The transcription factor PpTGA9 improves salt tolerance by interacting with PpATP1 in peach

双分子荧光互补 拟南芥 转录因子 互补 蛋白质片段互补分析 拟南芥 细胞生物学 生物 李子 酵母 亚细胞定位 生物化学 植物 突变体 基因 化学 细胞质
作者
Qijie Wu,Huiru Chi,Wenzhe Zhao,Wei Xiao,Qiuping Tan,Xinmin Li,Ling Li,Mingyue Sun
出处
期刊:Environmental and Experimental Botany [Elsevier]
卷期号:214: 105468-105468 被引量:2
标识
DOI:10.1016/j.envexpbot.2023.105468
摘要

Salt stress hinders plant growth and development by affecting the ability of plant roots to absorb water, in turn affecting photosynthetic capacity and other metabolic processes, and ultimately reducing yield and quality. Peach (Prunus persica) is a salt-sensitive species, but the mechanism of peach adaptation to salt stress is not clear. We previously screened 50 basic leucine zipper (bZIP) transcription factors (TFs) in peach and found that the PpbZIP30 TF has several conserved functions. The gene encoding this TF was found to be highly homologous (75.19 % similarity) to Arabidopsis thaliana AtTGA9, so it was named PpTGA9. Expression of PpTGA9 was induced by exogenous application of NaCl after different treatments of exogenous signals in peach seedlings, and overexpressed PpTGA9 in Arabidopsis plants enhanced resistance to salt stress. To clarify the role of PpbZIP30/PpTGA9 in salt resistance, PpATP1 was screened using a yeast two-hybrid cross and further validated by bimolecular fluorescence complementation (BiFC), pull down, and subcellular localization to show that the two interacted with each other in vitro and in the nucleus. To investigate the mechanism of interaction between PpTGA9 and PpATP1, we divided PpTGA9 into five segments and cotransformed them with PpATP1. We found that two glutamic acid (Gln)-rich structural domains (Q1 and Q2) were essential in the interaction between PpTGA9 and PpATP1, however, the N and bZIP regions did not have significant roles in this interaction. Further study revealed that PpATP1 protein interacts with itself to form homodimers and PpATP1 expression specificity analysis showed that it can rapidly respond to salt stress signals. These findings suggest that PpATP1 interacts with two Gln-rich structural domains (Q1 and Q2) of PpTGA9 and simultaneously forms homodimers. The two also form a PpTGA9/PpATP1 complex that has an active role in improving salt tolerance in peach.
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