Uptake and incorporation in pteridines of externally supplied GTP in normal and pigment-deficient eyes of Drosophila melanogaster.

Some aspects of the synthesis of drosopterins in the eyes of Drosophila melanogaster have been studied in flies with different levels of white gene expression. The activity of GTP cyclohydrolase was found to differ between wild-type and yellow-eyed mutants in vivo but not in vitro. To elucidate the uptake of substrate, we measured the removal of labeled GTP from the incubation medium by excised pupal eyes and followed the subsequent fate of this label. It was found that GTP was dephosphorylated to guanosine extracellularly before label was taken up by the eye tissue. The uptake was much lower in yellow and white eyes than in wild-type eyes, and in the latter, a considerable part of the label was present in pteridine compounds. The strain differences in the uptake of label seem to be due to different rates of intracellular utilization of guanine derivatives in pteridine synthesis. We suggest that this is caused by a hampered transport of precursor (possibly GTP) in white and zeste eyes through the membrane of red pigment granules.