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.
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Authors | Benjamin Busch, Nico Ueberschaar, Yuki Sugimoto, Christian Hertweck |
Journal | Journal 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 |
PMID | 22799266
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Chromones
- Polyketide Synthases
- aureothin
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Topics |
- Chromones
(metabolism)
- Mutation
- Polyketide Synthases
(chemistry, genetics, metabolism)
- Protein Multimerization
- Protein Structure, Tertiary
- Streptomyces
(chemistry, genetics, metabolism)
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