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Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis
Plants have evolved various strategies to sense and respond to saline environments, which severely reduce plant growth and limit agricultural productivity. Alteration to the cell wall is one strategy that helps plants adapt to salt stress. However, the physiological mechanism of how the cell wall co...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793456/ https://www.ncbi.nlm.nih.gov/pubmed/31257449 http://dx.doi.org/10.1093/jxb/erz311 |
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author | Yan, Jingwei Huang, Yun He, Huan Han, Tong Di, Pengcheng Sechet, Julien Fang, Lin Liang, Yan Scheller, Henrik Vibe Mortimer, Jenny C Ni, Lan Jiang, Mingyi Hou, Xilin Zhang, Aying |
author_facet | Yan, Jingwei Huang, Yun He, Huan Han, Tong Di, Pengcheng Sechet, Julien Fang, Lin Liang, Yan Scheller, Henrik Vibe Mortimer, Jenny C Ni, Lan Jiang, Mingyi Hou, Xilin Zhang, Aying |
author_sort | Yan, Jingwei |
collection | PubMed |
description | Plants have evolved various strategies to sense and respond to saline environments, which severely reduce plant growth and limit agricultural productivity. Alteration to the cell wall is one strategy that helps plants adapt to salt stress. However, the physiological mechanism of how the cell wall components respond to salt stress is not fully understood. Here, we show that expression of XTH30, encoding xyloglucan endotransglucosylase-hydrolase30, is strongly up-regulated in response to salt stress in Arabidopsis. Loss-of-function of XTH30 leads to increased salt tolerance and overexpression of XTH30 results in salt hypersensitivity. XTH30 is located in the plasma membrane and is highly expressed in the root, flower, stem, and etiolated hypocotyl. The NaCl-induced increase in xyloglucan (XyG)-derived oligosaccharide (XLFG) of the wild type is partly blocked in xth30 mutants. Loss-of-function of XTH30 slows down the decrease of crystalline cellulose content and the depolymerization of microtubules caused by salt stress. Moreover, lower Na(+) accumulation in shoot and lower H(2)O(2) content are found in xth30 mutants in response to salt stress. Taken together, these results indicate that XTH30 modulates XyG side chains, altered abundance of XLFG, cellulose synthesis, and cortical microtubule stability, and negatively affecting salt tolerance. |
format | Online Article Text |
id | pubmed-6793456 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-67934562019-10-18 Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis Yan, Jingwei Huang, Yun He, Huan Han, Tong Di, Pengcheng Sechet, Julien Fang, Lin Liang, Yan Scheller, Henrik Vibe Mortimer, Jenny C Ni, Lan Jiang, Mingyi Hou, Xilin Zhang, Aying J Exp Bot Research Papers Plants have evolved various strategies to sense and respond to saline environments, which severely reduce plant growth and limit agricultural productivity. Alteration to the cell wall is one strategy that helps plants adapt to salt stress. However, the physiological mechanism of how the cell wall components respond to salt stress is not fully understood. Here, we show that expression of XTH30, encoding xyloglucan endotransglucosylase-hydrolase30, is strongly up-regulated in response to salt stress in Arabidopsis. Loss-of-function of XTH30 leads to increased salt tolerance and overexpression of XTH30 results in salt hypersensitivity. XTH30 is located in the plasma membrane and is highly expressed in the root, flower, stem, and etiolated hypocotyl. The NaCl-induced increase in xyloglucan (XyG)-derived oligosaccharide (XLFG) of the wild type is partly blocked in xth30 mutants. Loss-of-function of XTH30 slows down the decrease of crystalline cellulose content and the depolymerization of microtubules caused by salt stress. Moreover, lower Na(+) accumulation in shoot and lower H(2)O(2) content are found in xth30 mutants in response to salt stress. Taken together, these results indicate that XTH30 modulates XyG side chains, altered abundance of XLFG, cellulose synthesis, and cortical microtubule stability, and negatively affecting salt tolerance. Oxford University Press 2019-10-01 2019-06-29 /pmc/articles/PMC6793456/ /pubmed/31257449 http://dx.doi.org/10.1093/jxb/erz311 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Papers Yan, Jingwei Huang, Yun He, Huan Han, Tong Di, Pengcheng Sechet, Julien Fang, Lin Liang, Yan Scheller, Henrik Vibe Mortimer, Jenny C Ni, Lan Jiang, Mingyi Hou, Xilin Zhang, Aying Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title | Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title_full | Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title_fullStr | Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title_full_unstemmed | Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title_short | Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis |
title_sort | xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in arabidopsis |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6793456/ https://www.ncbi.nlm.nih.gov/pubmed/31257449 http://dx.doi.org/10.1093/jxb/erz311 |
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