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The identification of carbon dioxide mediated protein post-translational modifications

Linthwaite, V.L.; Janus, J.M.; Brown, A.P.; Wong-Pascua, D.; O’Donoghue, A.C.; Porter, A.; Treumann, A.; Hodgson, D.R.W.; Cann, M.J.

The identification of carbon dioxide mediated protein post-translational modifications Thumbnail


V.L. Linthwaite

J.M. Janus

D. Wong-Pascua

A. Porter

A. Treumann


Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein carbamates will significantly advance our understanding of cellular CO2 interactions.


Linthwaite, V., Janus, J., Brown, A., Wong-Pascua, D., O’Donoghue, A., Porter, A., …Cann, M. (2018). The identification of carbon dioxide mediated protein post-translational modifications. Nature Communications, 9, Article 3092.

Journal Article Type Article
Acceptance Date Jul 3, 2018
Online Publication Date Aug 6, 2018
Publication Date Aug 6, 2018
Deposit Date Jul 4, 2018
Publicly Available Date Aug 10, 2018
Journal Nature Communications
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 9
Article Number 3092


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