UDP-N-acetylglucosamine pyrophosphorylase enhances rice survival at high temperature

Détails bibliographiques
Publié dans:	The New phytologist. - 1984. - 233(2022), 1 vom: 11. Jan., Seite 344-359
Auteur principal:	Xia, Saisai (Auteur)
Autres auteurs:	Liu, He, Cui, Yuanjiang, Yu, Haiping, Rao, Yuchun, Yan, Yuping, Zeng, Dali, Hu, Jiang, Zhang, Guangheng, Gao, Zhenyu, Zhu, Li, Shen, Lan, Zhang, Qiang, Li, Qing, Dong, Guojun, Guo, Longbiao, Qian, Qian, Ren, Deyong
Format:	Article en ligne
Langue:	English
Publié:	2022
Accès à la collection:	The New phytologist
Sujets:	Journal Article Research Support, Non-U.S. Gov't DNA damage heat stress high-temperature adaptation photosystem defects reactive oxygen species rice Plant Proteins Nucleotidyltransferases plus... EC 2.7.7.- UDPacetylglucosamine pyrophosphorylase EC 2.7.7.23

Description
Résumé:	© 2021 The Authors. New Phytologist © 2021 New Phytologist Foundation. High-temperature stress inhibits normal cellular processes and results in abnormal growth and development in plants. However, the mechanisms by which rice (Oryza sativa) copes with high temperature are not yet fully understood. In this study, we identified a rice high temperature enhanced lesion spots 1 (hes1) mutant, which displayed larger and more dense necrotic spots under high temperature conditions. HES1 encoded a UDP-N-acetylglucosamine pyrophosphorylase, which had UGPase enzymatic activity. RNA sequencing analysis showed that photosystem-related genes were differentially expressed in the hes1 mutant at different temperatures, indicating that HES1 plays essential roles in maintaining chloroplast function. HES1 expression was induced under high temperature conditions. Furthermore, loss-of-function of HES1 affected heat shock factor expression and its mutation exhibited greater vulnerability to high temperature. Several experiments revealed that higher accumulation of reactive oxygen species occurred in the hes1 mutant at high temperature. Terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) and comet experiments indicated that the hes1 underwent more severe DNA damage at high temperature. The determination of chlorophyll content and chloroplast ultrastructure showed that more severe photosystem defects occurred in the hes1 mutant under high temperature conditions. This study reveals that HES1 plays a key role in adaptation to high-temperature stress in rice
Description:	Date Completed 06.01.2022 Date Revised 06.01.2022 published: Print-Electronic Citation Status MEDLINE
ISSN:	1469-8137
DOI:	10.1111/nph.17768