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The identification of carbon dioxide mediated protein post-translational modifications

Author

Listed:
  • Victoria L. Linthwaite

    (Department of Biosciences, Durham University
    Biophysical Sciences Institute, Durham University)

  • Joanna M. Janus

    (Department of Biosciences, Durham University
    Biophysical Sciences Institute, Durham University)

  • Adrian P. Brown

    (Department of Biosciences, Durham University
    Biophysical Sciences Institute, Durham University)

  • David Wong-Pascua

    (Department of Chemistry, Durham University)

  • AnnMarie C. O’Donoghue

    (Biophysical Sciences Institute, Durham University
    Department of Chemistry, Durham University
    Centre for Sustainable Chemical Processes, Durham University)

  • Andrew Porter

    (NUPPA, The Protein Facility, Newcastle University, Cookson Building)

  • Achim Treumann

    (NUPPA, The Protein Facility, Newcastle University, Cookson Building)

  • David R. W. Hodgson

    (Biophysical Sciences Institute, Durham University
    Department of Chemistry, Durham University
    Centre for Sustainable Chemical Processes, Durham University)

  • Martin J. Cann

    (Department of Biosciences, Durham University
    Biophysical Sciences Institute, Durham University)

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.

Suggested Citation

  • Victoria L. Linthwaite & Joanna M. Janus & Adrian P. Brown & David Wong-Pascua & AnnMarie C. O’Donoghue & Andrew Porter & Achim Treumann & David R. W. Hodgson & Martin J. Cann, 2018. "The identification of carbon dioxide mediated protein post-translational modifications," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-05475-z
    DOI: 10.1038/s41467-018-05475-z
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    Cited by:

    1. Alejandra Guillén-García & Savannah E. R. Gibson & Caleb J. C. Jordan & Venkata K. Ramaswamy & Victoria L. Linthwaite & Elizabeth H. C. Bromley & Adrian P. Brown & David R. W. Hodgson & Tim R. Blower , 2022. "Allophycocyanin A is a carbon dioxide receptor in the cyanobacterial phycobilisome," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    2. M. Águila Ruiz-Sola & Serena Flori & Yizhong Yuan & Gaelle Villain & Emanuel Sanz-Luque & Petra Redekop & Ryutaro Tokutsu & Anika Küken & Angeliki Tsichla & Georgios Kepesidis & Guillaume Allorent & M, 2023. "Light-independent regulation of algal photoprotection by CO2 availability," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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