Near atmospheric carbon dioxide activates plant ubiquitin cross-linking.

ABSTRACT: Background Identifying CO₂-binding proteins is vital for our knowledge of CO₂-regulated molecular processes. The carbamate post-translational modification is a reversible CO₂-mediated adduct that can form on neutral N-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. We use ¹³C-NMR and TEO and identify ubiquitin as a plant CO₂-binding protein. Results We observe the carbamate post-translational modification on the Arabidopsis thaliana ubiquitin ε-amino groups of lysines 6, 33, and 48. We show that biologically relevant near atmospheric PCO₂ levels increase ubiqu

SUBMITTER: Gannon HG 

PROVIDER: S-EPMC10319984 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature