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• W2890680797 endingPage "2056" @default.
• W2890680797 startingPage "2050" @default.
• W2890680797 abstract "Lasso peptides are natural products belonging to the family of ribosomally synthesized and posttranslationally modified peptides (RiPPs) and are defined by their unique topology. Even though lasso peptide biosynthetic gene clusters are found in many different kinds of bacteria, most of the hitherto studied lasso peptides were of proteobacterial or actinobacterial origin. Despite this, no E. coli-based production system has been reported for actinobacterial lasso peptides, while there are numerous examples of this for proteobacterial lasso peptides. Here, a heterologous production system of the lasso peptide chaxapeptin was established in E. coli. Chaxapeptin, originally isolated from Streptomyces leeuwenhoekii strain C58, is closely related to the lasso peptide sungsanpin (produced by a marine Streptomyces sp.) and shares its inhibitory activity against cell invasion by the human lung cancer cell line A549. Our production system not only allowed isolation of the mature lasso peptide outside of the native producer with a yield of 0.1 mg/L (compared to 0.7 mg/L from S. leeuwenhoekii) but also was used for a mutational study to identify residues in the precursor peptide that are important for biosynthesis. In addition to these experiments, the stability of chaxapeptin against thermal denaturation and proteases was assessed." @default.
• W2890680797 created "2018-09-27" @default.
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• W2890680797 date "2018-09-04" @default.
• W2890680797 modified "2023-10-17" @default.
• W2890680797 title "Investigation of the Biosynthesis of the Lasso Peptide Chaxapeptin Using an <i>E. coli-</i>Based Production System" @default.
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• W2890680797 doi "https://doi.org/10.1021/acs.jnatprod.8b00392" @default.
• W2890680797 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30178995" @default.
• W2890680797 hasPublicationYear "2018" @default.
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