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Kang-Yun, C.S.* ; Liang, X.* ; Dershwitz, P.* ; Gu, W.* ; Schepers, A. ; Flatley, A. ; Lichtmannegger, J. ; Zischka, H. ; Zhang, L.* ; Lu, X.* ; Gu, B.* ; Ledesma, J.C.* ; Pelger, D.J.* ; DiSpirito, A.A.* ; Semrau, J.D.*

Evidence for methanobactin "Theft" and novel chalkophore production in methanotrophs: Impact on methanotrophic-mediated methylmercury degradation.

ISME J., DOI: 10.1038/s41396-021-01062-1 (2021)
DOI
: Verlagsversion online verfügbar 08/2022
Aerobic methanotrophy is strongly controlled by copper, and methanotrophs are known to use different mechanisms for copper uptake. Some methanotrophs secrete a modified polypeptide-methanobactin-while others utilize a surface-bound protein (MopE) and a secreted form of it (MopE*) for copper collection. As different methanotrophs have different means of sequestering copper, competition for copper significantly impacts methanotrophic activity. Herein, we show that Methylomicrobium album BG8, Methylocystis sp. strain Rockwell, and Methylococcus capsulatus Bath, all lacking genes for methanobactin biosynthesis, are not limited for copper by multiple forms of methanobactin. Interestingly, Mm. album BG8 and Methylocystis sp. strain Rockwell were found to have genes similar to mbnT that encodes for a TonB-dependent transporter required for methanobactin uptake. Data indicate that these methanotrophs "steal" methanobactin and such "theft" enhances the ability of these strains to degrade methylmercury, a potent neurotoxin. Further, when mbnT was deleted in Mm. album BG8, methylmercury degradation in the presence of methanobactin was indistinguishable from when MB was not added. Mc. capsulatus Bath lacks anything similar to mbnT and was unable to degrade methylmercury either in the presence or absence of methanobactin. Rather, Mc. capsulatus Bath appears to rely on MopE/MopE* for copper collection. Finally, not only does Mm. album BG8 steal methanobactin, it synthesizes a novel chalkophore, suggesting that some methanotrophs utilize both competition and cheating strategies for copper collection. Through a better understanding of these strategies, methanotrophic communities may be more effectively manipulated to reduce methane emissions and also enhance mercury detoxification in situ.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Methylococcus-capsulatus Bath; Particulate Methane Monooxygenase; Copper-binding; Iron; Acquisition; Protein; Siderophores; Competition; Expression; Evolution
ISSN (print) / ISBN 1751-7362
e-ISSN 1751-7370
Zeitschrift ISME Journal
Verlag Nature Publishing Group
Verlagsort Campus, 4 Crinan St, London, N1 9xw, England
Begutachtungsstatus Peer reviewed
Institut(e) Monoclonal Antibody (IDO-MAB)
Institute of Molecular Toxicology and Pharmacology (TOXI)
Förderungen U.S. Department of Energy (DOE)