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Intron retention via alternative splicing affects the thermotolerance regulation of ZmHsf17

文献类型: 外文期刊

作者: Zhang, Huaning 1 ; Meng, Xiangzhao 1 ; Li, Ran 2 ; Ma, Zhenyu 1 ; Liu, Ran 1 ; Liu, Zihui 1 ; Duan, Shuonan 1 ; Zhang, Wenying 3 ; Li, Guoliang 1 ; Guo, Xiulin 1 ;

作者机构: 1.Hebei Acad Agr & Forestry Sci, Inst Biotechnol & Food Sci, Hebei Key Lab Plant Genet Engn, Shijiazhuang, Peoples R China

2.Hebei North Univ, Coll Agr & Forestry Sci & Technol, Zhangjiakou, Peoples R China

3.Hebei Acad Agr & Forestry Sci, Inst Dryland Farming, Hengshui, Peoples R China

期刊名称:PHYSIOLOGIA PLANTARUM ( 影响因子:6.4; 五年影响因子:5.9 )

ISSN: 0031-9317

年卷期: 2024 年 176 卷 1 期

页码:

收录情况: SCI

摘要: Heat shock transcription factor (Hsf) plays a pivotal role in promoting rapid heat-induced transcriptional reprogramming in plants. The thermotolerance regulatory function of Hsfs is influenced by their own alternative splicing. In this study, we found that ZmHsf17-II, an intron retention isoform of subclass A2 gene ZmHsf17 of maize (Zea mays), accumulated in large amounts as a result of severe or sustained heat stress. It was confirmed by expression and purification that ZmHsf17-II encodes a small truncated peptide with 115 amino acids. ZmHsf17-II was found to be located in the nucleus and have no transcriptional activity. Overexpressing ZmHsf17-I in Arabidopsis could enhance plants' thermotolerance, while overexpressing ZmHsf17-II does not. Based on the results of molecular docking, Y2H and split LUC experiments, we found that ZmHsf17-II could bind to DBD region of ZmHsf17-I through the hydrogen bond interaction between the truncated DBD of ZmHsf17-II and three amino acid residues (Arg105, Thr109 and Lys142) of ZmHsf17-I DBD region. Further experiments showed that ZmHsf17-I could bind to its own promoter and exhibited transcriptional activation activity, while ZmHsf17-I interaction with ZmHsf17-II, transcriptional activation activity was interfered. Those findings indicate that ZmHsf17 can negatively regulate its own transcription by producing more intron retention isoforms via alternative splicing under heat stress.

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