Interaction of Vnd with the high-mobility protein, Dichaete, relieves Vnd–Gal4-mediated repression

<p><b>Copyright information:</b></p><p>Taken from "Contextual interactions determine whether the homeodomain protein, Vnd, acts as a repressor or activator"</p><p>Nucleic Acids Research 2005;33(1):1-12.</p><p>Published online 07 Jan 2005</p><p>PMCID:PMC546129.</p><p>© 2005, the authors © </p> The indicated Vnd–Gal4 fusion proteins were expressed transiently with increasing amounts of a pACT- expression plasmid. Expression of the VP16 activation domain fused to Dichaete from this construct relieves Vnd–Gal4-mediated repression of the luciferase reporter because of Vnd–Dichaete interactions. The baseline for each experimental series was set using pACT- with empty pBind. Because the Vnd domains have regulatory activity in the one-hybrid assay, the data are expressed as fold de-repression. Note that full de-repression of Vnd–Gal4 by Dichaete requires the presence of the homeodomain and sequences C-terminal to this domain

Additional file 1: of Increased Wnt and Notch signaling: a clue to the renal disease in Schimke immuno-osseous dysplasia?

Supplementary Methods, Tables, and Figures. (PDF 45904 kb