Authors
Sara Vasciaveo, Yechen Zhou, Yaoyu Ding, Charlotte K Hind, Á Tamás Gräff, Amy H Camp, J Mark Sutton, Sarah M Barry, Rachael Dickman
Published in
ACS chemical biology. Nov 05, 2026. Epub Nov 05, 2026.
Abstract
Sactipeptides are a class of ribosomally synthesised and post-translationally modified peptides (RiPPs), which have a cyclic topology formed by unique thioether crosslinks called sactionines. Sactionines are introduced by radical S-adenosylmethionine (rSAM) enzymes between cysteine residues and the α-carbon of other amino acids. Genome sequencing has revealed many putative sactipeptide biosynthetic gene clusters; however, few sactipeptides have been isolated and characterised. Here, we use genome mining to identify a novel sactipeptide from Bacillus smithii. The novel sactipeptide, named smithiosin, was extracted from the industrially important thermophile B. smithii and characterised as a novel homologue of the previously characterised sactipeptide subtilosin A from B. subtilis. Furthermore, the smithiosin precursor peptide gene was heterologously expressed in the subtilosin A producer Bacillus subtilis 168 without knockout of the native precursor peptide, successfully leading to the production of both subtilosin A and smithiosin. This demonstrates for the first time that a non-native precursor peptide is able to outcompete the subtilosin A precursor for all of the native biosynthetic enzymes in B. subtilis, including the radical SAM enzyme AlbA. It also opens a potential new opportunity for screening non-native precursor peptides with the subtilosin A biosynthetic enzymes via heterologous expression in B. subtilis.
PMID:
42981563
Bibliographic data and abstract were imported from PubMed on 05 Nov 2026.
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