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Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase
Microbial bromate reduction plays an important role in remediating bromate-contaminated waters as well as biogeochemical cycling of bromine. However, little is known about the molecular mechanism of microbial bromate reduction so far. Since the model strain Shewanella oneidensis MR-1 is capable of r...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9468665/ https://www.ncbi.nlm.nih.gov/pubmed/36110297 http://dx.doi.org/10.3389/fmicb.2022.955249 |
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author | Wang, Yicheng Fan, Jiale Shen, Yonglin Ye, Fan Feng, Zhiying Yang, Qianning Wang, Dan Cai, Xunchao Mao, Yanping |
author_facet | Wang, Yicheng Fan, Jiale Shen, Yonglin Ye, Fan Feng, Zhiying Yang, Qianning Wang, Dan Cai, Xunchao Mao, Yanping |
author_sort | Wang, Yicheng |
collection | PubMed |
description | Microbial bromate reduction plays an important role in remediating bromate-contaminated waters as well as biogeochemical cycling of bromine. However, little is known about the molecular mechanism of microbial bromate reduction so far. Since the model strain Shewanella oneidensis MR-1 is capable of reducing a variety of oxyanions such as iodate, which has a high similarity to bromate, we hypothesize that S. oneidensis MR-1 can reduce bromate. Here, we conducted an experiment to investigate whether S. oneidensis MR-1 can reduce bromate, and report bromate reduction mediated by a dimethylsulfoxide reductase encoded with dmsA. S. oneidensis MR-1 is not a bromate-respiring bacterium but can reduce bromate to bromide under microaerobic conditions. When exposed to 0.15, 0.2, 0.25, 0.5, and 1 mM bromate, S. oneidensis MR-1 reduced bromate by around 100, 75, 64, 48, and 23%, respectively, within 12 h. In vivo evidence from gene deletion mutants and complemented strains of S. oneidensis MR-1 indicates that MtrB, MtrC, CymA, GspD, and DmsA are involved in bromate reduction, but not NapA, FccA, or SYE4. Based on our results as well as previous findings, a proposed molecular mechanism for bromate reduction is presented in this study. Moreover, a genomic survey indicates that 9 of the other 56 reported Shewanella species encode proteins highly homologous to CymA, GspD, and DmsA of S. oneidensis MR-1 by sequence alignment. The results of this study contribute to understanding a pathway for microbial bromate reduction. |
format | Online Article Text |
id | pubmed-9468665 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-94686652022-09-14 Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase Wang, Yicheng Fan, Jiale Shen, Yonglin Ye, Fan Feng, Zhiying Yang, Qianning Wang, Dan Cai, Xunchao Mao, Yanping Front Microbiol Microbiology Microbial bromate reduction plays an important role in remediating bromate-contaminated waters as well as biogeochemical cycling of bromine. However, little is known about the molecular mechanism of microbial bromate reduction so far. Since the model strain Shewanella oneidensis MR-1 is capable of reducing a variety of oxyanions such as iodate, which has a high similarity to bromate, we hypothesize that S. oneidensis MR-1 can reduce bromate. Here, we conducted an experiment to investigate whether S. oneidensis MR-1 can reduce bromate, and report bromate reduction mediated by a dimethylsulfoxide reductase encoded with dmsA. S. oneidensis MR-1 is not a bromate-respiring bacterium but can reduce bromate to bromide under microaerobic conditions. When exposed to 0.15, 0.2, 0.25, 0.5, and 1 mM bromate, S. oneidensis MR-1 reduced bromate by around 100, 75, 64, 48, and 23%, respectively, within 12 h. In vivo evidence from gene deletion mutants and complemented strains of S. oneidensis MR-1 indicates that MtrB, MtrC, CymA, GspD, and DmsA are involved in bromate reduction, but not NapA, FccA, or SYE4. Based on our results as well as previous findings, a proposed molecular mechanism for bromate reduction is presented in this study. Moreover, a genomic survey indicates that 9 of the other 56 reported Shewanella species encode proteins highly homologous to CymA, GspD, and DmsA of S. oneidensis MR-1 by sequence alignment. The results of this study contribute to understanding a pathway for microbial bromate reduction. Frontiers Media S.A. 2022-08-30 /pmc/articles/PMC9468665/ /pubmed/36110297 http://dx.doi.org/10.3389/fmicb.2022.955249 Text en Copyright © 2022 Wang, Fan, Shen, Ye, Feng, Yang, Wang, Cai and Mao. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Wang, Yicheng Fan, Jiale Shen, Yonglin Ye, Fan Feng, Zhiying Yang, Qianning Wang, Dan Cai, Xunchao Mao, Yanping Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title | Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title_full | Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title_fullStr | Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title_full_unstemmed | Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title_short | Bromate reduction by Shewanella oneidensis MR-1 is mediated by dimethylsulfoxide reductase |
title_sort | bromate reduction by shewanella oneidensis mr-1 is mediated by dimethylsulfoxide reductase |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9468665/ https://www.ncbi.nlm.nih.gov/pubmed/36110297 http://dx.doi.org/10.3389/fmicb.2022.955249 |
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