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New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis)
The endosomal-type Na(+), K(+)/H(+) antiporters (NHXs) play important roles in K(+), vesicle pH homeostasis, and protein trafficking in plant. However, the structure governing ion transport mechanism and the key residues related to the structure–function of the endosomal-type NHXs remain unclear. He...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7014192/ https://www.ncbi.nlm.nih.gov/pubmed/31936580 http://dx.doi.org/10.3390/ijms21020428 |
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author | Cao, Boning Xia, Zhongqiang Liu, Changying Fan, Wei Zhang, Shuai Liu, Qiao Xiang, Zhonghuai Zhao, Aichun |
author_facet | Cao, Boning Xia, Zhongqiang Liu, Changying Fan, Wei Zhang, Shuai Liu, Qiao Xiang, Zhonghuai Zhao, Aichun |
author_sort | Cao, Boning |
collection | PubMed |
description | The endosomal-type Na(+), K(+)/H(+) antiporters (NHXs) play important roles in K(+), vesicle pH homeostasis, and protein trafficking in plant. However, the structure governing ion transport mechanism and the key residues related to the structure–function of the endosomal-type NHXs remain unclear. Here, the structure-function relationship of the only endosomal-type NHX from mulberry, MnNHX6, was investigated by homology modeling, mutagenesis, and localization analyses in yeast. The ectopic expression of MnNHX6 in arabidopsis and Nhx1 mutant yeast can enhance their salt tolerance. MnNHX6’s three-dimensional structure, established by homology modeling, was supported by empirical, phylogenetic, and experimental data. Structure analysis showed that MnNHX6 contains unusual 13 transmembrane helices, but the structural core formed by TM5-TM12 assembly is conserved. Localization analysis showed that MnNHX6 has the same endosomal localization as yeast Nhx1/VPS44, and Arg402 is important for protein stability of MnNHX6. Mutagenesis analysis demonstrated MnNHX6 contains a conserved cation binding mechanism and a similar charge-compensated pattern as NHE1, but shares a different role in ion selectivity than the vacuolar-type NHXs. These results improve our understanding of the role played by the structure–function related key residues of the plant endosomal-type NHXs, and provide a basis for the ion transport mechanism study of endosomal-type NHXs. |
format | Online Article Text |
id | pubmed-7014192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70141922020-03-09 New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) Cao, Boning Xia, Zhongqiang Liu, Changying Fan, Wei Zhang, Shuai Liu, Qiao Xiang, Zhonghuai Zhao, Aichun Int J Mol Sci Article The endosomal-type Na(+), K(+)/H(+) antiporters (NHXs) play important roles in K(+), vesicle pH homeostasis, and protein trafficking in plant. However, the structure governing ion transport mechanism and the key residues related to the structure–function of the endosomal-type NHXs remain unclear. Here, the structure-function relationship of the only endosomal-type NHX from mulberry, MnNHX6, was investigated by homology modeling, mutagenesis, and localization analyses in yeast. The ectopic expression of MnNHX6 in arabidopsis and Nhx1 mutant yeast can enhance their salt tolerance. MnNHX6’s three-dimensional structure, established by homology modeling, was supported by empirical, phylogenetic, and experimental data. Structure analysis showed that MnNHX6 contains unusual 13 transmembrane helices, but the structural core formed by TM5-TM12 assembly is conserved. Localization analysis showed that MnNHX6 has the same endosomal localization as yeast Nhx1/VPS44, and Arg402 is important for protein stability of MnNHX6. Mutagenesis analysis demonstrated MnNHX6 contains a conserved cation binding mechanism and a similar charge-compensated pattern as NHE1, but shares a different role in ion selectivity than the vacuolar-type NHXs. These results improve our understanding of the role played by the structure–function related key residues of the plant endosomal-type NHXs, and provide a basis for the ion transport mechanism study of endosomal-type NHXs. MDPI 2020-01-09 /pmc/articles/PMC7014192/ /pubmed/31936580 http://dx.doi.org/10.3390/ijms21020428 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Cao, Boning Xia, Zhongqiang Liu, Changying Fan, Wei Zhang, Shuai Liu, Qiao Xiang, Zhonghuai Zhao, Aichun New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title | New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title_full | New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title_fullStr | New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title_full_unstemmed | New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title_short | New Insights into the Structure-Function Relationship of the Endosomal-Type Na(+), K(+)/H(+) Antiporter NHX6 from Mulberry (Morus notabilis) |
title_sort | new insights into the structure-function relationship of the endosomal-type na(+), k(+)/h(+) antiporter nhx6 from mulberry (morus notabilis) |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7014192/ https://www.ncbi.nlm.nih.gov/pubmed/31936580 http://dx.doi.org/10.3390/ijms21020428 |
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