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Biosynthesis and engineering of the nonribosomal peptides with a C-terminal putrescine

Author

Listed:
  • Hanna Chen

    (Shandong University
    Linyi University)

  • Lin Zhong

    (Chinese Academy of Sciences)

  • Haibo Zhou

    (Shandong University)

  • Xianping Bai

    (Shandong University)

  • Tao Sun

    (Shandong University)

  • Xingyan Wang

    (Shandong University)

  • Yiming Zhao

    (Shandong University)

  • Xiaoqi Ji

    (Shandong University)

  • Qiang Tu

    (Chinese Academy of Sciences)

  • Youming Zhang

    (Shandong University
    Chinese Academy of Sciences)

  • Xiaoying Bian

    (Shandong University)

Abstract

The broad bioactivities of nonribosomal peptides rely on increasing structural diversity. Genome mining of the Burkholderiales strain Schlegelella brevitalea DSM 7029 leads to the identification of a class of dodecapeptides, glidonins, that feature diverse N-terminal modifications and a uniform putrescine moiety at the C-terminus. The N-terminal diversity originates from the wide substrate selectivity of the initiation module. The C-terminal putrescine moiety is introduced by the unusual termination module 13, the condensation domain directly catalyzes the assembly of putrescine into the peptidyl backbone, and other domains are essential for stabilizing the protein structure. Swapping of this module to another two nonribosomal peptide synthetases leads to the addition of a putrescine to the C-terminus of related nonribosomal peptides, improving their hydrophilicity and bioactivity. This study elucidates the mechanism for putrescine addition and provides further insights to generate diverse and improved nonribosomal peptides by introducing a C-terminal putrescine.

Suggested Citation

  • Hanna Chen & Lin Zhong & Haibo Zhou & Xianping Bai & Tao Sun & Xingyan Wang & Yiming Zhao & Xiaoqi Ji & Qiang Tu & Youming Zhang & Xiaoying Bian, 2023. "Biosynthesis and engineering of the nonribosomal peptides with a C-terminal putrescine," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42387-z
    DOI: 10.1038/s41467-023-42387-z
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