Cellular identity in multicellular organisms is maintained by characteristic transcriptional networks, nutrient consumption, energy production and metabolite utilization. Integrating these cell-specific programs are epigenetic modifiers, whose activity is often dependent on nutrients and their metabolites to function as substrates and co-factors. Emerging data has highlighted the role of the nutrient-sensing enzyme O-GlcNAc transferase (OGT) as an epigenetic modifier essential in coordinating cellular transcriptional programs and metabolic homeostasis. OGT utilizes the end-product of the hexosamine biosynthetic pathway to modify proteins with O-linked β-D-N-acetylglucosamine (O-GlcNAc). The levels of the modification are held in check by the O-GlcNAcase (OGA). Studies from model organisms and human disease underscore the conserved function these two enzymes of O-GlcNAc cycling play in transcriptional regulation, cellular plasticity and mitochondrial reprogramming. Here, we review these findings and present an integrated view of how O-GlcNAc cycling may contribute to cellular memory and transgenerational inheritance of responses to parental stress. We focus on a rare human genetic disorder where mutant forms of OGT are inherited or acquired de novo. Ongoing analysis of this disorder, OGT- X-linked intellectual disability (OGT-XLID), provides a window into how epigenetic factors linked to O-GlcNAc cycling may influence neurodevelopment.
X-ray studies of zinc and nickel perchlorate hexahydrate, Zn(ClO4)2.6H2O and Ni(ClO4)2.6H2O, respectively, at different temperatures have been carried out to correlate the structural changes with phase transitions in the compounds. The crystals are pseudohexagonal (P63
mc), exhibiting a three-component orthorhombic twinning (Pmn21). At high temperatures a slight deviation of the b/a ratio of the three twinned orthorhombic cells from 31/2 results in a three-component splitting of each spot in the X-ray photograph, which on cooling to room temperature coalesce into single ones, thus restoring the original b/a ratio. The diffuse streaks disappear in the high-temperature photographs due to a decrease in the probability of error in repetition along the b axes of the three orthorhombic cells with temperature. A successful refinement of the heat-treated ordered Zn(ClO4)2.6H2O crystal verifies the continuous perchlorate–water arrangement and three-component twinning of the orthorhombic cell. Low-temperature X-ray photographs indicate no structural change.
Sequential one-pot per-O-acetylation–S-/O-glycosidation under neat condition, regioselective 4,6-O-arylidenation and sequential one-pot benzylidenation–acetylation of Mg(OTf)2as non-hygroscopic, recyclable catalyst are reported.
FeCl3 modulated excellent 1,2-trans selective glycosylations based on trichloroacetimidate glycosyl donors even in the presence of apparently silent C-2 protecting group, along with orthogonal glycosylation reactions are reported.
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