Xyloglucan endotransglucosylase-hydrolase30 negatively affects salt tolerance in Arabidopsis

© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Détails bibliographiques
Publié dans:Journal of experimental botany. - 1985. - 70(2019), 19 vom: 15. Okt., Seite 5495-5506
Auteur principal: Yan, Jingwei (Auteur)
Autres auteurs: 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
Format: Article en ligne
Langue:English
Publié: 2019
Accès à la collection:Journal of experimental botany
Sujets:Journal Article Research Support, Non-U.S. Gov't Arabidopsis XLFG XTH30 cellulose microtubule salt stress xyloglucan Arabidopsis Proteins plus... AT1G32170 protein, Arabidopsis EC 2.4.1.- Glucosyltransferases XTH31 protein, Arabidopsis Glycoside Hydrolases EC 3.2.1.-
Description
Résumé:© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.
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 H2O2 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
Description:Date Completed 10.08.2020
Date Revised 08.10.2020
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erz311