Capicua is involved in Dorsal-mediated repression of zerknüllt expression in Drosophila embryo
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The maternal transcription factor Dorsal (Dl) functions as bothan activator and a repressor in a context-dependent manner tocontrol dorsal-ventral patterning in the Drosophila embryo. Previous studies have suggested that Dl is an intrinsic activatorand its repressive activity requires additional corepressors thatbind corepressor-binding sites near Dl-binding sites. However,the molecular identities of the corepressors have yet to beidentified. Here, we present evidence that Capicua (Cic) isinvolved in Dl-mediated repression in the zerknüllt (zen)ventral repression element (VRE). Computational and geneticanalyses indicate that a DNA-binding consensus sequence ofCic is highly analogous with previously identified corepressorbindingsequences and that Dl failed to repress zen expressionin lateral regions of cic mutant embryos. Furthermore,electrophoretic mobility shift assay (EMSA) shows that Cicdirectly interacts with several corepressor-binding sites in thezen VRE. These results suggest that Cic may function as acorepressor by binding the VRE.
Abstract
The maternal transcription factor Dorsal (Dl) functions as bothan activator and a repressor in a context-dependent manner tocontrol dorsal-ventral patterning in the Drosophila embryo. Previous studies have suggested that Dl is an intrinsic activatorand its repressive activity requires additional corepressors thatbind corepressor-binding sites near Dl-binding sites. However,the molecular identities of the corepressors have yet to beidentified. Here, we present evidence that Capicua (Cic) isinvolved in Dl-mediated repression in the zerknüllt (zen)ventral repression element (VRE). Computational and geneticanalyses indicate that a DNA-binding consensus sequence ofCic is highly analogous with previously identified corepressorbindingsequences and that Dl failed to repress zen expressionin lateral regions of cic mutant embryos. Furthermore,electrophoretic mobility shift assay (EMSA) shows that Cicdirectly interacts with several corepressor-binding sites in thezen VRE. These results suggest that Cic may function as acorepressor by binding the VRE.
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