Two AT-Hook proteins regulate A/NINV7 expression to modulate sucrose catabolism for cold tolerance in Poncirus trifoliata

© 2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 235(2022), 6 vom: 30. Sept., Seite 2331-2349
1. Verfasser: Dahro, Bachar (VerfasserIn)
Weitere Verfasser: Wang, Yue, Khan, Madiha, Zhang, Yang, Fang, Tian, Ming, Ruhong, Li, Chunlong, Liu, Ji-Hong
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2022
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Poncirus trifoliata AT-Hook Motif Containing Nuclear Localized protein cold stress histone acetyltransferase invertase sucrose metabolism Plant Proteins Reactive Oxygen Species mehr... Sucrose 57-50-1 beta-Fructofuranosidase EC 3.2.1.26
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520 |a Invertase (INV)-mediated sucrose (Suc) hydrolysis, leading to the irreversible production of glucose (Glc) and fructose (Frc), plays an essential role in abiotic stress tolerance of plants. However, the regulatory network associated with the Suc catabolism in response to cold environment remains largely elusive. Herein, the cold-induced alkaline/neutral INV gene PtrA/NINV7 of trifoliate orange (Poncirus trifoliata (L.) Raf.) was shown to function in cold tolerance via mediating the Suc hydrolysis. Meanwhile, a nuclear matrix-associated region containing A/T-rich sequences within its promoter was indispensable for the cold induction of PtrA/NINV7. Two AT-Hook Motif Containing Nuclear Localized (AHL) proteins, PtrAHL14 and PtrAHL17, were identified as upstream transcriptional activators of PtrA/NINV7 by interacting with the A/T-rich motifs. PtrAHL14 and PtrAHL17 function positively in the cold tolerance by modulating PtrA/NINV7-mediated Suc catabolism. Furthermore, both PtrAHL14 and PtrAHL17 could form homo- and heterodimers between each other, and interacted with two histone acetyltransferases (HATs), GCN5 and TAF1, leading to elevated histone3 acetylation level under the cold stress. Taken together, our findings unraveled a new cold-responsive signaling module (AHL14/17-HATs-A/NINV7) for orchestration of Suc catabolism and cold tolerance, which shed light on the molecular mechanisms underlying Suc catabolism catalyzed by A/NINVs under cold stress 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a Poncirus trifoliata 
650 4 |a AT-Hook Motif Containing Nuclear Localized protein 
650 4 |a cold stress 
650 4 |a histone acetyltransferase 
650 4 |a invertase 
650 4 |a sucrose metabolism 
650 7 |a Plant Proteins  |2 NLM 
650 7 |a Reactive Oxygen Species  |2 NLM 
650 7 |a Sucrose  |2 NLM 
650 7 |a 57-50-1  |2 NLM 
650 7 |a beta-Fructofuranosidase  |2 NLM 
650 7 |a EC 3.2.1.26  |2 NLM 
700 1 |a Wang, Yue  |e verfasserin  |4 aut 
700 1 |a Khan, Madiha  |e verfasserin  |4 aut 
700 1 |a Zhang, Yang  |e verfasserin  |4 aut 
700 1 |a Fang, Tian  |e verfasserin  |4 aut 
700 1 |a Ming, Ruhong  |e verfasserin  |4 aut 
700 1 |a Li, Chunlong  |e verfasserin  |4 aut 
700 1 |a Liu, Ji-Hong  |e verfasserin  |4 aut 
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773 1 8 |g volume:235  |g year:2022  |g number:6  |g day:30  |g month:09  |g pages:2331-2349 
856 4 0 |u http://dx.doi.org/10.1111/nph.18304  |3 Volltext 
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