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Diverse Protein Architectures and α- N -Methylation Patterns Define Split Borosin RiPP Biosynthetic Gene Clusters
Open accessPublished version of a preprint
Abstract
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 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. Abstract Figure
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Imani, A. S., Lee, A. R., Vishwanathan, N., de Waal, F., & Freeman, M. F.
- Affiliations
- University of Minnesota (US)
- Wageningen University & Research (NL)
- Corresponding author
- Freeman, Michael F.
- Venue
- ACS Chemical Biology
- Publisher
- American Chemical Society (ACS)
- Published
- 2022-03-17
- Volume
- 17
- Issue
- 4
- Pages
- 908-917
- ISSN
- 1554-8929 (ISSN-L)
- 1554-8937
- PMC
- PMC9019853
- OpenAlex
- W4220697305
- Cited by
- 22
- References
- 1
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 6 · 2023: 4 · 2022: 5
- FWCI
- 2.99
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- Locations
- ACS Chemical Biology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R35 GM133475)
- Topics
- Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Microbial Natural Products and Biosynthesis
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Keywords
- ribosomally synthesized and post-translationally modified peptides, N-methyltransferase, Shewanella oneidensis, hidden Markov models, sequence similarity networks, natural product biosynthesis, protein architecture, proteolytic stability
- MeSH terms
- Biological Products, Multigene Family, Methylation, Peptides, Protein Processing, Post-Translational, Ribosomes
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