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Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere

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Eyice, Özge, Myronova, Natalia, Pol, Arjan, Carrion, Ornella, Todd, Jonathan, Smith, Tom J., Gurman, Stephen J., Cuthbertson, Adam, Mazard, Sophie, Mennink-Kersten, Monique A. S. H. , Bugg, Tim, Andersson, K. Kristoffer, Johnston, Andrew W. B., Op Den Camp, Huub J. M. and Schäfer, Hendrik (2018) Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere. ISME Journal, 12 (1). 145-160 . doi:10.1038/ismej.2017.148

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Official URL: https://doi.org/10.1038/ismej.2017.148

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Abstract

Oxidation of methanethiol (MT) is a significant step in the sulfur cycle. MT is an intermediate of metabolism of globally significant organosulfur compounds including dimethylsulfoniopropionate (DMSP) and dimethylsulfide (DMS), which have key roles in marine carbon and sulfur cycling. In aerobic bacteria, MT is degraded by a MT oxidase (MTO). The enzymatic and genetic basis of MT oxidation have remained poorly characterized. Here, we identify for the first time the MTO enzyme and its encoding gene (mtoX) in the DMS-degrading bacterium Hyphomicrobium sp. VS. We show that MTO is a homotetrameric metalloenzyme that requires Cu for enzyme activity. MTO is predicted to be a soluble periplasmic enzyme and a member of a distinct clade of the Selenium-binding protein (SBP56) family for which no function has been reported. Genes orthologous to mtoX exist in many bacteria able to degrade DMS, other one-carbon compounds or DMSP, notably in the marine model organism Ruegeria pomeroyi DSS-3, a member of the Rhodobacteraceae family that is abundant in marine environments. Marker exchange mutagenesis of mtoX disrupted the ability of R. pomeroyi to metabolize MT confirming its function in this DMSP-degrading bacterium. In R. pomeroyi, transcription of mtoX was enhanced by DMSP, methylmercaptopropionate and MT. Rates of MT degradation increased after pre-incubation of the wild-type strain with MT. The detection of mtoX orthologs in diverse bacteria, environmental samples and its abundance in a range of metagenomic data sets point to this enzyme being widely distributed in the environment and having a key role in global sulfur cycling.

Item Type: Journal Article
Divisions: Faculty of Science > Chemistry
Faculty of Science > Life Sciences (2010- )
Journal or Publication Title: ISME Journal
Publisher: Nature Publishing Group
ISSN: 1751-7362
Official Date: January 2018
Dates:
DateEvent
January 2018Published
24 October 2017Available
27 July 2017Accepted
Volume: 12
Number: 1
Page Range: 145-160
DOI: 10.1038/ismej.2017.148
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), European Research Council (ERC)

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