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The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans
Arsenate (As (V)) is the dominant form of the toxic metalloid arsenic (As). Microorganisms have consequently developed mechanisms to detoxify and tolerate this kind of compounds. In the present work, we have explored the arsenate sensing and signaling mechanisms in the pathogenic fungus Candida albi...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2015
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4324303/ https://www.ncbi.nlm.nih.gov/pubmed/25717325 http://dx.doi.org/10.3389/fmicb.2015.00118 |
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author | Urrialde, Verónica Prieto, Daniel Pla, Jesús Alonso-Monge, Rebeca |
author_facet | Urrialde, Verónica Prieto, Daniel Pla, Jesús Alonso-Monge, Rebeca |
author_sort | Urrialde, Verónica |
collection | PubMed |
description | Arsenate (As (V)) is the dominant form of the toxic metalloid arsenic (As). Microorganisms have consequently developed mechanisms to detoxify and tolerate this kind of compounds. In the present work, we have explored the arsenate sensing and signaling mechanisms in the pathogenic fungus Candida albicans. Although mutants impaired in the Hog1 or Mkc1-mediated pathways did not show significant sensitivity to this compound, both Hog1 and Mkc1 became phosphorylated upon addition of sodium arsenate to growing cells. Hog1 phosphorylation upon arsenate challenge was shown to be Ssk1-dependent. A screening designed for the identification of transcription factors involved in the arsenate response identified Pho4, a transcription factor of the myc-family, as pho4 mutants were susceptible to As (V). The expression of PHO4 was shortly induced in the presence of sodium arsenate in a Hog1-independent manner. Pho4 level affects Hog1 phosphorylation upon As (V) challenge, suggesting an indirect relationship between Pho4 activity and signaling in C. albicans. Pho4 also mediates the response to arsenite as revealed by the fact that pho4 defective mutants are sensitive to arsenite and Pho4 becomes phosphorylated upon sodium arsenite addition. Arsenite also triggers Hog1 phosphorylation by a process that is, in this case, independent of the Ssk1 kinase. These results indicate that the HOG pathway mediates the response to arsenate and arsenite in C. albicans and that the Pho4 transcription factor can differentiate among As (III), As (V) and P(i), triggering presumably specific responses. |
format | Online Article Text |
id | pubmed-4324303 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-43243032015-02-25 The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans Urrialde, Verónica Prieto, Daniel Pla, Jesús Alonso-Monge, Rebeca Front Microbiol Microbiology Arsenate (As (V)) is the dominant form of the toxic metalloid arsenic (As). Microorganisms have consequently developed mechanisms to detoxify and tolerate this kind of compounds. In the present work, we have explored the arsenate sensing and signaling mechanisms in the pathogenic fungus Candida albicans. Although mutants impaired in the Hog1 or Mkc1-mediated pathways did not show significant sensitivity to this compound, both Hog1 and Mkc1 became phosphorylated upon addition of sodium arsenate to growing cells. Hog1 phosphorylation upon arsenate challenge was shown to be Ssk1-dependent. A screening designed for the identification of transcription factors involved in the arsenate response identified Pho4, a transcription factor of the myc-family, as pho4 mutants were susceptible to As (V). The expression of PHO4 was shortly induced in the presence of sodium arsenate in a Hog1-independent manner. Pho4 level affects Hog1 phosphorylation upon As (V) challenge, suggesting an indirect relationship between Pho4 activity and signaling in C. albicans. Pho4 also mediates the response to arsenite as revealed by the fact that pho4 defective mutants are sensitive to arsenite and Pho4 becomes phosphorylated upon sodium arsenite addition. Arsenite also triggers Hog1 phosphorylation by a process that is, in this case, independent of the Ssk1 kinase. These results indicate that the HOG pathway mediates the response to arsenate and arsenite in C. albicans and that the Pho4 transcription factor can differentiate among As (III), As (V) and P(i), triggering presumably specific responses. Frontiers Media S.A. 2015-02-11 /pmc/articles/PMC4324303/ /pubmed/25717325 http://dx.doi.org/10.3389/fmicb.2015.00118 Text en Copyright © 2015 Urrialde, Prieto, Pla and Alonso-Monge. http://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) or licensor 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 Urrialde, Verónica Prieto, Daniel Pla, Jesús Alonso-Monge, Rebeca The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title | The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title_full | The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title_fullStr | The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title_full_unstemmed | The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title_short | The Pho4 transcription factor mediates the response to arsenate and arsenite in Candida albicans |
title_sort | pho4 transcription factor mediates the response to arsenate and arsenite in candida albicans |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4324303/ https://www.ncbi.nlm.nih.gov/pubmed/25717325 http://dx.doi.org/10.3389/fmicb.2015.00118 |
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