Abstract
Peptide backbone N-methylation, as seen in cyclosporin A, has been considered to be exclusive to nonribosomal peptides. We have identified the first post-translationally modified peptide or protein harboring internal α-N-methylations through discovery of the genetic locus for the omphalotins, cyclic N-methylated peptides produced by the fungus Omphalotus olearius. We show that iterative autocatalytic activity of an N-methyltransferase fused to its peptide substrate is the signature of a new family of ribosomally encoded metabolites.
Highlights
This page was generated automatically upon download from the Eidgenössische Technische Hochschule (ETH) Zurich Research Collection
We have identified the first posttranslationally modified peptide or protein harboring internal α-N-methylations through discovery of the genetic locus for the omphalotins, cyclic N-methylated peptides produced by the fungus Omphalotus olearius
We show iterative autocatalytic activity of an N-methyltransferase fused to its peptide substrate is the signature of a new family of ribosomally encoded metabolites
Summary
This page was generated automatically upon download from the ETH Zurich Research Collection. Cyclic peptides such as the nematotoxic omphalotins from the basidiomycete O. olearius, in which 9 of the 12 backbone nitrogens are methylated, were assumed to be products of an NRPS6 (Fig. 1a).
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