King Lab

We explore how bacteria sense and respond to metabolites.  

Bacteria have an enormous impact on humans. For example, infectious diseases cause roughly a third of deaths worldwide. Further, bacteria-based biotechnologies provide promising opportunities for developing a more sustainable economy. However, advancing these areas requires uncovering new aspects of bacterial physiology. One such frontier involves deciphering how bacteria communicate using chemical messages, in the form of metabolites, to adapt to their changing environments.

In the King lab, we are unraveling how bacteria sense reactive metabolites. Our interest in reactive metabolites stems from the fact that they can form unique covalent adducts with protein residues, thereby serving as a chemical switch to regulate protein function. We focus our studies on modifications that can spontaneously revert, making their abundance on proteins responsive to local metabolite levels - an important requirement for sensing. An often-overlooked class of metabolites that exemplify this behaviour are the essential biological gases, CO₂ and O₂. These gases are known to trigger adaptive responses within certain pathogens and bacteria that are used in biotechnology applications, such as cyanobacteria that can capture CO₂ from the atmosphere. Our research on biological gas sensing is focused on two main areas:

1) Exploring protein carboxylation as a biochemical mechanism in CO₂ sensing.

2) Characterizing the role of reversible protein oxidation in redox sensing.

Through exploring these areas, we aim to generate knowledge that contributes toward developing: (1) next-generation antibiotics, and (2) sustainable biotechnologies that help mitigate climate change and promote a green economy.

For more information, please visit our research lab website.



Lab Room:

SSB 7166

Lab Phone: 

(778) 782-3904

Lab Website:

Selected Publications

  • King D.T., Zhu S., Hardie D.B., Serrano-Negrón J.E., Madden Z., Kolappan S., Vocadlo D.J. Chemoproteomic identification of CO₂-dependant lysine carboxylation in proteins. Nat. Chem. Biol. 18: 782-791 (2022)
  • King D.T., Serrano-Negrón J.E., Zhu Y., Moore C.L., Shoulders M.D., Foster L.J., Vocadlo D.J. Thermal proteome profiling reveals the O-GlcNAc-dependent meltome. J. Am. Chem. Soc. 144(9): 3833-3842 (2022)
  • Escobar E.E.*, King D.T.*, Serrano-Negrón J.E., Alteen M.G., Vocadlo D.J., Brodbelt J.S. Precision mapping of O-linked N-acetylglucosamine sites in proteins using ultraviolet photodissociation mass spectrometry. J. Am. Chem. Soc. 142: 11569-11577 (2020)

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