AtPPRT3, a novel E3 ubiquitin ligase, plays a positive role in ABA signaling

2020 ◽  
Vol 39 (11) ◽  
pp. 1467-1478 ◽  
Author(s):  
Yu Liu ◽  
Lu Peng ◽  
Xuemeng Gao ◽  
Yingying Liu ◽  
Zhibin Liu ◽  
...  
Plants ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1074
Author(s):  
Yu Liu ◽  
Shuya Xiao ◽  
Haoran Sun ◽  
Linsen Pei ◽  
Yingying Liu ◽  
...  

E3 ubiquitin ligase plays a vital role in the ubiquitin-mediated heat-related protein degradation pathway. Herein, we report that the expression of AtPPRT1, a C3HC4 zinc-finger ubiquitin E3 ligase gene, was induced by heat stress, and the β-glucuronidase (GUS) gene driven by the AtPPRT1 promoter has shown increased activity after basal and acquired thermotolerance. To further explore the function of AtPPRT1 in heat stress response (HSR), we used the atpprt1 mutant and AtPPRT1-overexpressing lines (OE2 and OE10) to expose in heat shock. In this study, the atpprt1 mutant had a lower germination and survival rate than those of Col-0 when suffered from the heat stress, whereas OEs enhanced basal and acquired thermotolerance in Arabidopsis seedlings. When compared to Col-0 and OEs, loss-of-function in AtPPRT1 resulted in lower chlorophyll retention and higher content of reactive oxygen species (ROS) after heat treatment. Moreover, the transcript levels of AtPPRT1 and several heat-related genes (AtZAT12, AtHSP21 and AtHSFA7a) were upregulated to greater extents in OEs and lower extents in atpprt1 compared to Col-0 after heat treated. Hence, we suggest that AtPPRT1 may act as a positive role in regulating the high temperature by mediating the degradation of unknown target proteins.


2020 ◽  
Vol 13 (11) ◽  
pp. 1556-1569
Author(s):  
Feifei Yu ◽  
Xiaoqiang Cao ◽  
Guangchao Liu ◽  
Qian Wang ◽  
Ran Xia ◽  
...  

2020 ◽  
Author(s):  
Maria Derkacheva ◽  
Gang Yu ◽  
Jose S. Rufian ◽  
Shushu Jiang ◽  
Paul Derbyshire ◽  
...  

SummaryPlant immunity is tightly controlled by a complex and dynamic regulatory network, which ensures optimal activation upon detection of potential pathogens. Accordingly, each component of this network is a potential target for manipulation by pathogens. Here, we report that RipAC, a type III-secreted effector from the bacterial pathogen Ralstonia solanacearum, targets the plant E3 ubiquitin ligase PUB4 to inhibit pattern-triggered immunity (PTI). PUB4 plays a positive role in PTI by regulating the homeostasis of the central immune kinase BIK1. Before PAMP perception, PUB4 promotes the degradation of non-activated BIK1, while, after PAMP perception, PUB4 contributes to the accumulation of activated BIK1. RipAC leads to BIK1 degradation, which correlates with its PTI-inhibitory activity. RipAC causes a reduction in pathogen-associated molecular pattern (PAMP)-induced PUB4 accumulation and phosphorylation. Our results shed light on the role played by PUB4 in immune regulation, and illustrate an indirect targeting of the immune signalling hub BIK1 by a bacterial effector.


2018 ◽  
Vol 94 (5) ◽  
pp. 836-846 ◽  
Author(s):  
Ronghui Pan ◽  
John Satkovich ◽  
Cheng Chen ◽  
Jianping Hu

2018 ◽  
Vol 37 (9) ◽  
pp. 1269-1278 ◽  
Author(s):  
Boya Wang ◽  
Chuzhe Li ◽  
Xiangge Kong ◽  
Ying Li ◽  
Zhibin Liu ◽  
...  

Author(s):  
Leilani M. Chirino ◽  
Suresh Kumar ◽  
Mariko Okumura ◽  
David E. Sterner ◽  
Michael Mattern ◽  
...  

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