Lily LlHSFC2 coordinates with HSFAs to balance heat stress response and improve thermotolerance
文献类型: 外文期刊
作者: Wu, Ze 1 ; Li, Ting 1 ; Ding, Liping 1 ; Wang, Chengpeng 4 ; Teng, Renda 1 ; Xu, Sujuan 1 ; Cao, Xing 5 ; Teng, Nianjun 1 ;
作者机构: 1.Nanjing Agr Univ, Coll Hort, Natl Forestry & Grassland Adm, Key Lab Landscaping,Key Lab Biol Ornamental Plants, Nanjing 210095, Peoples R China
2.Baguazhou Sci & Technol Innovat Ctr Modern Hort In, Nanjing 210043, Peoples R China
3.Nanjing Agr Univ, Coll Agr, Nanjing 210095, Peoples R China
4.Shandong Acad Agr Sci, Inst Leisure Agr, Key Lab East China Urban Agr, Minist Agr & Rural Affairs, Jinan 250100, Peoples R China
5.Yantai Univ, Coll Architecture, Yantai 264005, Peoples R China
关键词: AtHSFA2; heat stress transcription factor; high temperature; Lilium longiflorum; LlHSFA3A; LlHSFC2; thermotolerance
期刊名称:NEW PHYTOLOGIST ( 影响因子:9.4; 五年影响因子:10.5 )
ISSN: 0028-646X
年卷期: 2024 年 241 卷 5 期
页码:
收录情况: SCI
摘要: Heat stress transcription factors (HSFs) are core regulators of plant heat stress response. Much research has focused on class A and B HSFs, leaving those of class C relatively understudied. Here, we reported a lily (Lilium longiflorum) heat-inducible HSFC2 homology involved in thermotolerance. LlHSFC2 was located in the nucleus and cytoplasm and exhibited a repression ability by binding heat stress element. Overexpression of LlHSFC2 in Arabidopsis, tobacco (Nicotiana benthamiana), and lily, all increased the thermotolerance. Conversely, silencing of LlHSFC2 in lily reduced its thermotolerance. LlHSFC2 could interact with itself, or interact with LlHSFA1, LlHSFA2, LlHSFA3A, and LlHSFA3B of lily, AtHSFA1e and AtHSFA2 of Arabidopsis, and NbHSFA2 of tobacco. LlHSFC2 interacted with HSFAs to accelerate their transactivation ability and act as a transcriptional coactivator. Notably, compared with the separate LlHSFA3A overexpression, co-overexpression of LlHSFC2/LlHSFA3A further enhanced thermotolerance of transgenic plants. In addition, after suffering HS, the homologous interaction of LlHSFC2 was repressed, but its heterologous interaction with the heat-inducible HSFAs was promoted, enabling it to exert its co-activation effect for thermotolerance establishment and maintenance. Taken together, we identified that LlHSFC2 plays an active role in the general balance and maintenance of heat stress response by cooperating with HSFAs, and provided an important candidate for the enhanced thermotolerance breeding of crops and horticulture plants.
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