ArticleChembiochem : a European journal of chemical biology2020
Role of Two Exceptional trans Adenylation Domains and MbtH-like Proteins in the Biosynthesis of the Nonribosomal Peptide WS9324A from Streptomyces calvus ATCC 13382.
Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 39 citations in OpenAlex.
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- Herbicolin A production and its modulation by quorum sensing in a Pantoea agglomerans rhizobacterium bioactive against a broad spectrum of plant-pathogenic fungi.Microbial biotechnology · 2023Article
- Identification and heterologous expression of the globomycin biosynthetic gene cluster.Synthetic and systems biotechnology · 2023Article
- A genetic tool to express long fungal biosynthetic genes.Fungal biology and biotechnology · 2023Article
- Discovery of unusual dimeric piperazyl cyclopeptides encoded by aProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Aminoacyl chain translocation catalysed by a type II thioesterase domain in an unusual non-ribosomal peptide synthetase.Nature communications · 2022Article
- Role of Two Exceptional trans Adenylation Domains and MbtH-like Proteins in the Biosynthesis of the Nonribosomal Peptide WS9324A from Streptomyces calvus ATCC 13382.Chembiochem : a European journal of chemical biology · 2020Article
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4 authors at 2 institutions in 2 countries.
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Abstract
Nonribosomal peptide synthetases (NRPS) are organized in a modular arrangement. Usually, the modular order corresponds to the assembly of the amino acids in the respective peptide, following the collinearity rule. The WS9326A biosynthetic gene cluster from Streptomyces calvus shows deviations from this rule. Most interesting is the presence of two trans adenylation domains that are located downstream of the modular NRPS arrangement. Adenylation domains are responsible for the activation of their respective amino acids. In this study, we confirmed the involvement of the trans adenylation domains in WS9326A biosynthesis by performing gene knockout experiments and by observing the selective adenylation of their predicted amino acid substrates in vitro. We conclude that the trans adenylation domains are essential for WS9326A biosynthesis. Moreover, both adenylation domains are observed to have MbtH-like protein dependency. Overall, we conclude that the trans adenylation domains are essential for WS9326A biosynthesis.
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