Journal
CHEMISTRY & BIOLOGY
Volume 16, Issue 2, Pages 141-147Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2009.01.007
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Funding
- NIH of U.S [CA094426]
- National Natural Science Foundation of China [30525001, 90713012, 20832009]
- Ministry of Science and Technology of China [2006AA022185]
- Chinese Academy of Science [KJCX2-YWH08]
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Thiopeptides, with potent activity against various drug-resistant pathogens, contain a characteristic macrocyclic core consisting of multiple thiazoles, dehydroamino acids, and a 6-membered nitrogen heterocycle. Their biosynthetic pathways remain elusive, in spite of great efforts by in vivo feeding experiments. Here, cloning, sequencing, and characterization of the thiostrepton and siomycin A gene clusters unveiled a biosynthetic paradigm for the thiopeptide specific core formation, featuring ribosomally synthesized precursor peptides and conserved posttranslational modifications. The paradigm generality for thiopeptide biosynthesis was supported by genome mining and ultimate confirmation of the thiocillin I production in Bacillus cereus ATCC 14579, a strain that was previously unknown as a thiopeptide producer. These findings set the stage to accelerate the discovery of thiopeptides by prediction at the genetic level and to generate structural diversity by applying combinatorial biosynthesis methods.
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