The functional characterization of the gene coding for O-linked β-N-acetylglucosaminidase (OGA) in Drosophila melanogaster

O-linked β-N-acetylglucosaminidase (OGA) is the enzyme responsible for removing the O-linked β-N-acetylglucosamine (O-GlcNAc) modification from serine and threonine residues of a variety of proteins, while its addition to protein targets is catalyzed by O-linked β-N-acetylglucosamine transferase (OGT). sxc/Ogt is essential in Drosophila melanogaster; however, it is unknown whether Oga is also essential in flies. I found that, in flies, a significant decrease in Oga transcript induced by RNAi knockdown is not lethal and that a nonsense mutation that putatively results in the translation of a C-terminally truncated version of OGA is viable when crossed to a deficiency known to span the Oga locus in the genome; however, reduced viability was observed when ubiquitously overexpressing two copies of Oga cDNA. Reduced expression of Oga and Ogt in Drosophila insulin-producing cells, via targeted RNAi expression with a dILP2-GAL4 driver, results in a slight increase and decrease, respectively, in male body weight.