The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i>
Bicarbonate (HCO<sub>3</sub><sup>−</sup>) transporter family including the anion exchanger (AE) group is involved in multiple physiological processes through regulating acid-base homeostasis. HCO<sub>3</sub><sup>−</sup> transporters have been extensive...
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oai:doaj.org-article:034bf461fdf740bfb8a8587b77ec500f2021-11-25T18:06:07ZThe Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i>10.3390/jof71109552309-608Xhttps://doaj.org/article/034bf461fdf740bfb8a8587b77ec500f2021-11-01T00:00:00Zhttps://www.mdpi.com/2309-608X/7/11/955https://doaj.org/toc/2309-608XBicarbonate (HCO<sub>3</sub><sup>−</sup>) transporter family including the anion exchanger (AE) group is involved in multiple physiological processes through regulating acid-base homeostasis. HCO<sub>3</sub><sup>−</sup> transporters have been extensively studied in mammals, but fungal homologues of AE are poorly understood. Here, we characterized the AE group member (MoAE4) in <i>Magnaporthe oryzae</i>. MoAE4 exhibits more sequence and structure homologies with the reported AE4 and BOR1 proteins. In addition to the common sublocalization on cytomembrane, MoAE4 also localizes on tonoplast. Yeast complementation verified that MoAE4 rescues boron sensitivity and endows NaHCO<sub>3</sub> tolerance in the <i>BOR1</i> deleted yeast. <i>MoAE4</i> gene is bicarbonate induced in <i>M. oryzae</i>; and loss of <i>MoAE4</i> (Δ<i>MoAE4</i>) resulted in mycelial growth inhibited by NaHCO<sub>3</sub>. Lucigenin fluorescence quenching assay confirmed that Δ<i>MoAE4</i> accumulated less HCO<sub>3</sub><sup>−</sup> in vacuole and more HCO<sub>3</sub><sup>−</sup> in cytosol, revealing a real role of MoAE4 in bicarbonate transport. Δ<i>MoAE4</i> was defective in conidiation, appressorium formation, and pathogenicity. More H<sub>2</sub>O<sub>2</sub> was detected to be accumulated in Δ<i>MoAE4</i> mycelia and infected rice cells. Summarily, our data delineate a cytomembrane and tonoplast located HCO<sub>3</sub><sup>−</sup> transporter, which is required for development and pathogenicity in <i>M. oryzae</i>, and revealing a potential drug target for blast disease control.Yuejia DangYi WeiPenghui ZhangXinchun LiuXinrui LiShaowei WangHao LiangShi-Hong ZhangMDPI AGarticleanion exchange protein 4 (AE4)HCO<sub>3</sub><sup>−</sup> transportertonoplastpathogenicity<i>Magnaporthe oryzae</i>Biology (General)QH301-705.5ENJournal of Fungi, Vol 7, Iss 955, p 955 (2021) |
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topic |
anion exchange protein 4 (AE4) HCO<sub>3</sub><sup>−</sup> transporter tonoplast pathogenicity <i>Magnaporthe oryzae</i> Biology (General) QH301-705.5 |
spellingShingle |
anion exchange protein 4 (AE4) HCO<sub>3</sub><sup>−</sup> transporter tonoplast pathogenicity <i>Magnaporthe oryzae</i> Biology (General) QH301-705.5 Yuejia Dang Yi Wei Penghui Zhang Xinchun Liu Xinrui Li Shaowei Wang Hao Liang Shi-Hong Zhang The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
description |
Bicarbonate (HCO<sub>3</sub><sup>−</sup>) transporter family including the anion exchanger (AE) group is involved in multiple physiological processes through regulating acid-base homeostasis. HCO<sub>3</sub><sup>−</sup> transporters have been extensively studied in mammals, but fungal homologues of AE are poorly understood. Here, we characterized the AE group member (MoAE4) in <i>Magnaporthe oryzae</i>. MoAE4 exhibits more sequence and structure homologies with the reported AE4 and BOR1 proteins. In addition to the common sublocalization on cytomembrane, MoAE4 also localizes on tonoplast. Yeast complementation verified that MoAE4 rescues boron sensitivity and endows NaHCO<sub>3</sub> tolerance in the <i>BOR1</i> deleted yeast. <i>MoAE4</i> gene is bicarbonate induced in <i>M. oryzae</i>; and loss of <i>MoAE4</i> (Δ<i>MoAE4</i>) resulted in mycelial growth inhibited by NaHCO<sub>3</sub>. Lucigenin fluorescence quenching assay confirmed that Δ<i>MoAE4</i> accumulated less HCO<sub>3</sub><sup>−</sup> in vacuole and more HCO<sub>3</sub><sup>−</sup> in cytosol, revealing a real role of MoAE4 in bicarbonate transport. Δ<i>MoAE4</i> was defective in conidiation, appressorium formation, and pathogenicity. More H<sub>2</sub>O<sub>2</sub> was detected to be accumulated in Δ<i>MoAE4</i> mycelia and infected rice cells. Summarily, our data delineate a cytomembrane and tonoplast located HCO<sub>3</sub><sup>−</sup> transporter, which is required for development and pathogenicity in <i>M. oryzae</i>, and revealing a potential drug target for blast disease control. |
format |
article |
author |
Yuejia Dang Yi Wei Penghui Zhang Xinchun Liu Xinrui Li Shaowei Wang Hao Liang Shi-Hong Zhang |
author_facet |
Yuejia Dang Yi Wei Penghui Zhang Xinchun Liu Xinrui Li Shaowei Wang Hao Liang Shi-Hong Zhang |
author_sort |
Yuejia Dang |
title |
The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
title_short |
The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
title_full |
The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
title_fullStr |
The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
title_full_unstemmed |
The Bicarbonate Transporter (MoAE4) Localized on Both Cytomembrane and Tonoplast Promotes Pathogenesis in <i>Magnaporthe oryzae</i> |
title_sort |
bicarbonate transporter (moae4) localized on both cytomembrane and tonoplast promotes pathogenesis in <i>magnaporthe oryzae</i> |
publisher |
MDPI AG |
publishDate |
2021 |
url |
https://doaj.org/article/034bf461fdf740bfb8a8587b77ec500f |
work_keys_str_mv |
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