Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum
Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum
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DOI：
10.1128/jvi.78.7.3704-3709.2004
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发表时间：
2004-04-01
影响因子：
5.4
通讯作者：
Dolja, VV
中科院分区：
文献类型：
--
作者：
Peremyslov, VV;Pan, YW;Dolja, VV
甜菜黄化闭锁病毒的细胞间运动需要四种结构蛋白和一个6 kDa的蛋白(P6)，这是一种常规的非结构运动蛋白。在这里，我们证明，无论是病毒感染还是p6过表达都会导致p6与粗面内质网相关。P6蛋白具有一个单跨跨膜N-末端结构域和一个位于内质网细胞质表面的亲水性C-末端结构域。在受感染的细胞中，p6通过位于蛋白质N端附近的半胱氨酸残基形成二硫键。诱变分析表明，p6的每个结构域以及蛋白质的二聚化对于p6在病毒运动中的功能是必不可少的。
Cell-to-cell movement of beet yellows closterovirus requires four structural proteins and a 6-kDa protein (p6) that is a conventional, nonstructural movement protein. Here we demonstrate that either virus infection or p6 overexpression results in association of p6 with the rough endoplasmic reticulum. The p6 protein possesses a single-span, transmembrane, N-terminal domain and a hydrophilic, C-terminal domain that is localized on the cytoplasmic face of the endoplasmic reticulum. In the infected cells, p6 forms a disulfide bridge via a cysteine residue located near the protein's N terminus. Mutagenic analyses indicated that each of the p6 domains, as well as protein dimerization, is essential for p6 function in virus movement.