Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology

Carolyn E. Mills, Curt Waltmann, Andre G. Archer, Nolan W. Kennedy, Charlotte H. Abrahamson, Alexander D. Jackson, Eric W. Roth, Sasha Shirman, Michael C. Jewett, Niall M. Mangan, Monica Olvera de la Cruz and Danielle Tullman-Ercek ()
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Carolyn E. Mills: Northwestern University
Curt Waltmann: Northwestern University
Andre G. Archer: Northwestern University
Nolan W. Kennedy: Northwestern University
Charlotte H. Abrahamson: Northwestern University
Alexander D. Jackson: Northwestern University
Eric W. Roth: Northwestern University Atomic and Nanoscale Characterization Experimental Center
Sasha Shirman: Northwestern University
Michael C. Jewett: Northwestern University
Niall M. Mangan: Northwestern University
Monica Olvera de la Cruz: Northwestern University
Danielle Tullman-Ercek: Northwestern University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract Engineering subcellular organization in microbes shows great promise in addressing bottlenecks in metabolic engineering efforts; however, rules guiding selection of an organization strategy or platform are lacking. Here, we study compartment morphology as a factor in mediating encapsulated pathway performance. Using the 1,2-propanediol utilization microcompartment (Pdu MCP) system from Salmonella enterica serovar Typhimurium LT2, we find that we can shift the morphology of this protein nanoreactor from polyhedral to tubular by removing vertex protein PduN. Analysis of the metabolic function between these Pdu microtubes (MTs) shows that they provide a diffusional barrier capable of shielding the cytosol from a toxic pathway intermediate, similar to native MCPs. However, kinetic modeling suggests that the different surface area to volume ratios of MCP and MT structures alters encapsulated pathway performance. Finally, we report a microscopy-based assay that permits rapid assessment of Pdu MT formation to enable future engineering efforts on these structures.

Date: 2022
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DOI: 10.1038/s41467-022-31279-3

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