Phosphorylation and interaction of the movement and coat proteins of brome mosaic virus in infected barley protoplasts
Phosphorylation and interaction of the movement and coat proteins of brome mosaic virus in infected barley protoplasts
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DOI：
10.1007/s00705-007-1038-6
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发表时间：
2007-10-01
影响因子：
2.7
通讯作者：
Mise, K.
中科院分区：
文献类型：
--
作者：
Akamatsu, N.;Takeda, A.;Mise, K.
雀麦花叶病毒（BMV）的3 a运动蛋白（B3 a）在BMV的细胞间运动中起重要作用。已知B3a结合核酸，将RNA转运到邻近细胞，并形成管状结构。在这里，我们测试的假设，磷酸化可能是一种机制，调节B3a的功能，并表明，不仅B3a，而且外壳蛋白，BCP，被磷酸化的BMV感染的大麦原生质体。BCP和B3a都在BMV感染的原生质体与抗B3a抗血清的免疫沉淀复合物中检测到，这意味着BCP和B3a之间的相互作用。
The 3a movement protein (B3a) of brome mosaic virus (BMV) plays essential roles in the cell-to-cell movement of BMV. B3a is known to bind nucleic acids, to transport RNA to neighbouring cells, and to form tubular structures. Here, we tested the assumption that phosphorylation may be a mechanism that regulates B3a functions and showed that not only B3a but also the coat protein, BCP, was phosphorylated in BMV-infected barley protoplasts. Both BCP and B3a were detected in a complex immunoprecipitated from BMV-infected protoplasts with anti-B3a antiserum, implying an interaction between BCP and B3a.