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.
Dr Adrian Brown firstname.lastname@example.org
Professor Ann O'Donoghue email@example.com
Professor David Hodgson firstname.lastname@example.org
Professor Martin Cann email@example.com
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. https://doi.org/10.1038/s41467-018-05475-z
|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|
|Peer Reviewed||Peer Reviewed|
Published Journal Article
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