UDP‐N‐acetylglucosamine pyrophosphorylase enhances rice survival at high temperature. Issue 1 (27th October 2021)
- Record Type:
- Journal Article
- Title:
- UDP‐N‐acetylglucosamine pyrophosphorylase enhances rice survival at high temperature. Issue 1 (27th October 2021)
- Main Title:
- UDP‐N‐acetylglucosamine pyrophosphorylase enhances rice survival at high temperature
- Authors:
- Xia, Saisai
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 - Abstract:
- Summary: 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 toSummary: 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. … (more)
- Is Part Of:
- New phytologist. Volume 233:Issue 1(2022)
- Journal:
- New phytologist
- Issue:
- Volume 233:Issue 1(2022)
- Issue Display:
- Volume 233, Issue 1 (2022)
- Year:
- 2022
- Volume:
- 233
- Issue:
- 1
- Issue Sort Value:
- 2022-0233-0001-0000
- Page Start:
- 344
- Page End:
- 359
- Publication Date:
- 2021-10-27
- Subjects:
- DNA damage -- heat stress -- high‐temperature adaptation -- photosystem defects -- reactive oxygen species -- rice
Botany -- Periodicals
580 - Journal URLs:
- http://nph.onlinelibrary.wiley.com/hub/journal/10.1111/(ISSN)1469-8137/ ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/nph.17768 ↗
- Languages:
- English
- ISSNs:
- 0028-646X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6085.000000
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British Library STI - ELD Digital store - Ingest File:
- 26822.xml