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LlbHLH87 interacts with LlSPT to modulate thermotolerance via activation of LlHSFA2 and LlEIN3 in lily

文献类型: 外文期刊

作者: Wu, Ze 1 ; Gong, Xue 1 ; Zhang, Yinyi 1 ; Li, Ting 1 ; Xiang, Jun 1 ; Fang, Qianqian 1 ; Yu, Junpeng 1 ; Ding, Liping 1 ; Liang, Jiahui 4 ; Teng, Nianjun 1 ;

作者机构: 1.Nanjing Agr Univ, Coll Hort, Natl Forestry & Grassland Adm, Key Lab Landscaping,Minist Agr & Rural Affairs,Key, Nanjing 210095, Peoples R China

2.Nanjing Agr Univ, Nanjing Oriole Isl Modern Agr Dev Co Ltd, Lily Sci & Technol Backyard Qixia Jiangsu, Jiangsu Grad Workstat, Nanjing 210043, Peoples R China

3.Nanjing Agr Univ, Coll Agr, Nanjing 210095, Peoples R China

4.Beijing Acad Agr & Forestry Sci, Inst Grassland Flowers & Ecol, Beijing 100097, Peoples R China

关键词: bHLH transcription factor; heat stress; Lilium longiflorum; LlbHLH87; LlEIN3; LlHSFA2; LlSPT

期刊名称:PLANT JOURNAL ( 影响因子:5.7; 五年影响因子:7.0 )

ISSN: 0960-7412

年卷期: 2024 年 120 卷 4 期

页码:

收录情况: SCI

摘要: Basic helix-loop-helix (bHLH) proteins comprise one of the largest families of transcription factors in plants, which play roles in plant development, secondary metabolism, and the response to biotic/abiotic stresses. However, the roles of bHLH proteins in thermotolerance are largely unknown. Herein, we identified a heat-inducible member of the bHLH family in lily (Lilium longiflorum), named LlbHLH87, which plays a role in thermotolerance. LlbHLH87 was rapidly induced by transient heat stress, and its encoded protein was localized to the nucleus, exhibiting transactivation activity in both yeast and plant cells. Overexpression of LlbHLH87 in Arabidopsis enhanced basal thermotolerance, while silencing of LlbHLH87 in lily reduced basal thermotolerance. Further analysis showed that LlbHLH87 bound to the promoters of HEAT STRESS TRANSCRIPTION FACTOR A2 (LlHSFA2) and ETHYLENE-INSENSITIVE 3 (LlEIN3) to directly activate their expression. In addition, LlbHLH87 interacted with itself and with SPATULA (LlSPT) protein. LlSPT was activated by extended heat stress and its protein competed for the homologous interaction of LlbHLH87, which reduced the transactivation ability of LlbHLH87 for target genes. Compared with that observed under LlbHLH87 overexpression alone, co-overexpression of LlbHLH87 and LlSPT reduced the basal thermotolerance of lily to sudden heat shock, but improved its thermosensitivity to prolonged heat stress treatment. Overall, our data demonstrated that LlbHLH87 regulates thermotolerance via activation of LlEIN3 and LlHSFA2, along with an antagonistic interaction with LlSPT.

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