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Given the documented genetic interactions and the similarities in effects on marker gene expression, we were surprised by the apparent lack of physical interaction between ABI4 and any other ABIs. Therefore we tested whether such interactions might either be masked by the high level of basal expression, or require formation of a ternary complex. Although further truncations of ABI4 in the BD fusion resulted in lower basal reporter-gene expression, none interacted with the AD-ABIs (data not shown). While deletion of various carboxy-terminal regions might remove domains required for interaction with other proteins, all the truncations encoded the complete AP2 domain, including the potential dimerization domain. Although it is also possible that these truncations are misfolded and/or unstable, and therefore not available for interaction, one of the ABI4 truncations in a BD fusion has been used successfully as a ‘bait’ construct in a two-hybrid screen (S.N., unpublished results).
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