PT  - JOURNAL ARTICLE
AU  - Aman S. Imani
AU  - Aileen R. Lee
AU  - Nisha Vishwanathan
AU  - Floris de Waal
AU  - Michael F. Freeman
TI  - Diverse Protein Architectures and α-<em>N</em>-Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters
AID  - 10.1101/2021.12.24.474128
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.12.24.474128
4099  - http://biorxiv.org/content/early/2021/12/24/2021.12.24.474128.short
4100  - http://biorxiv.org/content/early/2021/12/24/2021.12.24.474128.full
AB  - 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 1,600 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.Competing Interest StatementThe authors have declared no competing interest.