Figure 7. The heterotrimeric complexes exhibit differences in their ability to undergo subunit exchange.

The heterotrimers Hal3^PD_H378A/Cab3^PD (H* + C) and Hal3^PD_H378A/Vhs3^PD_H459A/Cab3^PD (H* + V* + C) were titrated with five- and 10-fold (relative to the monomer concentration of the inactive heterotrimer) of either Hal3^PD (H) or Vhs3^PD (V). The activities (reported as nmol/min/nmol protein) were adjusted to the monomer concentration of the inactive heterotrimers (i.e. excess Hal3^PD or Vhs3^PD added was not considered in the calculation). The data indicated the average of an experiment performed in triplicate; the error bars indicate the standard deviation. Values were compared to that of the inactive control (buffer) by one-way ANOVA followed by Dunnet’s post-test (*p < 0.05).