Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks

Yuqing Li, Yeying Ma, Yinzheng Xia, Tao Zhang, Shuaishuai Sun, Jiangtao Gao (), Hongwei Yao () and Huan Wang ()
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Yuqing Li: Nanjing University
Yeying Ma: Nanjing University
Yinzheng Xia: Nanjing University
Tao Zhang: Fujian Agriculture and Forestry University
Shuaishuai Sun: Nanjing University
Jiangtao Gao: Fujian Agriculture and Forestry University
Hongwei Yao: Soochow University
Huan Wang: Nanjing University

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract Cyclic peptide natural products represent an important class of bioactive compounds and clinical drugs. Enzymatic side-chain macrocyclization of ribosomal peptides is a major strategy developed by nature to generate these chemotypes, as exemplified by the superfamily of ribosomally synthesized and post-translational modified peptides. Despite the diverse types of side-chain crosslinks in this superfamily, the participation of histidine residues is rare. Herein, we report the discovery and biosynthesis of bacteria-derived tricyclic lanthipeptide noursin, which is constrained by a tri amino acid labionin crosslink and an unprecedented histidine-to-butyrine crosslink, named histidinobutyrine. Noursin displays copper-binding ability that requires the histidinobutyrine crosslink and represents the first copper-binding lanthipeptide. A subgroup of lanthipeptide synthetases, named LanKCHbt, were identified to catalyze the formation of both the labionin and the histidinobutyrine crosslinks in precursor peptides and produce noursin-like compounds. The discovery of the histidinobutyrine-containing lanthipeptides expands the scope of post-translational modifications, structural diversity and bioactivity of ribosomally synthesized and post-translational modified peptides.

Date: 2023
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DOI: 10.1038/s41467-023-38517-2

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