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

Gannon, Harry G; Riaz-Bradley, Amber; Cann, Martin J

Abstract

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 Arabidopsis nucleoside diphosphate kinase (AtNDK1). We demonstrate that altered side chain reactivity at K9 is deleterious for AtNDK1 structure and catalytic function, but that CO2 does not impact catalysis. We show that nucleotide substrate removes CO2 from AtNDK1, and the carbamate PTM is functionless within the detection limits of our experiments. The AtNDK1 K9 PTM is the first demonstration of a functionless carbamate. In light of this finding, we speculate that non-functionality is a possible feature of the many newly identified carbamate PTMs.

Citation

Gannon, H. G., Riaz-Bradley, A., & Cann, M. J. (2024). A Non-Functional Carbon Dioxide-Mediated Post-Translational Modification on Nucleoside Diphosphate Kinase of Arabidopsis thaliana. International Journal of Molecular Sciences, 25(2), Article 898. https://doi.org/10.3390/ijms25020898

• Journal Article Type: Article
• Acceptance Date: Jan 10, 2024
• Online Publication Date: Jan 11, 2024
• Publication Date: Jan 2, 2024
• Deposit Date: Mar 26, 2024
• Publicly Available Date: Mar 26, 2024
• Journal: International journal of molecular sciences
• Print ISSN: 1661-6596
• Electronic ISSN: 1422-0067
• Publisher: MDPI
• Peer Reviewed: Peer Reviewed
• Volume: 25
• Issue: 2
• Article Number: 898
• DOI: https://doi.org/10.3390/ijms25020898
• Public URL: https://durham-repository.worktribe.com/output/2192780
• PMID: 38255974