Post translational Modifications (PTMs) play a major role in regulating cell signaling and communication, enzymatic activity, protein-protein interactions, protein localization, protein turnover, cell and DNA repair. The study of post-translational modification (PTM) of proteins and their major biological functions inside the cell is a critical question in the understanding biological function and the development of new medicines. Hydroxybutyrylation of lysine residues in histone proteins has been identified recently. Zhao (2016) and co-workers were able to show the direct coupling of the 3-hydroxybutyrate lysine (Kbhb) modification with the gene expression. This demonstrated a connection between metabolism, epigenetics and gene expression, and opens up a gateway to study in-depth, how cell metabolism controls the gene expression and vice versa. To study the PTM in depth, it is critical to obtain homogeneously modified proteins. Due to the complexity, technical challenges and inefficiency, it is difficult to obtain proteins with post-translationally modified form using total synthesis or peptide synthesis. Here we report the synthesis of Nε-3-hydroxybutyryl Lysine (Kbhb) and genetic encoding using an aminoacyl-tRNA synthetase (aaRS)/tRNA system. This allows for the production of proteins containing the site-specifically incorporated lysine PTM. The ability to obtain a homogenous composition of proteins with the post-translationally modified form, which is focused site specifically will greatly enable further studies directed at understanding the biological function of these PTMs.

Synthesis and the genetic encoding of Nε-3-hydroxybutyryl lysine: Novel post translational modification

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.