Abstract
Grainyhead belongs to a recently identified group of transcription factors which share a 250-amino-acid domain required for binding to DNA and a carboxy-terminal dimerization domain. The activities of Grainyhead and other members of the family appear to be modulated so that they can participate in different developmental processes. We have examined the structure and function of mRNAs from the Drosophila grainyhead gene and demonstrated that alternate splicing is responsible for generating a neuroblast-specific isoform of the protein. A mutation which abolishes this isoform results in pupal and adult lethality. Reporter genes containing different Grainyhead binding sites exhibit tissue-specific patterns of expression that correlate with the Grainyhead isoforms, suggesting that the alternate splicing serves to alter the repertoire of target genes controlled in the neuroblasts.