Diverse Protein Architectures and α- N-Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters

Aman S Imani, Aileen R Lee, Nisha Vishwanathan, Floris De Waal, Michael F. Freeman

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Borosins are ribosomally synthesized and post-translationally modified peptides (RiPPs) with α-N-methylations installed on the peptide backbone that impart unique properties like proteolytic stability to these natural products. The borosin RiPP family was initially reported only in fungi until our recent discovery and characterization of a Type IV split borosin system in the metal-respiring bacterium Shewanella oneidensis. Here, we used hidden Markov models and sequence similarity networks to identify over 1600 putative pathways that show split borosin biosynthetic gene clusters are widespread in bacteria. Noteworthy differences in precursor and α-N-methyltransferase open reading frame sizes, architectures, and core peptide properties allow further subdivision of the borosin family into six additional discrete structural types, of which five have been validated in this study.

Original languageEnglish (US)
Pages (from-to)908-917
Number of pages10
JournalACS Chemical Biology
Volume17
Issue number4
DOIs
StatePublished - Apr 15 2022

Bibliographical note

Funding Information:
This work was supported by the National Institute of General Medical Sciences (T32 GM008347 for A.R.L. and R35 GM133475 for M.F.F.) along with the University of Minnesota and the BioTechnology Institute.

Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.

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