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Post-translational modification of intracellular proteins with  O -linked  N -acetylglucosamine ( O -GlcNAc) catalysed by  O -GlcNAc transferase (OGT) has been linked to regulation of diverse cellular functions. OGT possesses a C-terminal glycosyltransferase catalytic domain and N-terminal tetratricopeptide repeats that are implicated in protein–protein interactions.  Drosophila  OGT ( Dm OGT) is encoded by  super sex combs  ( sxc ), mutants of which are pupal lethal. However, it is not clear if this phenotype is caused by reduction of  O -GlcNAcylation. Here we use a genetic approach to demonstrate that post-pupal  Drosophila  development can proceed with negligible OGT catalysis, while early embryonic development is OGT activity-dependent. Structural and enzymatic comparison between human OGT (hOGT) and  Dm OGT informed the rational design of  Dm OGT point mutants with a range of reduced catalytic activities. Strikingly, a severely hypomorphic OGT mutant complements  sxc  pupal lethality. However, the hypomorphic OGT mutant-rescued progeny do not produce F2 adults, because a set of  Hox  genes is de-repressed in F2 embryos, resulting in homeotic phenotypes. Thus, OGT catalytic activity is required up to late pupal stages, while further development proceeds with severely reduced OGT activity.

Dual functionality of O -GlcNAc transferase is required for Drosophila development