Structural and biochemical analyses of a lasso peptide natural product containing an unusual disulfide bond between consecutive cysteines

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ID: 328051
2026
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Abstract
Abstract Lasso peptides are a group of ribosomally synthesized and post-translationally modified peptides with a unique lariat topology. They have been classified into four classes based on disulfide bond patterns. In this study, we isolated a lasso peptide containing a disulfide bond in the macrocyclic ring, which is identical to jiangxilassin A. Analysis of the three-dimensional solution structure of this peptide suggested that the disulfide bond enhances the rigidity of the macrocyclic ring. To investigate whether the disulfide bond is required for enzymatic modification, we replaced either cysteine residue with serine. Upon heterologous expression, both mutants produced disulfide-linked dimers that retained macrolactam ring formation, dehydration, and methylation, although their production levels were substantially lower than the level observed for the wild type. These results indicate that the vicinal disulfide bond is not strictly required for these post-translational modifications but contributes to the efficient production of jiangxilassin A.
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openalex_W7211955660 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Atsushi Kawakami, Takeshi Tsunoda, Hiroyuki Kumeta, Chitose Maruyama, Yoshimitsu Hamano, Tohru Dairi, Yasushi Ogasawara
Journal bioscience biotechnology and biochemistry
Year 2026
DOI
10.1093/bbb/zbag135
URL
https://doi.org/10.1093/bbb/zbag135
Keywords Keywords not found

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