Effector procaspases acquire high proteolytic activity only after they have been cleaved by active initiator caspases. In contrast, purified initiator procaspases can cleave themselves, and this autocatalytic cleavage stimulates their activity only modestly. Biochemical reconstitution experiments demonstrated that high activity of the initiator caspase-8 and caspase-9 required their incorporation into the DISC or apoptosome, respectively. Each of these procaspases has an adaptor domain (which enables it to assemble with other proteins), a prodomain, a low-affinity dimerization domain, and a catalytic domain. The catalytic domains of these caspases are identical at only 34% of the amino acids. Two competing models for the activation of caspase-9 have been proposed. In the allosteric model, Apaf-1 proteins in the apoptosome specifically interact with the catalytic domains of caspase-9 proteins, thereby triggering a transition to a catalytically active conformation. In the dimerization model, Apaf-1 proteins simply increase the local concentration of caspase-9 by binding several adaptor domains simultaneously, thereby promoting dimerization and coincident activation of caspase-9. To distinguish between these models, you make a hybrid protein containing part of caspase-9 and part of caspase-8, as shown in the figure. You test whether this hybrid protein can be activated by Fas ligand or cytochrome c. What do you expect if the allosteric model is correct?