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Heterologous Production and Structure Determination of a New Lanthipeptide Sinosporapeptin Using a Cryptic Gene Cluster in an Actinobacterium Sinosporangium siamense
Keita Saito , Keiichiro Mukai , Issara Kaweewan , Hiroyuki Nakagawa , Takeshi Hosaka , Shinya Kodani
J. Microbiol. 2023;61(6):641-648.   Published online June 12, 2023
DOI: https://doi.org/10.1007/s12275-023-00059-z
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AbstractAbstract
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.

Citations

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  • Heterologous biosynthesis of myxobacterial lanthipeptides melittapeptins
    Issara Kaweewan, Keiichiro Mukai, Pratchaya Rukthanapitak, Hiroyuki Nakagawa, Takeshi Hosaka, Shinya Kodani
    Applied Microbiology and Biotechnology.2024;[Epub]     CrossRef
  • Facile Method for Determining Lanthipeptide Stereochemistry
    Youran Luo, Shuyun Xu, Autumn M. Frerk, Wilfred A. van der Donk
    Analytical Chemistry.2024; 96(4): 1767.     CrossRef
  • Antimicrobial Peptides Derived from Bacteria: Classification, Sources, and Mechanism of Action against Multidrug-Resistant Bacteria
    Raynichka Mihaylova-Garnizova, Slavena Davidova, Yordan Hodzhev, Galina Satchanska
    International Journal of Molecular Sciences.2024; 25(19): 10788.     CrossRef

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