Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

The human orthologs of CG14962 (ASCIZ) and ctp (Dynein light chain) also interact in this assay.

Interaction in vitro; proteins produced as a recombinant fusion protein in bacterial system.

In addition to a 1:7 complex, AUC profiles reveal smaller sub-saturated species which are favored relative to the high-occupancy complex even with an excess of ctp.

Interaction in vitro; proteins produced as a recombinant fusion protein in bacterial system.

With increasing concentrations of ctp, a smear of higher order complexes appears.

Interaction in vitro; proteins produced as a recombinant fusion protein in bacterial system.

Predominantly 1:2-1:4 complexes visualized.

Four types of Asciz-ctp complexes detected with stoichiometries of 1:2 , 1:4 , 2:6 , 2:8 with 2:6 being most stable.

Interaction in vitro; proteins produced as recombinant fusion proteins in bacterial system.

Multiple single and combination Asciz QT domains were tested to determine order and stability of binding to ctp. QT domains were replaced with AAA residues within the context of QT-4 for the different combinations.

Interaction in vitro; bait produced as a recombinant fusion protein in bacterial system; prey produced as a recombinant fusion protein in bacterial system.

Interaction in vitro; proteins produced as recombinant fusion proteins in bacterial system.

Multiple combinations Asciz QT domains were tested to determine order and stability of binding to ctp. QT domains were replaced with AAA residues within the context of QT-4 aa 270-340, for the different combinations. QT2,3 bound most efficiently and QT2,4 bound earliest.

Interaction in vitro; proteins produced as recombinant fusion proteins in bacterial system.

Asciz QT domain 2,3 interacts with 2 ctp dimers most abundantly. QT domains 2,4 and 3,4 interact with one ctp dimer most abundantly.

Interaction in vitro; proteins produced as a recombinant fusion proteins in bacterial system.

ctp forms dimers, 3mers and 4mers; dimers most abundantly interact with Asciz QT-4 domains.