ArticleAngewandte Chemie (International ed. in English)2019
Loss of Single-Domain Function in a Modular Assembly Line Alters the Size and Shape of a Complex Polyketide.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Microbial communities associated with marine sponges from diverse geographic locations harbor biosynthetic novelty.Applied and environmental microbiology · 2024Article
- Novel Sources of Biodiversity and Biomolecules from Bacteria Isolated from a High Middle Ages Soil Sample in Palermo (Sicily, Italy).Microbiology spectrum · 2023Article
- Insights into azalomycin F assembly-line contribute to evolution-guided polyketide synthase engineering and identification of intermodular recognition.Nature communications · 2023Article
- Structural identification of pyridinopyrone compounds with anti-neuroinflammatory activity from streptomyces sulphureus DSM 40104.Frontiers in microbiology · 2023Article
- Genomic and Metabolomic Investigation of a Rhizosphere IsolateMolecules (Basel, Switzerland) · 2021Article
- Antimicrobial Activity and Identification of the Biosynthetic Gene Cluster of X-14952B FromFrontiers in microbiology · 2021Article
- Biosynthesis of the Nuclear Factor of Activated T Cells Inhibitor NFAT-133 inACS chemical biology · 2020Article
- Synthetic biology enabling access to designer polyketides.Current opinion in chemical biology · 2020Review
- Site directed mutagenesis as a precision tool to enable synthetic biology with engineered modular polyketide synthases.Synthetic and systems biotechnology · 2020Review
- Loss of Single-Domain Function in a Modular Assembly Line Alters the Size and Shape of a Complex Polyketide.Angewandte Chemie (International ed. in English) · 2019Article
Corrections and comments
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3 authors.
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Abstract
The structural wealth of complex polyketide metabolites produced by bacteria results from intricate, highly evolved biosynthetic programs of modular assembly lines, in which the number of modules defines the size of the backbone, and the domain composition controls the degree of functionalization. We report a remarkable case where polyketide chain length and scaffold depend on the function of a single β-keto processing domain: A ketoreductase domain represents a switch between diverging biosynthetic pathways leading either to the antifungal aureothin or to the nematicidal luteoreticulin. By a combination of heterologous expression, mutagenesis, metabolite analyses, and in vitro biotransformation we elucidate the factors governing non-colinear polyketide assembly involving module skipping and demonstrate that a simple point mutation in type I polyketide synthase (PKS) can have a dramatic effect on the metabolic profile. This finding sheds new light on possible evolutionary scenarios and may inspire future synthetic biology approaches.
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Registered trials
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