PuSH - Publication Server of Helmholtz Zentrum München: MbnC is not required for the formation of the N-terminal oxazolone in the methanobactin from <em>Methylosinus trichosporium</em> OB3b.

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Dershwitz, P.* ; Gu, W.* ; Roche, J.* ; Kang-Yun, C.S.* ; Semrau, J.D.* ; Bobik, T.A.* ; Fulton, B.* ; Zischka, H. ; DiSpirito, A.A.*

MbnC is not required for the formation of the N-terminal oxazolone in the methanobactin from Methylosinus trichosporium OB3b.

Appl. Environ. Microbiol. 88:e0184121 (2022)

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Methanobactins (MBs) are ribosomally synthesized and post-translationally modified peptides (RiPPs) produced by methanotrophs for copper uptake. The post-translational modification that define MBs is the formation of two heterocyclic groups with associated thioamines from X-Cys dipeptide sequences. Both heterocyclic groups in the MB from Methylosinus trichosporium OB3b (MB-OB3b) are oxazolone groups. The precursor gene for MB-OB3b, mbnA, which is part of a gene cluster that contains both annotated and unannotated genes. One of those unannotated genes, mbnC, is found in all MB operons, and in conjunction with mbnB, is reported to be involved in the formation of both heterocyclic groups in all MBs. To determine the function of mbnC, a deletion mutation was constructed in M. trichosporium OB3b, and the MB produced from the ΔmbnC mutant was purified and structurally characterized by UV-visible absorption spectroscopy, mass spectrometry and solution NMR spectroscopy. MB-OB3b from ΔmbnC was missing the C-terminal Met and also found to contain a Pro and a Cys in place of the pyrrolidiny-oxazolone-thioamide group. These results demonstrate MbnC is required for the formation of the C-terminal pyrrolidinyl-oxazolone-thioamide group from the Pro-Cys dipeptide, but not for the formation of the N-terminal 3-methylbutanol-oxazolone-thioamide group from the N-terminal dipeptide Leu-Cys. IMPORTANCE A number of environmental and medical applications have been proposed for MBs, including bioremediation of toxic metals, nanoparticle formation, as well as for the treatment of copper- and iron-related diseases. However, before MBs can be modified and optimized for any specific application, the biosynthetic pathway for MB production must be defined. The discovery that mbnC is involved in the formation of the C-terminal oxazolone group with associated thioamide but not for the formation of the N-terminal oxazolone group with associated thioamide in M. trichosporium OB3b suggests the enzymes responsible for post-translational modification(s) of the two oxazolone groups are not identical.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

Keywords Aerobic Methane Oxidation ; Chalkophore ; Methanobactin ; Methanotroph ; Ribosomally Synthesized And Posttranslational Modified Peptide; Thermodynamic Properties; Copper; Binding

ISSN (print) / ISBN 0099-2240

e-ISSN 1098-5336

Journal Applied and Environmental Microbiology

Quellenangaben Volume: 88, Issue: 2, Article Number: e0184121

Publisher American Society for Microbiology (ASM)

Publishing Place 1752 N St Nw, Washington, Dc 20036-2904 Usa

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Institute of Molecular Toxicology and Pharmacology (TOXI)

Grants ISU Bailey Research and Career Development award
Roy J. Carver Charitable Trust (Muscatine, IA, USA)
National Science Foundation
U.S. Department of Energy Office of Science