Multiple domains within the Cauliflower mosaic virus gene VI product interact with the full-length protein
Multiple domains within the Cauliflower mosaic virus gene VI product interact with the full-length protein
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DOI：
10.1094/mpmi.2002.15.10.1050
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发表时间：
2002-10-01
影响因子：
3.5
通讯作者：
Leisner, SM
中科院分区：
文献类型：
--
作者：
Li, YZ;Leisner, SM
花椰菜花叶病毒(CaMV)基因VI产物(P6)是病毒繁殖所必需的多功能蛋白。很可能这些功能中至少有一些需要P6自关联。这里描述的工作是为了确认P6自关联并确定参与这种相互作用的结构域。酵母双杂交分析表明，全长P6自交，这种相互作用是特异的。进一步的分析表明，至少有四个独立的结构域与全长P6结合。当中央结构域(称为结构域D3)被移除时，这些相互作用被取消。然而，缺失的P6能够与全长野生型蛋白和分离的结构域D3结合。缺乏D3结构域的病毒不能产生全身性感染。分离的结构域D3能够与至少两个其他结构域结合，但不能自结合。这表明D3结构域通过与其他结构域结合而不是自身结合来促进P6的自我关联。参与P6自结合的多个结构域的存在可能有助于解释该蛋白形成杆状病毒特有的细胞内包涵体的能力。
The Cauliflower mosaic virus (CaMV) gene VI product (P6) is a multifunctional protein essential for viral propagation. It is likely that at least some of these functions require P6 self-association. The work described here was performed to confirm that P6 self-associates and to identify domains involved in this interaction. Yeast two-hybrid analyses indicated that full-length P6 self-associates and that this interaction is specific. Additional analyses indicated that at least four independent domains bind to full-length P6. When a central domain (termed domain D3) was removed, these interactions were abolished. However, this deleted P6 was able to bind to the full-length wild-type protein and to isolated domain D3. Viruses lacking domain D3 were incapable of producing a systemic infection. Isolated domain D3 was capable of binding to at least two of the other domains but was unable to self-associate. This suggests that domain D3 facilitates P6 self-association by binding to the other domains but not itself. The presence of multiple domains involved in P6 self-association may help explain the ability of this protein to form the intracellular inclusions characteristic of caulimoviruses.