| Title | Heterologous Production and Structure Determination of a New Lanthipeptide Sinosporapeptin Using a Cryptic Gene Cluster in an Actinobacterium Sinosporangium siamense |
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| Author | Keita Saito1, Keiichiro Mukai2,3, Issara Kaweewan4, Hiroyuki Nakagawa5, Takeshi Hosaka2,3, and Shinya Kodani1,4,6* |
| Address | 1Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka 422‑8529, Japan, 2Graduate School of Medicine, Science and Technology, Shinshu University, Nagano 399‑4598, Japan, 3Department of Biomolecular Innovation, Institute for Biomedical Sciences, Shinshu University, Nagano 399‑4598, Japan, 4Faculty of Agriculture, Shizuoka University, Shizuoka 422‑8529, Japan, 5Research Center for Advanced Analysis, Core Technology Research Headquarters, National Agriculture and Food Research Organization (NARO), Ibaraki 305‑8642, Japan, 6College of Agriculture, Academic Institute, Shizuoka University, Shizuoka 422‑8529, Japan |
| Bibliography | Journal of Microbiology, 61(6),641-648, 2023, |
| DOI | 10.1007/s12275-023-00059-z |
| Key Words | Heterologous expression · Lanthipeptide · Lipolanthine · Biosynthesis |
| Abstract | Lipolanthine is a subclass of lanthipeptide that has the modification of lipid moiety at the N-terminus. A cryptic biosynthetic gene cluster comprising four genes (sinA, sinKC, sinD, and sinE) involved in the biosynthesis of lipolanthine was identified in the genome of an actinobacterium Sinosporangium siamense. Heterologous coexpression of a precursor peptide coding gene sinA and lanthipeptide synthetase coding gene sinKC in the host Escherichia coli strain BL21(DE3) resulted in the synthesis of a new lanthipeptide, sinosporapeptin. It contained unusual amino acids, including one labionin and two dehydrobutyrine residues, as determined using NMR and MS analyses. Another coexpression experiment with two additional genes of decarboxylase (sinD) and N-acetyl transferase (sinE) resulted in the production of a lipolanthine-like modified sinosporapeptin. |