A Non-Functional Carbon Dioxide-Mediated Post-Translational Modification on Nucleoside Diphosphate Kinase of .

The carbamate post-translational modification (PTM), formed by the nucleophilic attack of carbon dioxide by a dissociated lysine epsilon-amino group, is proposed as a widespread mechanism for sensing this biologically important bioactive gas. Here, we demonstrate the discovery and in vitro characterization of a carbamate PTM on K9 of nucleoside diphosphate kinase (NDK1). We demonstrate that altered side chain reactivity at K9 is deleterious for NDK1 structure and catalytic function, but that CO does not impact catalysis.

Near atmospheric carbon dioxide activates plant ubiquitin cross-linking.

Background Identifying CO-binding proteins is vital for our knowledge of CO-regulated molecular processes. The carbamate post-translational modification is a reversible CO-mediated adduct that can form on neutral -terminal α-amino or lysine ε-amino groups. Methods We have developed triethyloxonium ion (TEO) as a chemical proteomics tool to trap the carbamate post-translational modification on protein covalently.