Abstract
HOMEODOMAIN proteins regulate diverse developmental processes in a wide range of organisms, yet bind in vitro to DNA sequences that are remarkably similar1. This has raised the fundamental question of how target gene specificity is achieved in vivo. The Drosophila fushi tarazu protein (Ftz) contains a homeodomain2 and is required for the formation of alternate segments3. We have shown previously that a homeodomain-deleted Ftz polypeptide (FtzΔHD), incapable of binding DNA in vitro, could regulate endogenous ftz gene expression4. Here we test FtzΔHD activities in a ftzmutant background and find that, surprisingly, FtzΔHD can directly regulated ftz-dependent segmentation, suggesting that it can control target gene expression through interactions with other proteins. A likely candidate is the pair-rule protein Paired (Prd). FtzΔHD bound directly to Prd in vitro and required Prd to repress wingless in vivo. These results emphasize the pivotal importance of protein–protein interactions in homeodomain protein function.
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Copeland, J., Nasiadka, A., Dietrich, B. et al. Patterning of the Drosophila embryo by a homeodomain-deleted Ftz polypeptide. Nature 379, 162–165 (1996). https://doi.org/10.1038/379162a0
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DOI: https://doi.org/10.1038/379162a0
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