One of the goals of synthetic biology is to engineer metabolic pathways to produce valuable chemical compounds and biofuels. To gain economic advantage over abiotic processes, metabolically engineered processes must attain high fluxes, sustain high yields, and have minimal effect on host growth rates. Major obstacles that must be overcome for the use of synthetic metabolic pathways include diffusion limitations, alternative metabolic routes, toxic intermediates, and inhibitory products. To avoid these problems in their own metabolic pathways, bacteria use bacterial microcompartments (BMCs), organelles composed entirely of protein that contain cargo proteins, functionally related enzymes and auxiliary proteins, within a proteinaceous shell. The ability to group enzymes in a BMC shell that regulates substrate and product transport is a promising tool for synthetic biology. However, knowledge of BMC cargo protein localization mechanisms is unknown, but necessary for the development of BMCs as nanocontainers for biosynthesis or biocatalysis. This study sought to optimize heterologous expression of of ethanolamine utilization (Eut) BMC cargo proteins with the objective of studying interactions between BMC shell proteins and cargo proteins using in vitro pull-down experiments. Results from this study will inform future work on engineering BMCs for synthetic biology applications.
This research was supported by the Undergraduate Research Opportunities Program (UROP).
Dahlgren, Kelsey; Bloch, Sarah; Perdue, Sarah; Schmidt-Dannert, Claudia.
Identification of Specific Cargo and Shell Protein Binding Partners in Eut BMCs.
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