Issue 48, 2019

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

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

Supplementary files

Article information

Article type
Edge Article
Submitted
23 iyl 2019
Accepted
08 noy 2019
First published
04 dek 2019
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2019,10, 10979-10990

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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