V.L. Linthwaite
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.
Authors
J.M. Janus
Dr Adrian Brown a.p.brown@durham.ac.uk
Experimental Officer
D. Wong-Pascua
Professor Ann O'Donoghue annmarie.odonoghue@durham.ac.uk
Professor
A. Porter
A. Treumann
Professor David Hodgson d.r.w.hodgson@durham.ac.uk
Professor
Professor Martin Cann m.j.cann@durham.ac.uk
Professor
Abstract
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.
Citation
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 |
Journal | Nature Communications |
Publisher | Nature Research |
Peer Reviewed | Peer Reviewed |
Volume | 9 |
Article Number | 3092 |
DOI | https://doi.org/10.1038/s41467-018-05475-z |
Public URL | https://durham-repository.worktribe.com/output/1327305 |
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This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
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