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Structure and Biosynthesis of Crocagins: Polycyclic Posttranslationally Modified Ribosomal Peptides from Chondromyces crocatus
Author(s) -
Viehrig Konrad,
Surup Frank,
Volz Carsten,
Herrmann Jennifer,
Abou Fayad Antoine,
Adam Sebastian,
Köhnke Jesko,
Trauner Dirk,
Müller Rolf
Publication year - 2017
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201612640
Subject(s) - gene cluster , biosynthesis , gene , biochemistry , peptide , genome , computational biology , biology , ribosomal rna , chemistry , in vitro , amino acid
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.