Decoding the stoichiometric composition and organisation of bacterial metabolosomes

Mengru Yang, Deborah M. Simpson, Nicolas Wenner, Philip Brownridge, Victoria M. Harman, Jay C. D. Hinton, Robert J. Beynon and Lu-Ning Liu ()
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Mengru Yang: University of Liverpool
Deborah M. Simpson: University of Liverpool
Nicolas Wenner: University of Liverpool
Philip Brownridge: University of Liverpool
Victoria M. Harman: University of Liverpool
Jay C. D. Hinton: University of Liverpool
Robert J. Beynon: University of Liverpool
Lu-Ning Liu: University of Liverpool

Nature Communications, 2020, vol. 11, issue 1, 1-11

Abstract: Abstract Some enteric bacteria including Salmonella have evolved the propanediol-utilising microcompartment (Pdu MCP), a specialised proteinaceous organelle that is essential for 1,2-propanediol degradation and enteric pathogenesis. Pdu MCPs are a family of bacterial microcompartments that are self-assembled from hundreds of proteins within the bacterial cytosol. Here, we seek a comprehensive understanding of the stoichiometric composition and organisation of Pdu MCPs. We obtain accurate stoichiometry of shell proteins and internal enzymes of the natural Pdu MCP by QconCAT-driven quantitative mass spectrometry. Genetic deletion of the major shell protein and absolute quantification reveal the stoichiometric and structural remodelling of metabolically functional Pdu MCPs. Decoding the precise protein stoichiometry allows us to develop an organisational model of the Pdu metabolosome. The structural insights into the Pdu MCP are critical for both delineating the general principles underlying bacterial organelle formation, structural robustness and function, and repurposing natural microcompartments using synthetic biology for biotechnological applications.

Date: 2020
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DOI: 10.1038/s41467-020-15888-4

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