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A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4
Indium (In) is a critical metal widely used in electronic equipment, and the supply of this precious metal is a major challenge for sustainable development. The use of microorganisms for the recovery of this critical high-tech element has been considered an excellent eco-friendly strategy. The Rhoda...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8679861/ https://www.ncbi.nlm.nih.gov/pubmed/34925279 http://dx.doi.org/10.3389/fmicb.2021.772127 |
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author | Caldeira, Joana B. Chung, Ana Paula Piedade, Ana Paula Morais, Paula V. Branco, Rita |
author_facet | Caldeira, Joana B. Chung, Ana Paula Piedade, Ana Paula Morais, Paula V. Branco, Rita |
author_sort | Caldeira, Joana B. |
collection | PubMed |
description | Indium (In) is a critical metal widely used in electronic equipment, and the supply of this precious metal is a major challenge for sustainable development. The use of microorganisms for the recovery of this critical high-tech element has been considered an excellent eco-friendly strategy. The Rhodanobacter sp. B2A1Ga4 strain, highly resistant to In, was studied in order to disclose the bacterial mechanisms closely linked to the ability to cope with this metal. The mutation of the gene encoding for a DedA protein homolog, YqaA, affected drastically the In resistance and the cellular metabolic activity of strain Rhodanobacter sp. B2A1Ga4 in presence of this metal. This indicates that this protein plays an important role in its In resistance phenotype. The negative impact of In might be related to the high accumulation of the metal into the mutant cells showing In concentration up to approximately 4-fold higher than the native strain. In addition, the expression of the yqaA gene in this mutant reverted the bacterial phenotype with a significant decrease of In accumulation levels into the cells and an increase of In resistance. Membrane potential measurements showed similar values for native and mutant cells, suggesting that there was no loss of proton-motive force in the mutant cells. The results from this study suggest a potential role of this DedA family protein as a membrane transporter involved in the In efflux process. The mutant strain also has the potential to be used as a biotool in bioaccumulation strategies, for the recovery of In in biomining activities. |
format | Online Article Text |
id | pubmed-8679861 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86798612021-12-18 A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 Caldeira, Joana B. Chung, Ana Paula Piedade, Ana Paula Morais, Paula V. Branco, Rita Front Microbiol Microbiology Indium (In) is a critical metal widely used in electronic equipment, and the supply of this precious metal is a major challenge for sustainable development. The use of microorganisms for the recovery of this critical high-tech element has been considered an excellent eco-friendly strategy. The Rhodanobacter sp. B2A1Ga4 strain, highly resistant to In, was studied in order to disclose the bacterial mechanisms closely linked to the ability to cope with this metal. The mutation of the gene encoding for a DedA protein homolog, YqaA, affected drastically the In resistance and the cellular metabolic activity of strain Rhodanobacter sp. B2A1Ga4 in presence of this metal. This indicates that this protein plays an important role in its In resistance phenotype. The negative impact of In might be related to the high accumulation of the metal into the mutant cells showing In concentration up to approximately 4-fold higher than the native strain. In addition, the expression of the yqaA gene in this mutant reverted the bacterial phenotype with a significant decrease of In accumulation levels into the cells and an increase of In resistance. Membrane potential measurements showed similar values for native and mutant cells, suggesting that there was no loss of proton-motive force in the mutant cells. The results from this study suggest a potential role of this DedA family protein as a membrane transporter involved in the In efflux process. The mutant strain also has the potential to be used as a biotool in bioaccumulation strategies, for the recovery of In in biomining activities. Frontiers Media S.A. 2021-11-26 /pmc/articles/PMC8679861/ /pubmed/34925279 http://dx.doi.org/10.3389/fmicb.2021.772127 Text en Copyright © 2021 Caldeira, Chung, Piedade, Morais and Branco. 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 Caldeira, Joana B. Chung, Ana Paula Piedade, Ana Paula Morais, Paula V. Branco, Rita A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title | A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title_full | A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title_fullStr | A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title_full_unstemmed | A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title_short | A DedA Family Membrane Protein in Indium Extrusion in Rhodanobacter sp. B2A1Ga4 |
title_sort | deda family membrane protein in indium extrusion in rhodanobacter sp. b2a1ga4 |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8679861/ https://www.ncbi.nlm.nih.gov/pubmed/34925279 http://dx.doi.org/10.3389/fmicb.2021.772127 |
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