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  Identification, structure and function of the methyltransferase involved in the biosynthesis of the dithiolopyrrolone antibiotic xenorhabdin

Su, L., Huber, E. M., Westphalen, M., Gellner, J., Bode, E., Köbel, T., et al. (2024). Identification, structure and function of the methyltransferase involved in the biosynthesis of the dithiolopyrrolone antibiotic xenorhabdin. bioRxiv: the preprint server for biology, 2024.01.12.575338.

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 Creators:
Su, Li1, Author           
Huber, Eva M.2, Author
Westphalen, Margaretha2, Author
Gellner, Jonas2, Author
Bode, Edna1, Author           
Köbel, Tania3, Author
Grün, Peter1, Author
Alanjary, Mohammad M.2, Author
Glatter, Timo4, Author                 
Schindler, Daniel3, Author                 
Groll, Michael2, Author
Bode, Helge B.1, Author                 
Affiliations:
1Natural Product Function and Engineering, Department of Natural Products in Organismic Interactions, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266308              
2external, ou_persistent22              
3Core Facility MPG MAXGenesys DNAfoundry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266268              
4Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              

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 Abstract: Xenorhabdins (XRDs) are produced by Xenorhabdus species and are members of the dithiopyrrolone (DTP) class of natural products that have potent antibacterial, antifungal and anticancer activity. The amide moiety of their DTP core can be methylated or not to fine-tune the bioactivity properties. However, the enzyme responsible for the amide N-methylation remained elusive. Here, we identified and characterized the amide methyltransferase XrdM that is encoded nearly 600 kb away from the XRD gene cluster using proteomic analysis, methyltransferase candidate screening, gene deletion, and allied approaches. In addition, crystallographic analysis and site-directed mutagenesis proved that XrdM is completely distinct from the recently reported DTP methyltransferase DtpM, and that both have been tailored in a species-specific manner for DTP biosynthesis in Gram-negative/positive organisms. Our study expands the limited knowledge of post-NRPS amide methylation in DTP biosynthesis and reveals the evolution of two structurally completely different enzymes for the same reaction in different organisms.Competing Interest StatementThe authors have declared no competing interest.

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Language(s): eng - English
 Dates: 2024-01-12
 Publication Status: Issued
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 Table of Contents: -
 Rev. Type: No review
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Title: bioRxiv : the preprint server for biology
  Abbreviation : bioRxiv
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: 2024.01.12.575338 Start / End Page: - Identifier: ZDB: 2766415-6
CoNE: https://pure.mpg.de/cone/journals/resource/2766415-6