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SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance
In plant cells, the plasma membrane Na(+)/H(+) antiporter SOS1 (salt overly sensitive 1) mediates Na(+) extrusion using the proton gradient generated by plasma membrane H(+)-ATPases, and these two proteins are key plant halotolerance factors. In the present study, two genes from Sesuvium portulacast...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4560418/ https://www.ncbi.nlm.nih.gov/pubmed/26340746 http://dx.doi.org/10.1371/journal.pone.0137447 |
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author | Zhou, Yang Yin, Xiaochang Duan, Ruijun Hao, Gangping Guo, Jianchun Jiang, Xingyu |
author_facet | Zhou, Yang Yin, Xiaochang Duan, Ruijun Hao, Gangping Guo, Jianchun Jiang, Xingyu |
author_sort | Zhou, Yang |
collection | PubMed |
description | In plant cells, the plasma membrane Na(+)/H(+) antiporter SOS1 (salt overly sensitive 1) mediates Na(+) extrusion using the proton gradient generated by plasma membrane H(+)-ATPases, and these two proteins are key plant halotolerance factors. In the present study, two genes from Sesuvium portulacastrum, encoding plasma membrane Na(+)/H(+) antiporter (SpSOS1) and H(+)-ATPase (SpAHA1), were cloned. Localization of each protein was studied in tobacco cells, and their functions were analyzed in yeast cells. Both SpSOS1 and SpAHA1 are plasma membrane-bound proteins. Real-time polymerase chain reaction (PCR) analyses showed that SpSOS1 and SpAHA1 were induced by salinity, and their expression patterns in roots under salinity were similar. Compared with untransformed yeast cells, SpSOS1 increased the salt tolerance of transgenic yeast by decreasing the Na(+) content. The Na(+)/H(+) exchange activity at plasma membrane vesicles was higher in SpSOS1-transgenic yeast than in the untransformed strain. No change was observed in the salt tolerance of yeast cells expressing SpAHA1 alone; however, in yeast transformed with both SpSOS1 and SpAHA1, SpAHA1 generated an increased proton gradient that stimulated the Na(+)/H(+) exchange activity of SpSOS1. In this scenario, more Na(+) ions were transported out of cells, and the yeast cells co-expressing SpSOS1 and SpAHA1 grew better than the cells transformed with only SpSOS1 or SpAHA1. These findings demonstrate that the plasma membrane Na(+)/H(+) antiporter SpSOS1 and H(+)-ATPase SpAHA1 can function in coordination. These results provide a reference for developing more salt-tolerant crops via co-transformation with the plasma membrane Na(+)/H(+) antiporter and H(+)-ATPase. |
format | Online Article Text |
id | pubmed-4560418 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-45604182015-09-10 SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance Zhou, Yang Yin, Xiaochang Duan, Ruijun Hao, Gangping Guo, Jianchun Jiang, Xingyu PLoS One Research Article In plant cells, the plasma membrane Na(+)/H(+) antiporter SOS1 (salt overly sensitive 1) mediates Na(+) extrusion using the proton gradient generated by plasma membrane H(+)-ATPases, and these two proteins are key plant halotolerance factors. In the present study, two genes from Sesuvium portulacastrum, encoding plasma membrane Na(+)/H(+) antiporter (SpSOS1) and H(+)-ATPase (SpAHA1), were cloned. Localization of each protein was studied in tobacco cells, and their functions were analyzed in yeast cells. Both SpSOS1 and SpAHA1 are plasma membrane-bound proteins. Real-time polymerase chain reaction (PCR) analyses showed that SpSOS1 and SpAHA1 were induced by salinity, and their expression patterns in roots under salinity were similar. Compared with untransformed yeast cells, SpSOS1 increased the salt tolerance of transgenic yeast by decreasing the Na(+) content. The Na(+)/H(+) exchange activity at plasma membrane vesicles was higher in SpSOS1-transgenic yeast than in the untransformed strain. No change was observed in the salt tolerance of yeast cells expressing SpAHA1 alone; however, in yeast transformed with both SpSOS1 and SpAHA1, SpAHA1 generated an increased proton gradient that stimulated the Na(+)/H(+) exchange activity of SpSOS1. In this scenario, more Na(+) ions were transported out of cells, and the yeast cells co-expressing SpSOS1 and SpAHA1 grew better than the cells transformed with only SpSOS1 or SpAHA1. These findings demonstrate that the plasma membrane Na(+)/H(+) antiporter SpSOS1 and H(+)-ATPase SpAHA1 can function in coordination. These results provide a reference for developing more salt-tolerant crops via co-transformation with the plasma membrane Na(+)/H(+) antiporter and H(+)-ATPase. Public Library of Science 2015-09-04 /pmc/articles/PMC4560418/ /pubmed/26340746 http://dx.doi.org/10.1371/journal.pone.0137447 Text en © 2015 Zhou et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Zhou, Yang Yin, Xiaochang Duan, Ruijun Hao, Gangping Guo, Jianchun Jiang, Xingyu SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title | SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title_full | SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title_fullStr | SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title_full_unstemmed | SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title_short | SpAHA1 and SpSOS1 Coordinate in Transgenic Yeast to Improve Salt Tolerance |
title_sort | spaha1 and spsos1 coordinate in transgenic yeast to improve salt tolerance |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4560418/ https://www.ncbi.nlm.nih.gov/pubmed/26340746 http://dx.doi.org/10.1371/journal.pone.0137447 |
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