Two Drosophila genes (DG1 and DG2) encoding products related to cGMP-dependent protein kinase were isolated, showing 55% and 64% amino acid identity to the bovine lung enzyme, respectively.
The isolation of two Drosophila genes homologous to mammalian cGMP-dependent protein kinase provides a genetic model for studying cyclic nucleotide signaling.
Two Drosophila genes encoding products related to cGMP-dependent protein kinase have been isolated by cross-hybridization to a Drosophila cAMP-dependent protein kinase catalytic subunit gene. Both genes encode products with putative cGMP binding and kinase domains on the same polypeptide chain, as found for the prototypical bovine lung cGMP-dependent protein kinase. The deduced product of one gene (DG1; cytological position, 21D) is 14% larger than the bovine enzyme and differs substantially in sequence at the amino terminus, the region responsible in the bovine enzyme for dimerization. The second gene (DG2; cytological position, 24A) is transcribed into three major RNA species of different size. The largest (DG2; T1) and smallest (DG2;T3) RNAs encode overlapping polypeptides of similar sequence to the whole length of bovine lung cGMP-dependent protein kinase. The translation product of the third major RNA (DG2;T2) lacks sequences similar to those that constitute the dimerization and kinase inhibitory domains of the bovine enzyme. The percentage amino acid identity between DG1 or DG2 and bovine lung cGMP-dependent protein kinase is 55 and 64%, respectively. A common progenitor of the two cGMP-dependent protein kinase genes, DG1 and DG2, is strongly suggested by the conserved positions of introns in these genes.
Kalderon et al. (Thu,) reported a other. Two Drosophila genes (DG1 and DG2) encoding products related to cGMP-dependent protein kinase were isolated, showing 55% and 64% amino acid identity to the bovine lung enzyme, respectively.