Dynamic posttranslational modifications (PTMs) are a major mechanism by which protein function is modulated. One often-overlooked PTM is protein O-GlcNAcylation. O-GlcNAc is added and removed by a single pair of proteins, OGT and OGA, respectively. O-GlcNAc transfer is the final step of the hexosamine biosynthetic pathway and as such its addition/removal likely informs upon a cell or organism’s overall nutritive state. Of particular interest is not only the ability to translate information regarding the nutritive state into the up or down-regulation of certain genes, but also to transmit this information to future generations. Using both in vitro biochemical approaches and the model organism C. elegans, I have generated data suggesting that O-GlcNAc cycling is uniquely poised to play a role in this transmission. Specifically, my data suggests that there is an interplay between OGT, OGA, O-GlcNAcylation and known regulators of gene expression. This work provides insight into the mechanism by which the nutritive state is translated into changes in transcriptional profiles at the level of the entire organism across generations.

Epigenetics and O-GlcNAc cycling: The relationship between dynamic O-linked glycosylation and transcriptional regulation

253rd National Meeting (2017)

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