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

Only heterodimers of Antp 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.

Antp 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 Antp bind DNA cooperatively as a heterodimer. exd alone does not bind the DNA, and Antp alone binds only weakly. Mutations to the binding sites disrupt the interaction.

Various combinations of exd and Antp were mixed with [32]P labeled DNA from a TfAP-2 regulatory region. DNA-protein complexes observed by EMSA were used to deduce protein-protein interactions.

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

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

Positive control.

Source was live HEK293 cells; proteins produced from transfected constructs.

Positive control.

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

Source was HEK293 cell line; fluorescence donor produced from tagged transgenic construct; fluorescence acceptor produced from tagged transgenic construct.

Published coordinates are relative to the HD domain.

Antp was fused to Hsap\TBP and formed a trimer with exd.