Journal
ACS CHEMICAL BIOLOGY
Volume 8, Issue 9, Pages 1888-1893Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb400189j
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Funding
- Australian Research Council [FF0883440, LP110201096]
- Diagnostic Technology P/L
- NIH [CA108874]
- Deutsche Forschungsgemeinschaft
- Bundesministerium fur Bildung und Forschung
- Australian Postgraduate Award
- Adrian Lee Travel Scholarship
- China Scholarship Council (CSC)
- Australian Research Council [LP110201096] Funding Source: Australian Research Council
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Many chemically complex cyanobacterial polyketides and nonribosomal peptides are of great pharmaceutical interest, but the levels required for exploitation are difficult to achieve from native sources. Here we develop a framework for the expression of these multifunctional cyanobacterial assembly lines in Escherichia coli using the lyngbyatoxin biosynthetic pathway, derived from a marine microbial assemblage dominated by the cyanobacterium Moorea producens. Heterologous expression of this pathway afforded high titers of both lyngbyatoxin A (25.6 mg L-1) and its precursor indolactam-V (150 mg L-1). Production, isolation, and identification of all expected chemical intermediates of lyngbyatoxin biosynthesis in E. coli also confirmed the previously proposed biosynthetic route, setting a solid chemical foundation for future pathway engineering. The successful production of the nonribosomal peptide lyngbyatoxin A in E. coli also opens the possibility for future heterologous expression, characterization, and exploitation of other cyanobacterial natural product pathways.
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