Vertex protein PduN tunes encapsulated pathway performance by dictating bacterial metabolosome morphology
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jun 29, 2022
- Source ID
- 10.1038/s41467-022-31279-3
Entities
People
- Alexander D. Jackson
- Andre G. Archer
- Carolyn E Mills
- Charlotte H. Abrahamson
- Curt Waltmann
- Danielle Tullman-Ercek
- Eric W. Roth
- Michael C Jewett
- Monica Olvera de la Cruz
- Niall M Mangan
- Nolan W Kennedy
- Sasha Shirman
Organizations
- Army Research Office
- Division of Electrical, Communications & Cyber Systems
- Division of Graduate Education
- Division of Materials Research
- National Institutes of Health
- Sherman Fairchild Foundation
- United States Department of Energy