We show that other proteins can be targeted to this intracellular filamentous arrangement. This cytoscaffold is constructed from a three-component system comprising a bacterial microcompartment shell protein and two complementary de novo coiled-coil peptides. The cytoscaffold has potential for the development of next-generation cell factories, where it could be used to organize enzyme pathways and metabolite transporters to enhance metabolic flux.Ībstract = "We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm. Finally, the shell-protein scaffold can be directed to the inner membrane of the cell, demonstrating how synthetic cellular organization can be coupled with spatial optimization through in-cell protein design. This is consistent with improved metabolic efficiency through enzyme colocation. Specifically, the enzymes pyruvate decarboxylase and alcohol dehydrogenase have been directed to the filaments leading to enhanced ethanol production in these engineered bacterial cells compared with those that do not produce the scaffold. We have developed a system for producing a supramolecular scaffold that permeates the entire Escherichia coli cytoplasm.
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