A Lanthipeptide-like N-Terminal Leader Region Guides Peptide Epimerization by Radical SAM Epimerases: Implications for RiPP Evolution

Sebastian W. Fuchs, Gerald Lackner, Brandon I. Morinaka, Yohei Morishita, Teigo Asai, Sereina Riniker, Jörn Piel

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Ribosomally synthesized and posttranslationally modified peptide natural products (RiPPs) exhibit diverse structures and bioactivities and are classified into distinct biosynthetic families. A recently reported family is the proteusins, with the prototype members polytheonamides being generated by almost 50 maturation steps, including introduction of d-residues at multiple positions by an unusual radical SAM epimerase. A region in the protein-like N-terminal leader of proteusin precursors is identified that is crucial for epimerization. It resembles a precursor motif previously shown to mediate interaction in thioether bridge-formation in class I lanthipeptide biosynthesis. Beyond this region, similarities were identified between proteusin and further RiPP families, including class I lanthipeptides. The data suggest that common leader features guide distinct maturation types and that nitrile hydratase-like enzymes are ancestors of several RiPP classes.

Original languageEnglish
Pages (from-to)12330-12333
Number of pages4
JournalAngewandte Chemie - International Edition
Volume55
Issue number40
DOIs
Publication statusPublished - 2016 Sep 26

Keywords

  • RiPPs
  • epimerases
  • lanthipeptides
  • leader peptides
  • proteusin

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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