20-hydroxyecdysone stimulates tissue-specific yolk-protein gene transcription in both male and female Drosophila.

The yolk polypeptides of Drosophila are normally synthesized in the fat body and ovarian follicle cells of adult females. In response to 20-hydroxyecdysone males synthesize yolk polypeptides. The actual level of yolk polypeptides synthesized in males is not always a direct reflection of the YP-transcripts present. Initially YP-transcripts are efficiently translated into polypeptides whereas later they are not and the YP-transcripts can have a half-life of less than 8 h in males. We suggest that the expression of the genes coding for the yolk polypeptides in males may be regulated at transcriptional and translational levels. Treatment of females with 20-hydroxyecdysone leads to a transient increase in YP-transcript accumulation, but the response is difficult to assess in whole flies due to the high variability in transcript levels during normal development. Analysing the response to 20-hydroxyecdysone at the level of specific tissues shows that transcript accumulation is dramatically increased in body walls (fat-body cells, epidermis and oenocytes) of both males and females. Gut, Malpighian tubules, testis and ovaries are not affected. Treatment of females with 20-hydroxyecdysone followed by measuring YP-transcript accumulation over the next 24 h in ovaries and body walls separately, confirms that only body walls respond to the hormone. There is an increase in yolk-polypeptide synthesis during the period of increased YP-transcript accumulation in females. We conclude that the response of the YP-genes to 20-hydroxyecdysone is tissue-, but not sex-specific.