Inhibition of Aha1p-stimulated ATPase activity of Hsp82p, Hsp82pG313S and Hsp82pA587T.

Figure 6

A. Inhibition of Aha1p-stimulated ATPase activity of wildtype Hsp82p (circles), Hsp82pG313S (squares), and Hsp82pA587T (triangles) by increasing concentrations of Sba1p. ATPase rate for wildtype Hsp82p and Hsp82pA587T shown on left axis (Reactions contained 2 µM Hsp82p, 10 µM Aha1p and indicated concentrations of Sba1p). ATPase rate for Hsp82pG313S shown on right axis (reactions contained 5 µM Hsp82p, 10 µM Aha1p and indicated concentrations of Sba1p). B. Inhibition of Hch1p-stimulated ATPase activity of wildtype Hsp82p (circles), and Hsp82pA587T (triangles) by increasing concentrations of Sba1p. Reactions contained 2 µM Hsp82p, 10 µM Hch1p and indicated concentrations of Sba1p. C. Inhibition of Aha1p-stimulated ATPase activity of wildtype Hsp82p (black bars) and Hsp82pA587T (white bars) by Sti1p. All reactions contained 2 µM Hsp82p and indicated concentrations of co-chaperones. D. Inhibition of Aha1p-stimulated ATPase activity of Hsp82pG313S (grey bars) by Sti1p. All reactions contained 2 µM Hsp82p and indicated concentrations of co-chaperones. E. Inhibition of Hch1p-stimulated ATPase activity of wildtype Hsp82p (black bars) and Hsp82pA587T (white bars) by Sti1p. All reactions contained 2 µM Hsp82p and indicated concentrations of co-chaperones. ATPase rates shown in µM ATP hydrolyzed per minute per µM of enzyme (1/min).