Control of type III protein secretion using a minimal genetic system

Miryoung Song, David J. Sukovich, Luciano Ciccarelli, Julia Mayr, Jesus Fernandez-Rodriguez, Ethan A. Mirsky, Alex C. Tucker, D. Benjamin Gordon, Thomas C. Marlovits and Christopher A. Voigt ()
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Miryoung Song: Massachusetts Institute of Technology, Synthetic Biology Center
David J. Sukovich: Massachusetts Institute of Technology, Synthetic Biology Center
Luciano Ciccarelli: Center for Structural Systems Biology (CSSB), University Medical Center Hamburg-Eppendorf (UKE)
Julia Mayr: Center for Structural Systems Biology (CSSB), University Medical Center Hamburg-Eppendorf (UKE)
Jesus Fernandez-Rodriguez: Massachusetts Institute of Technology, Synthetic Biology Center
Ethan A. Mirsky: Massachusetts Institute of Technology, Synthetic Biology Center
Alex C. Tucker: Massachusetts Institute of Technology, Synthetic Biology Center
D. Benjamin Gordon: MIT-Broad Foundry, Broad Institute of MIT and Harvard
Thomas C. Marlovits: Center for Structural Systems Biology (CSSB), University Medical Center Hamburg-Eppendorf (UKE)
Christopher A. Voigt: Massachusetts Institute of Technology, Synthetic Biology Center

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract Gram-negative bacteria secrete proteins using a type III secretion system (T3SS), which functions as a needle-like molecular machine. The many proteins involved in T3SS construction are tightly regulated due to its role in pathogenesis and motility. Here, starting with the 35 kb Salmonella pathogenicity island 1 (SPI-1), we eliminated internal regulation and simplified the genetics by removing or recoding genes, scrambling gene order and replacing all non-coding DNA with synthetic genetic parts. This process results in a 16 kb cluster that shares no sequence identity, regulation or organizational principles with SPI-1. Building this simplified system led to the discovery of essential roles for an internal start site (SpaO) and small RNA (InvR). Further, it can be controlled using synthetic regulatory circuits, including under SPI-1 repressing conditions. This work reveals an incredible post-transcriptional robustness in T3SS assembly and aids its control as a tool in biotechnology.

Date: 2017
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DOI: 10.1038/ncomms14737

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