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Issue 48, 2019
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Structure elucidation of the syringafactin lipopeptides provides insight in the evolution of nonribosomal peptide synthetases

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Abstract

Modular biosynthetic machineries such as polyketide synthases (PKSs) or nonribosomal peptide synthetases (NRPSs) give rise to a vast structural diversity of bioactive metabolites indispensable in the treatment of cancer or infectious diseases. Here, we provide evidence for different evolutionary processes leading to the diversification of modular NRPSs and thus, their respective products. Discovery of a novel lipo-octapeptide family from Pseudomonas, the virginiafactins, and detailed structure elucidation of closely related peptides, the cichofactins and syringafactins, allowed retracing recombinational diversification of the respective NRPS genes. Bioinformatics analyses allowed us to spot an evolutionary snapshot of these processes, where recombination occurred both within the same and between different biosynthetic gene clusters. Our systems feature a recent diversification process, which may represent a typical paradigm to variations in modular biosynthetic machineries.

Graphical abstract: Structure elucidation of the syringafactin lipopeptides provides insight in the evolution of nonribosomal peptide synthetases

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Publication details

The article was received on 23 Jul 2019, accepted on 08 Nov 2019 and first published on 04 Dec 2019


Article type: Edge Article
DOI: 10.1039/C9SC03633D
Chem. Sci., 2019,10, 10979-10990
  • Open access: Creative Commons BY-NC license
    All publication charges for this article have been paid for by the Royal Society of Chemistry

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    Structure elucidation of the syringafactin lipopeptides provides insight in the evolution of nonribosomal peptide synthetases

    S. Götze, J. Arp, G. Lackner, S. Zhang, H. Kries, M. Klapper, M. García-Altares, K. Willing, M. Günther and P. Stallforth, Chem. Sci., 2019, 10, 10979
    DOI: 10.1039/C9SC03633D

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