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Identification of AtSM34, a novel tonoplast intrinsic protein-interacting polypeptide expressed in response to osmotic stress in germinating seedlings
  • 时间:0
  • 分类:Q51[生物学—生物化学] Q945.78[生物学—植物学]
  • 作者机构:[1]State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, Beijing 100193, China, [2]Institute of Forestry and Pomology, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100093, China
  • 相关基金:This work was supported by the National Natural Science Foundation of China (30770193), the National Basic Research Program of China (2006CB100100), and the “111 Project” (B06003).
中文摘要:

Aquaporins 被含有在许多植物生理的过程,尽管涉及他们的规定的机制充分没被理解。为了获得进一步的卓见进规章的因素,在这进程包含了,我们使用了酵母为潜在的有约束力的搭挡屏蔽到 Arabidopsis tonoplast 的二混血儿的系统内在的蛋白质(尖端) AtTIP1; 1。这是识别从 Arabidopsis thaliana 在 vacuolar 膜与高水位线渗透被联系的第一蛋白质。用 AtTIP1; 1 作为诱饵,新奇有约束力的蛋白质在酵母和植物房间被识别。这猎物蛋白质,命名 AtSM34,是有 34 kD 的一个预言的分子的团的 309 aa 多肽并且包含了一个单个 MYB/SANT-like 领域。AtSM34 倡导者:GUS 组织化学的染色分析在花,茎和叶子检测了 AtSM34 表示特别地在脉管的纸巾,响应渗透的应力。AtSM34 表示在 endoplasmic 蜂窝胃膜是局部性的,并且顺序删除分析表明编码区域(氨基酸 1-83 ) 的 N 终端为这本地化是批评的。AtSM34 的 Overexpression 导致了超敏性到外长的甘露糖醇,山梨糖醇和 abscisic 酸,并且在萌芽引起了重要延期。AtSM34 与 AtTIP1 交往了; 2 并且 AtTIP2; 1,它是必要的为 tonoplast 渗透并且高度的调整的蛋白质在发芽表示了幼苗。这些数据显示 AtSM34 是在开发的一个早阶段涉及幼苗的渗透的压力反应的新奇尖端绑定蛋白质。

英文摘要:

Aquaporins are implicated in a wide variety of plant physiological processes, although the mechanisms involved in their regula- tion are not fully understood. To gain further insight into the regulatory factors involved in this process, we used a yeast two-hybrid system to screen for potential binding partners to the Arabidopsis tonoplast intrinsic protein (TIP) AtTIP1;1. This was the first protein identified to be associated with high water permeability in vacuolar membranes from Arabidopsis thaliana. Using AtTIP1;1 as bait, a novel binding protein was identified in both yeast and plant cells. This prey protein, named AtSM34, was a 309 aa polypeptide with a predicted molecular mass of 34 kD and contained a single MYB/SANT-like domain. AtSM34 pro- moter:: GUS histochemical staining analysis detected AtSM34 expression in flowers, stems and leaves, particularly in the vascular tissues, in response to osmotic stress. AtSM34 expression was localized in the endoplasmic reticulum membrane, and sequence deletion analysis revealed that the N-terminal coding region (amino acids 1-83) was critical for this localization. Overexpression of AtSM34 resulted in hypersensitivity to exogenous mannitol, sorbitol and abscisic acid, and caused a significant delay in germi- nation. AtSM34 interacted with AtTIP1 ;2 and AtTIP2; 1, which are essential proteins for modulation of tonoplast permeability and highly expressed in germinating seedlings. These data indicate AtSM34 is a novel TIPs binding protein involved in the osmotic stress response of seedlings at an early stage of development.

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