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

Only heterodimers of abd-A and exd bind strongly to the DNA probe tested; alone, neither binds the DNA probe very well, if at all. Heterodimer formation is affected by mutations in the DNA target.

abd-A and/or exd proteins were mixed with [32]P labeled fkh 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.

exd and hth were expressed and purified together as a heterodimer. Addition of abd-A results in trimer and tetramer formation on [32]P labeled DNA. Formation of these higher order complexes is

inhibited and partially supershifted by the addition of anti-En antibody indicating the complex contains en

Source was embryos of transgenic fly line; bait produced from tagged transgenic construct; prey produced from tagged transgenic construct.

Embryos were collected overnight and incubated at 4 degrees C for 28 hrs prior to BiFC detection.

Source was embryos of transgenic fly line; bait produced from tagged transgenic construct; prey produced from tagged transgenic construct.

Embryos were collected overnight and incubated at 4 degrees C for 28 hrs prior to BiFC detection.

Interaction in vitro; proteins produced by in vitro transcription/translation.

exd, hth and abd-A, in various combinations, were mixed with [32]P labeled DNA. DNA-protein complexes observed by EMSA, corresponding to abd-A-exd heterodimers and abd-A-exd-hth heterotrimers, were used to deduce protein-protein interactions.

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

abd-A and exd were mixed with [32]P labeled DNA. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions. Addition of grh resulted in a tetra-complex with abd-A, exd and DNA.