Protein arginine deiminase 4 antagonizes methylglyoxal-induced histone glycation.

ABSTRACT: Protein arginine deiminase 4 (PAD4) facilitates the post-translational citrullination of the core histones H3 and H4. While the precise epigenetic function of this modification has not been resolved, it has been shown to associate with general chromatin decompaction and compete with arginine methylation. Recently, we found that histones are subjected to methylglyoxal (MGO)-induced glycation on nucleophilic side chains, particularly arginines, under metabolic stress conditions. These non-enzymatic adducts change chromatin architecture and the epigenetic landscape by competing with enzymatic modifications, as well as changing the overall biophysical properties of the fiber. Here, we report that PAD4 antagonizes histone MGO-glycation by protecting the reactive arginine sites, as well as by co

SUBMITTER: Zheng Q 

PROVIDER: S-EPMC7319962 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature