Himmelbach A, Chapdelaine Y, Hohn T
Friedrich Miescher Institute, Basel, Switzerland.
Virology. 1996 Mar 1;217(1):147-57. doi: 10.1006/viro.1996.0102.
The cauliflower mosaic virus (CaMV) inclusion body protein (pVI) is able to specifically interact with the viral capsid precursor protein (pIV). By using the yeast two-hybrid system and a blot assay, the pIV region required for the recognition of pVI was mapped to the lysine-rich domain. This region of only 48 amino acids when fused to dihydrofolate reductase (DHFR) mediated pVI and DNA binding in vitro. Competition experiments confirmed that pVI and DNA bind to the same region of pIV. Since pVI is absent from the mature virus, models are discussed in which pVI plays an accessory role in CaMV assembly, in addition to its function in transactivating translation.
花椰菜花叶病毒（CaMV）包涵体蛋白（pVI）能够与病毒衣壳前体蛋白（pIV）特异性相互作用。通过酵母双杂交系统和印迹分析，将pVI识别所需的pIV区域定位到富含赖氨酸的结构域。当与二氢叶酸还原酶（DHFR）融合时，这个仅48个氨基酸的区域在体外介导pVI与DNA结合。竞争实验证实pVI和DNA结合到pIV的同一区域。由于成熟病毒中不存在pVI，因此除了其在反式激活翻译中的功能外，还讨论了pVI在CaMV组装中起辅助作用的模型。
