Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module.

Benjamin Busch, Nico Ueberschaar, Yuki Sugimoto, Christian Hertweck

Leibniz Institute for Natural Product Research and Infection Biology, HKI, Jena, Germany.

Journal of the American Chemical Society 2012 Aug 1

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The course of the enigmatic iterative use of a polyketide synthase module was deduced from targeted domain inactivation in the aureothin assembly line. Mutational analyses revealed that the N-terminus of AurA is not involved in the iteration process, ruling out an ACP-ACP shuttle. Furthermore, an AurA(KS°, ACP°)-AurA(AT(0)) heterodimer proved to be nonfunctional, whereas aureothin production was restored in a ΔaurA mutant complemented with AurA(KS°)-AurA(ACP°). This finding supports a model according to which the ACP-bound polyketide intermediate is transferred back to the KS domain on the opposite PKS strand.

Citation

Benjamin Busch, Nico Ueberschaar, Yuki Sugimoto, Christian Hertweck. Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module. Journal of the American Chemical Society. 2012 Aug 1;134(30):12382-5