Reversible Histone Glycation Drives Disease-Associated Changes in Chromatin Architecture

Glycation is a covalent protein modification that accumulates in the cellular environment. Histone proteins are particularly susceptible to glycation due to their extremely long half-lives and nucleophilic disordered tails. Here, we performed ATAC-seq on 293T cells cultured in the presence or absence of 0.5mM methylglioxal, a reactive glycolytic intermediate, for 12 hours. We demonstrate that methylglioxal treatment is associated with changes in histone occupancy and chromatin architecture globally. 293T cells were cultured in the presence or absence of 0.5 mM MGO for 12 hours. ATAC-seq libraries were generated from 50,000 cells from each condition.