Structure and Biosynthesis of Crocagins

Polycyclic Posttranslationally Modified Ribosomal Peptides from Chondromyces crocatus

verfasst von: Konrad Viehrig, Frank Surup, Carsten Volz, Jennifer Herrmann, Antoine Abou Fayad, Sebastian Adam, Jesko Köhnke, Dirk Trauner, Rolf Müller
Abstract: Secondary metabolome mining efforts in the myxobacterial multiproducer of natural products, Chondromyces crocatus Cm c5, resulted in the isolation and structure elucidation of crocagins, which are novel polycyclic peptides containing a tetrahydropyrrolo[2,3-b]indole core. The gene cluster was identified through an approach combining genome analysis, targeted gene inactivation in the producer, and in vitro experiments. Based on our findings, we developed a biosynthetic scheme for crocagin biosynthesis. These natural products are formed from the three C-terminal amino acids of a precursor peptide and thus belong to a novel class of ribosomally synthesized and post-translationally modified peptides (RiPPs). We demonstrate that crocagin A binds to the carbon storage regulator protein CsrA, thereby inhibiting the ability of CsrA to bind to its cognate RNA target.
Externe Organisation(en): Universität des Saarlandes
Helmholtz-Zentrum für Infektionsforschung GmbH (HZI)
Ludwig-Maximilians-Universität München (LMU)
Typ: Artikel
Journal: Angewandte Chemie - International Edition
Band: 56
Seiten: 7407-7410
Anzahl der Seiten: 4
ISSN: 1433-7851
Publikationsdatum: 09.06.2017
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Katalyse, Allgemeine Chemie
Elektronische Version(en): https://doi.org/10.1002/anie.201612640 (Zugang: Geschlossen)

BibTeX

@article{a730ae34508e43bdbd8c7b031c782183,
title = "Structure and Biosynthesis of Crocagins: Polycyclic Posttranslationally Modified Ribosomal Peptides from Chondromyces crocatus",
abstract = "Secondary metabolome mining efforts in the myxobacterial multiproducer of natural products, Chondromyces crocatus Cm c5, resulted in the isolation and structure elucidation of crocagins, which are novel polycyclic peptides containing a tetrahydropyrrolo[2,3-b]indole core. The gene cluster was identified through an approach combining genome analysis, targeted gene inactivation in the producer, and in vitro experiments. Based on our findings, we developed a biosynthetic scheme for crocagin biosynthesis. These natural products are formed from the three C-terminal amino acids of a precursor peptide and thus belong to a novel class of ribosomally synthesized and post-translationally modified peptides (RiPPs). We demonstrate that crocagin A binds to the carbon storage regulator protein CsrA, thereby inhibiting the ability of CsrA to bind to its cognate RNA target.",
keywords = "biosynthesis, inhibitors, myxobacteria, natural products, RiPPs",
author = "Konrad Viehrig and Frank Surup and Carsten Volz and Jennifer Herrmann and {Abou Fayad}, Antoine and Sebastian Adam and Jesko K{\"o}hnke and Dirk Trauner and Rolf M{\"u}ller",
year = "2017",
month = jun,
day = "9",
doi = "10.1002/anie.201612640",
language = "English",
volume = "56",
pages = "7407--7410",
journal = "Angewandte Chemie - International Edition",
issn = "1433-7851",
publisher = "John Wiley and Sons Ltd",
number = "26",
}