Functional and Genetic Characterization of the Oligomerization and DNA Binding Properties of the Drosophila Doublesex Proteins

摘要: The doublesex (dsx) gene of Drosophila melanogaster encodes both male-specific (DSXM) and female-specific (DSXF) polypeptides, which are required for normal differentiation numerous sexually dimorphic somatic traits. DSX polypeptides transcription factors have been shown previously to bind through a zinc finger-like domain specific sites in an enhancer regulating sex-specific expression yolk protein genes. We determined the consensus target sequence this DNA binding be palindromic (A)(G)NNAC(T)(A) A(A)(T)GTNN(T)(C) composed two half-sites around central (A/T) base pair. As predicted by symmetric nature site, we found that proteins exist as dimers vivo mapped independent dimerization domains yeast two-hybrid method; one non-sex-specific amino-terminal region includes partially carboxy-terminal male female polypeptides. further identified missense mutation eliminates dsx function flies, same prevents DSXF system, indicating critical role vivo.