Related Experiment Video
Updated: Sep 6, 2025

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
Published on: November 16, 2016
Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology
Carolyn E Mills1, Curt Waltmann2, Andre G Archer3
1Department of Chemical and Biological Engineering, Northwestern University, Evanston, IL, USA.
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.
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein....
Stringent Response in E. coli
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Bacterial Protein Maturation
Gene Regulation in Microbial Communities: Quorum Sensing
The Unfolded Protein Response

