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Near atmospheric carbon dioxide activates plant ubiquitin cross-linking

Gannon, Harry G; Cann, Martin J

Near atmospheric carbon dioxide activates plant ubiquitin cross-linking Thumbnail


Harry G Gannon


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 ubiquitin conjugation dependent on lysine 6. We further demonstrate that CO2 increases the ubiquitin E2 ligase (AtUBC5) charging step via the transthioesterification reaction in which Ub is transferred from the E1 ligase active site to the E2 active site. Conclusions and general significance Therefore, plant ubiquitin is a CO2-binding protein, and the carbamate post-translational modification represents a potential mechanism through which plant cells can respond to fluctuating PCO2.

Journal Article Type Article
Online Publication Date Jun 22, 2023
Publication Date 2023
Deposit Date Jun 23, 2023
Publicly Available Date Jun 23, 2023
Journal BBA Advances
Print ISSN 2667-1603
Peer Reviewed Peer Reviewed
Volume 4
Article Number 100096
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Copyright Statement
This is an open access article distributed under the terms of the Creative Commons CC-BY license, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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