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钙调蛋白结合蛋白磷酸酶PP7参与拟南芥的耐热性。

Calmodulin-binding protein phosphatase PP7 is involved in thermotolerance in Arabidopsis.

作者信息

Liu Hong-Tao, Li Guo-Liang, Chang Hui, Sun Da-Ye, Zhou Ren-Gang, Li Bing

机构信息

Institute of Molecular Cell Biology, Hebei Normal University, Shijiazhuang 050016, China.

出版信息

Plant Cell Environ. 2007 Feb;30(2):156-64. doi: 10.1111/j.1365-3040.2006.01613.x.

Abstract

PP7 is the first protein Ser/Thr phosphatase to be found to interact with calmodulin (CaM) in plants. The T-DNA insertion AtPP7 knockout line and AtPP7 overexpression lines were employed to study the specific function of AtPP7. The AtPP7 knockout impaired the thermotolerance of Arabidopsis seedlings while the overexpression of AtPP7 resulted in plants with increased thermotolerance. Results from real-time polymerase chain reaction (PCR) showed that the expression of AtHSP70 and AtHSP101 genes was up-regulated in AtPP7 overexpression lines after heat shock (HS) at 37 degrees C for 1 h. Protein gel blot analysis showed that HSP70 protein levels increased in AtPP7 overexpression lines after HS at 37 degrees C for 2 h. The expression of the AtPP7 gene was also induced by HS at 37 degrees C in wild-type Arabidopsis. Using a yeast two-hybrid screen, we showed an interaction between AtPP7 and CaM. In addition, we found that AtPP7 interacts with an HS transcription factor (HSF), suggesting a possible role for AtPP7 in regulating the expression of heat shock protein (HSP) genes.

摘要

PP7是在植物中发现的首个与钙调蛋白(CaM)相互作用的蛋白丝氨酸/苏氨酸磷酸酶。利用T-DNA插入AtPP7基因敲除系和AtPP7过表达系来研究AtPP7的具体功能。AtPP7基因敲除削弱了拟南芥幼苗的耐热性,而AtPP7过表达则使植株的耐热性增强。实时聚合酶链反应(PCR)结果表明,在37℃热激(HS)处理1小时后,AtPP7过表达系中AtHSP70和AtHSP101基因的表达上调。蛋白质凝胶印迹分析表明,在37℃热激处理2小时后,AtPP7过表达系中HSP70蛋白水平增加。在野生型拟南芥中,37℃热激也可诱导AtPP7基因的表达。通过酵母双杂交筛选,我们发现AtPP7与CaM之间存在相互作用。此外,我们发现AtPP7与一个热激转录因子(HSF)相互作用,这表明AtPP7在调节热激蛋白(HSP)基因的表达中可能发挥作用。

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