期刊
ACS CHEMICAL BIOLOGY
卷 8, 期 9, 页码 1888-1893出版社
AMER CHEMICAL SOC
DOI: 10.1021/cb400189j
关键词
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资金
- 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
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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