Extensive Mutational Analysis of Modular-Iterative Mixed Polyketide Biosynthesis of Lankacidin in Streptomyces rochei
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概要
- 論文の詳細を見る
Extensive mutations of lankacidin synthase genes were carried out to analyze the modular-iterative mixed polyketide biosynthesis of lankacidin. Three ketoreductase domains (lkcC-KR, lkcF-KR1, and lkcF-KR2) were inactivated by in-frame deletion and site-directed mutagenesis of their active sites. The mutants ceased or diminished lankacidin production, indicating that the three KR domains are functional in lankacidin biosynthesis. However, all of the KR mutants failed to accumulate the expected unreduced metabolites. Mutational analysis of two tandemly aligned acyl carrier protein domains (lkcC-ACP1 and lkcC-ACP2) revealed that either ACP is sufficient for lankacidin production. Disruption and complementation experiments on three unique genes/domain (lkcD for acyltransferase, lkcB for dehydratase, and lkcC-MT for a C-methyltransferase domain) suggested that their gene products function iteratively during lankacidin biosynthesis.
- 社団法人 日本農芸化学会の論文
- 2009-12-23
著者
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ARAKAWA Kenji
Department of Chemistry, Box 351700, University of Washington
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KINASHI Haruyasu
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima Uni
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Kinashi Haruyasu
Dep. Of Molecular Biotechnology Graduate School Of Advanced Sciences Of Matter Hiroshima Univ.
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TATSUNO SATOSHI
Department of Radiology, Ichikawa General Hospital, Tokyo Dental College
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Arakawa Kenji
Dep. Of Molecular Biotechnology Graduate School Of Advanced Sciences Of Matter Hiroshima Univ.
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Kinashi Haruyasu
Department Of Molecular Biotechnology Graduate School Of Advanced Sciences Of Matter Hiroshima Unive
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Tatsuno Satoshi
Department Of Molecular Biotechnology Graduate School Of Advanced Sciences Of Matter Hiroshima Unive
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Arakawa Kenji
Department Of Chemistry Box 351700 University Of Washington
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Kinashi Haruyasu
Department Of Fermentation Technology Faculty Of Engineering Hiroshima University
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