Near atmospheric carbon dioxide activates plant ubiquitin cross-linking

Gannon, Harry G; Cann, Martin J

doi:10.1016/j.bbadva.2023.100096

Cited by 1 publication

(1 citation statement)

References 57 publications

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“…However, typically, we have less evidence for the sensing mechanisms that respond directly to the gas. Signalling molecules that respond directly to CO 2 (or to the bicarbonate ion that is in a pHdependent equilibrium) include the Class III nucleotidylyl cyclases of animals, fungi, and prokaryotes [2], a subset of connexins (typified by Cx26) in mammals [13], receptor protein tyrosine phosphatase γ of mammals [14], ubiquitin in mammals and Arabidopsis [4,15], PII of Synechocystis sp. PCC 6803 [16], and PP2C phosphatases of plants and fungi [17].…”

Section: Introductionmentioning

confidence: 99%

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

Gannon,

Riaz-Bradley,

Cann

2024

IJMS

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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.

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