Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis

Borosins are ribosomally encoded and posttranslationally modified peptide (RiPP) natural products featuring amide-backbone α-N-methylation. Here, the authors report the discovery and characterization of type IV borosin ‘split’ pathways encoding distinct, separate α-N-methyltransferases and precursor...

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Auteurs principaux: Fredarla S. Miller, Kathryn K. Crone, Matthew R. Jensen, Sudipta Shaw, William R. Harcombe, Mikael H. Elias, Michael F. Freeman
Format: article
Langue:EN
Publié: Nature Portfolio 2021
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Accès en ligne:https://doaj.org/article/09ca9420fa074e35a3fbd77a88dcba46
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Résumé:Borosins are ribosomally encoded and posttranslationally modified peptide (RiPP) natural products featuring amide-backbone α-N-methylation. Here, the authors report the discovery and characterization of type IV borosin ‘split’ pathways encoding distinct, separate α-N-methyltransferases and precursor peptide substrates.