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O -linkedN -acetylglucosamine transferase (OGT) reversibly modifies serine and threonine residues of many intracellular proteins with a single β-O -linkedN -acetylglucosamine residue (O -GlcNAc), and has been implicated in insulin signaling, neurodegenerative disease, cellular stress response, and other important processes in mammals. OGT also glycosylates RNA polymerase II and various transcription factors, which suggests that it might be directly involved in transcriptional regulation. We report here that theDrosophila OGT is encoded by the Polycomb group (PcG) gene,super sex combs (sxc ). Furthermore, major sites ofO -GlcNAc modification on polytene chromosomes correspond to PcG protein binding sites. Our results thus suggest a direct role forO -linked glycosylation by OGT in PcG-mediated epigenetic gene silencing, which is important in developmental regulation, stem cell maintenance, genomic imprinting, and cancer. In addition, we observe rescue ofsxc lethality by a humanOgt cDNA transgene; thusDrosophila may provide an ideal model to study important functional roles of OGT in mammals.

Drosophila O -GlcNAc transferase (OGT) is encoded by the Polycomb group (PcG) gene, super sex combs ( sxc )