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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Autores principales:	Fredarla S. Miller, Kathryn K. Crone, Matthew R. Jensen, Sudipta Shaw, William R. Harcombe, Mikael H. Elias, Michael F. Freeman
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/09ca9420fa074e35a3fbd77a88dcba46
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spelling	oai:doaj.org-article:09ca9420fa074e35a3fbd77a88dcba462021-12-02T17:42:05ZConformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis10.1038/s41467-021-25575-72041-1723https://doaj.org/article/09ca9420fa074e35a3fbd77a88dcba462021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25575-7https://doaj.org/toc/2041-1723Borosins 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.Fredarla S. MillerKathryn K. CroneMatthew R. JensenSudipta ShawWilliam R. HarcombeMikael H. EliasMichael F. FreemanNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Fredarla S. Miller Kathryn K. Crone Matthew R. Jensen Sudipta Shaw William R. Harcombe Mikael H. Elias Michael F. Freeman Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
description	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.
format	article
author	Fredarla S. Miller Kathryn K. Crone Matthew R. Jensen Sudipta Shaw William R. Harcombe Mikael H. Elias Michael F. Freeman
author_facet	Fredarla S. Miller Kathryn K. Crone Matthew R. Jensen Sudipta Shaw William R. Harcombe Mikael H. Elias Michael F. Freeman
author_sort	Fredarla S. Miller
title	Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
title_short	Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
title_full	Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
title_fullStr	Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
title_full_unstemmed	Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis
title_sort	conformational rearrangements enable iterative backbone n-methylation in ripp biosynthesis
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/09ca9420fa074e35a3fbd77a88dcba46
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Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis

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