Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 insect cell system or bacterial system.

Dronc and Dark assemble into a multimeric complex in vitro.

Interaction in vitro; protein produced as a recombinant fusion protein in baculovirus-infected Sf9 insect cell system or bacterial system.

16 molecules of Dronc are arranged into two layers and sandwiched between two octameric rings of Dark.

Source was larvae of transgenic fly line; bait produced from tagged transgenic construct; prey produced from endogenous gene.

Mutation of Dronc ubiquitylation site K78 increases binding to Dark.

Dark-Dronc interaction requires Dark auto-inhibited (D333A) form to prevent it from oligomerizing, and Dronc proteolysis resistant (D113A, E135A, E143A, E352A) form. Dark-Dronc forms a hexamer, two heptamers and an octamer. Forced wild type Dark apoptosome formation by incubation with high concentrations of dATP is not as efficient as the Dark auto-inhibited monomer at forming a complex with Dronc

Interaction in vitro; proteins produced as recombinant fusion proteins in baculovirus and insect cell system.