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Rucli S, Descostes N, Ermakova Y, Chitnavis U, Couturier J, Boskovic A, Boulard M. Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II. Genome biology 2025 26(1) 40128797
Abstract:
How reversible glycosylation of DNA-bound proteins acts on transcription remains scarcely understood. O-linked β-N-acetylglucosamine (O-GlcNAc) is the only known form of glycosylation modifying nuclear proteins, including RNA polymerase II (RNA Pol II) and many transcription factors. Yet, the regulatory function of the O-GlcNAc modification in mammalian chromatin remains unclear.
O-GlcNAc proteins:
YTDC1, MYC, PO5F1, PO2F1, TBP, SOX2, TYY1, TET1, TET2, SIN3A, KLF4, CTCF, HCFC1, NF2L1, SMAD3, ZN281, RAF1, BRD4, NRF1
Species: Mus musculus
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