Bacterial SBP56 identified as a Cu-dependent methanethiol oxidase widely distributed in the biosphere
| Autor: | Thomas J. Smith, Sophie Mazard, Monique A. S. H. Mennink-Kersten, Andrew W. B. Johnston, Özge Eyice, Hendrik Schäfer, Adam Cuthbertson, Timothy D. H. Bugg, Huub J. M. Op den Camp, Ornella Carrión, Nataliia Myronova, Kerstin Andersson, S.J. Gurman, Jonathan D. Todd, Arjan Pol |
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| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Aerobic bacteria Ruegeria Sulfonium Compounds Selenium-Binding Proteins Sulfides Dimethylsulfoniopropionate Microbiology 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Environmental Microbiology Sulfhydryl Compounds Rhodobacteraceae Ecology Evolution Behavior and Systematics Oxidase test biology Periplasmic space biology.organism_classification Hyphomicrobium 030104 developmental biology Biochemistry chemistry Ecological Microbiology Methanethiol oxidase Original Article Oxidoreductases Bacteria |
| Zdroj: | The Isme Journal, 12, pp. 145-160 The Isme Journal, 12, 145-160. The Author(s) The ISME Journal |
| ISSN: | 1751-7370 1751-7362 |
| Popis: | 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.The ISME Journal advance online publication, 24 October 2017; doi:10.1038/ismej.2017.148. |
| Databáze: | OpenAIRE |
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