Details

Autor(en) / Beteiligte

• Zhao, Xiling
• van der Donk, Wilfred A.

Titel

Structural Characterization and Bioactivity Analysis of the Two-Component Lantibiotic Flv System from a Ruminant Bacterium

Ist Teil von

• Cell chemical biology, 2016-02, Vol.23 (2), p.246-256

Ort / Verlag

United States: Elsevier Ltd

Erscheinungsjahr

2016

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• The discovery of new ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) has greatly benefitted from the influx of genomic information. The lanthipeptides are a subset of this class of compounds. Adopting the genome-mining approach revealed a novel lanthipeptide gene cluster encoded in the genome of Ruminococcus flavefaciens FD-1, an anaerobic bacterium that is an important member of the rumen microbiota of livestock. The post-translationally modified peptides were produced via heterologous expression in Escherichia coli. Subsequent structural characterization and assessment of their bioactivity revealed features reminiscent of and distinct from previously reported lanthipeptides. The lanthipeptides of R. flavefaciens FD-1 represent a unique example within two-component lanthipeptides, consisting of a highly conserved α-peptide and a diverse set of eight β-peptides. [Display omitted] •Production of nine different lanthipeptides from an anaerobic ruminant bacterium•Novel example of substrate diversification in two-component lanthipeptides•Flavecin synthetase FlvM2 converts eight diverse peptides into polycyclic structures An unusual gene cluster from Ruminococcus flavefaciens contains 12 substrate and two lanthipeptide synthetase genes. The post-translationally modified peptides were produced in E. coli and comprise four structurally conserved lipid II binding peptides and eight structurally diverse β-peptides, some of which displayed synergistic antimicrobial activity.