Cloning and characterization of the Drosophila NOS gene (dNOS) revealed a 152 kDa protein with 43% identity to rat neuronal NOS and Ca2+/calmodulin-dependent activity.
The cloning and characterization of Drosophila NOS demonstrates remarkable structural and functional conservation of nitric oxide synthase between vertebrates and invertebrates.
Nitric oxide (NO) is an intercellular messenger involved with various aspects of mammalian physiology ranging from vasodilation and macrophage cytotoxicity to neuronal transmission. NO is synthesized from L-arginine by NO synthase (NOS). Here, we report the cloning of a Drosophila NOS gene, dNOS, located at cytological position 32B. The dNOS cDNA encodes a protein of 152 kDa, with 43% amino acid sequence identity to rat neuronal NOS. Like mammalian NOSs, DNOS protein contains putative binding sites for calmodulin, FMN, FAD, and NADPH. DNOS activity is Ca2+/calmodulin dependent when expressed in cell culture. An alternative RNA splicing pattern also exists for dNOS, which is identical to that for vertebrate neuronal NOS. These structural and functional observations demonstrate remarkable conservation of NOS between vertebrates and invertebrates.
Regulski et al. (Tue,) reported a other. dNOS cloning and characterization was evaluated on Molecular and biochemical characterization of dNOS. Cloning and characterization of the Drosophila NOS gene (dNOS) revealed a 152 kDa protein with 43% identity to rat neuronal NOS and Ca2+/calmodulin-dependent activity.