Department of Applied Biology, Chungnam National University, Daejeon 305-764, Korea ; Department of Bioscience II, Bio-Medical Science, Daejeon 305-301, Korea.
Department of Applied Biology, Chungnam National University, Daejeon 305-764, Korea.
Plant Pathol J. 2013 Dec;29(4):454-9. doi: 10.5423/PPJ.NT.04.2013.0045.
The Potexvirus Alternanthera mosaic virus (AltMV) has multifunctional triple gene block (TGB) proteins, among which our studies have focused on the properties of the TGB1 protein. The TGB1 of AltMV has functions including RNA binding, RNA silencing suppression, and cell-to-cell movement, and is known to form homologous interactions. The helicase domains of AltMV TGB1 were separately mutated to identify which regions are involved in homologous TGB1 interactions. The yeast two hybrid system and Bimolecular Fluorescence Complementation (BiFC) in planta were utilized to examine homologous interactions of the mutants. Helicase motif I of AltMV TGB1 was found to be critical to maintain homologous interactions. Mutations in the remaining helicase motifs did not inhibit TGB1 homologous interactions. In the absence of homologous interaction of TGB1, subcellular localization of helicase domain I mutants showed distinctively different patterns from that of WT TGB1. These results provide important information to study viral movement and replication of AltMV.
百脉根坏死斑点病毒（AltMV）的 Potexvirus 具有多功能三联基因块（TGB）蛋白，其中我们的研究集中在 TGB1 蛋白的特性上。AltMV 的 TGB1 具有 RNA 结合、RNA 沉默抑制和细胞间运动等功能，已知其具有同源相互作用。我们分别突变 AltMV TGB1 的解旋酶结构域，以确定哪些区域参与同源 TGB1 相互作用。利用酵母双杂交系统和植物体内双分子荧光互补（BiFC）来检测突变体的同源相互作用。发现 AltMV TGB1 的解旋酶 motif I 对于维持同源相互作用至关重要。剩余解旋酶 motif 中的突变并未抑制 TGB1 的同源相互作用。在没有 TGB1 同源相互作用的情况下，解旋酶结构域 I 突变体的亚细胞定位与 WT TGB1 的定位明显不同。这些结果为研究 AltMV 的病毒运动和复制提供了重要信息。
