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Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4
Antimonite [Sb(III)]-oxidizing bacteria can transform the toxic Sb(III) into the less toxic antimonate [Sb(V)]. Recently, the cytoplasmic Sb(III)-oxidase AnoA and the periplasmic arsenite [As(III)] oxidase AioAB were shown to responsible for bacterial Sb(III) oxidation, however, disruption of each g...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group
2017
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333119/ https://www.ncbi.nlm.nih.gov/pubmed/28252030 http://dx.doi.org/10.1038/srep43225 |
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author | Li, Jingxin Yang, Birong Shi, Manman Yuan, Kai Guo, Wei Wang, Qian Wang, Gejiao |
author_facet | Li, Jingxin Yang, Birong Shi, Manman Yuan, Kai Guo, Wei Wang, Qian Wang, Gejiao |
author_sort | Li, Jingxin |
collection | PubMed |
description | Antimonite [Sb(III)]-oxidizing bacteria can transform the toxic Sb(III) into the less toxic antimonate [Sb(V)]. Recently, the cytoplasmic Sb(III)-oxidase AnoA and the periplasmic arsenite [As(III)] oxidase AioAB were shown to responsible for bacterial Sb(III) oxidation, however, disruption of each gene only partially decreased Sb(III) oxidation efficiency. This study showed that in Agrobacterium tumefaciens GW4, Sb(III) induced cellular H(2)O(2) content and H(2)O(2) degradation gene katA. Gene knock-out/complementation of katA, anoA, aioA and anoA/aioA and Sb(III) oxidation and growth experiments showed that katA, anoA and aioA were essential for Sb(III) oxidation and resistance and katA was also essential for H(2)O(2) resistance. Furthermore, linear correlations were observed between cellular H(2)O(2) and Sb(V) content in vivo and chemical H(2)O(2) and Sb(V) content in vitro (R(2) = 0.93 and 0.94, respectively). These results indicate that besides the biotic factors, the cellular H(2)O(2) induced by Sb(III) also catalyzes bacterial Sb(III) oxidation as an abiotic oxidant. The data reveal a novel mechanism that bacterial Sb(III) oxidation is associated with abiotic (cellular H(2)O(2)) and biotic (AnoA and AioAB) factors and Sb(III) oxidation process consumes cellular H(2)O(2) which contributes to microbial detoxification of both Sb(III) and cellular H(2)O(2). |
format | Online Article Text |
id | pubmed-5333119 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-53331192017-03-06 Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 Li, Jingxin Yang, Birong Shi, Manman Yuan, Kai Guo, Wei Wang, Qian Wang, Gejiao Sci Rep Article Antimonite [Sb(III)]-oxidizing bacteria can transform the toxic Sb(III) into the less toxic antimonate [Sb(V)]. Recently, the cytoplasmic Sb(III)-oxidase AnoA and the periplasmic arsenite [As(III)] oxidase AioAB were shown to responsible for bacterial Sb(III) oxidation, however, disruption of each gene only partially decreased Sb(III) oxidation efficiency. This study showed that in Agrobacterium tumefaciens GW4, Sb(III) induced cellular H(2)O(2) content and H(2)O(2) degradation gene katA. Gene knock-out/complementation of katA, anoA, aioA and anoA/aioA and Sb(III) oxidation and growth experiments showed that katA, anoA and aioA were essential for Sb(III) oxidation and resistance and katA was also essential for H(2)O(2) resistance. Furthermore, linear correlations were observed between cellular H(2)O(2) and Sb(V) content in vivo and chemical H(2)O(2) and Sb(V) content in vitro (R(2) = 0.93 and 0.94, respectively). These results indicate that besides the biotic factors, the cellular H(2)O(2) induced by Sb(III) also catalyzes bacterial Sb(III) oxidation as an abiotic oxidant. The data reveal a novel mechanism that bacterial Sb(III) oxidation is associated with abiotic (cellular H(2)O(2)) and biotic (AnoA and AioAB) factors and Sb(III) oxidation process consumes cellular H(2)O(2) which contributes to microbial detoxification of both Sb(III) and cellular H(2)O(2). Nature Publishing Group 2017-03-02 /pmc/articles/PMC5333119/ /pubmed/28252030 http://dx.doi.org/10.1038/srep43225 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Li, Jingxin Yang, Birong Shi, Manman Yuan, Kai Guo, Wei Wang, Qian Wang, Gejiao Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title | Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title_full | Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title_fullStr | Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title_full_unstemmed | Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title_short | Abiotic and biotic factors responsible for antimonite oxidation in Agrobacterium tumefaciens GW4 |
title_sort | abiotic and biotic factors responsible for antimonite oxidation in agrobacterium tumefaciens gw4 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5333119/ https://www.ncbi.nlm.nih.gov/pubmed/28252030 http://dx.doi.org/10.1038/srep43225 |
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