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

Abstract
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.
AuthorsBenjamin Busch, Nico Ueberschaar, Yuki Sugimoto, Christian Hertweck
JournalJournal of the American Chemical Society (J Am Chem Soc) Vol. 134 Issue 30 Pg. 12382-5 (Aug 01 2012) ISSN: 1520-5126 [Electronic] United States
PMID22799266 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Chromones
  • Polyketide Synthases
  • aureothin
Topics
  • Chromones (metabolism)
  • Mutation
  • Polyketide Synthases (chemistry, genetics, metabolism)
  • Protein Multimerization
  • Protein Structure, Tertiary
  • Streptomyces (chemistry, genetics, metabolism)

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