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

Dfd and exd bind DNA cooperatively; exd does not bind DNA on its own; alone, Dfd binds the probe tested only weakly.

Various combinations of Dfd and exd were mixed with [32]P labeled DNA. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.

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

Dfd and exd form heterodimers that bind DNA; exd alone does not bind DNA; Dfd alone binds DNA but less efficiently than the Dfd-exd heterodimer.

Various combinations of Dfd and exd were mixed with [32]P labeled DNA. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.

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

The exd-hth heterodimer and Dfd bind cooperatively to DNA; exd-hth alone does not bind to the DNA probe tested, and Dfd alone binds only weakly.

Dfd was mixed with a preformed exd-hth heterodimer ("exd-HM") and [32]P labeled DNA containing the modC Dfd autoregulatory element. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.

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

Kd = 1.3mM

exd does not bind DNA in the absence of Dfd.

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

Various combinations of exd and Dfd were mixed with [32]P labeled DNA. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.