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Autocatalytic backbone N-methylation in a family of ribosomal peptide natural products
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Autocatalytic backbone N-methylation in a family of ribosomal peptide natural products
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Journal Article
Autocatalytic backbone N-methylation in a family of ribosomal peptide natural products
2017
Overview
Characterization of the gene cluster for omphalotin biosynthesis reveals that they are ribosomally synthesized peptides whose internal α-
N
-methyl groups are installed by a methyltransferase fused to the precursor peptide substrate.
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.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
