Characterization and DNA-binding properties of GRF, a novel monomeric binding orphan receptor related to GCNF and betaFTZ-F1.
A PCR approach has been used to isolate, from Bombyx mori, a cDNA encoding a novel orphan receptor (GRF) that is most closely related to Bombyx betaFTZ-F1 and to the vertebrate germ cell nuclear factor. The major GRF mRNA is detected in most tissues as an 8-kb transcript whose amount follows the circulating ecdysteroid concentration with a delay. The expression pattern of GRF is similar to that of the Bombyx homologue of the Drosophila early-late gene DHR3, and precedes that of betaFTZ-F1 in all stages and tissues examined. The GRF protein is thus likely to be required in many tissues, but in a temporally restricted manner suggesting that GRF has a well-defined function in the ecdysteroid-induced transcription cascade. The GRF protein binds in vitro to a single oestrogen receptor half-site AGGTCA preceded by a 5'-TCA extension, and is therefore a potential co-regulator of the orphan receptors betaFTZ-F1 and DHR39.