Nie Xianguang, Ji Xiaoyu, Liu Yujia, Zheng Lei, Wang Yucheng
State Key Laboratory of Tree Genetics and Breeding (Northeast Forestry University), 26 Hexing Road, Harbin 150040, China.
Key Laboratory of Biogeography and Bioresource in Arid Land, Xinjiang Institute of Ecology and Geography, Chinese Academy of Sciences, Urumqi 830011, China.
Int J Mol Sci. 2014 Jun 4;15(6):10005-17. doi: 10.3390/ijms150610005.
Protein-protein interactions are important for the molecular understanding of the biological processes of proteins. The dimerization of bZIPs (basic leucine zipper proteins) is involved in modifying binding site specificities, altering dimer stability, and permitting a new set of specific protein-to-protein interactions to occur at the promoter. In the present study, we studied the whether ThbZIP1 form homo- and heterodimers using the yeast two-hybrid method. Five bZIP genes were cloned from Tamarix hispida to investigate their interaction with ThbZIP1. Our results showed that ThbZIP1 can form homodimers with itself, and three out of five bZIPs could interact with the ThbZIP1 protein to form heterodimers. Real-time RT-PCR results suggested that these ThbZIPs can all respond to abiotic stresses and abscisic acid (ABA), and shared very similar expression patterns in response to NaCl, ABA or PEG6000. Subcellular localization studies showed that all ThbZIPs are targeted to the nucleus. Our results showed that ThbZIP1 are dimeric proteins, which can form homo- or heterodimers.
蛋白质-蛋白质相互作用对于从分子层面理解蛋白质的生物学过程至关重要。碱性亮氨酸拉链蛋白（bZIPs）的二聚化参与改变结合位点特异性、改变二聚体稳定性，并使得启动子区域出现一组新的特定蛋白质-蛋白质相互作用。在本研究中，我们使用酵母双杂交方法研究了ThbZIP1是否形成同二聚体和异二聚体。从刚毛柽柳中克隆了5个bZIP基因，以研究它们与ThbZIP1的相互作用。我们的结果表明，ThbZIP1可以与自身形成同二聚体，并且5个bZIP中有3个可以与ThbZIP1蛋白相互作用形成异二聚体。实时定量逆转录聚合酶链反应（Real-time RT-PCR）结果表明，这些ThbZIPs均能对非生物胁迫和脱落酸（ABA）作出响应，并且在响应NaCl、ABA或聚乙二醇6000（PEG6000）时具有非常相似的表达模式。亚细胞定位研究表明，所有ThbZIPs均定位于细胞核。我们的结果表明，ThbZIP1是二聚体蛋白，可形成同二聚体或异二聚体。
