Interchenar retrotransfer of aureothin intermediates in an iterative polyketide synthase module.
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.
Leibniz Institute for Natural Product Research and Infection Biology, HKI, Jena, Germany.
Benjamin
B
Busch
Nico
N
Ueberschaar
Yuki
Y
Sugimoto
Christian
C
Hertweck
D002867:Chromones / Q000378:metabolism*; D009154:Mutation; D048630:Polyketide Synthases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D013302:Streptomyces / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D002867:Chromones; D048630:Polyketide Synthases; C012198:aureothin