Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex
Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex
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DOI：
10.1093/emboj/21.9.2292
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发表时间：
2002-05-01
期刊：
影响因子：
11.4
通讯作者：
Park, YI
中科院分区：
文献类型：
--
作者：
Kim, SH;Palukaitis, P;Park, YI
黄瓜花叶病毒 (CMV) 的 2a（聚合酶）蛋白在体内和体外均被磷酸化。使用2a蛋白突变体和烟草蛋白激酶的体外测定表明，2a蛋白具有至少三个磷酸化位点，其中之一位于N端126个氨基酸区域内。该区域对于与 CMV 1a 蛋白的相互作用至关重要且足够。当体外磷酸化时，2a 蛋白 N 末端区域无法与 1a 蛋白相互作用。由于1a-2a相互作用对于CMV的复制至关重要，这表明2a蛋白N末端区域的磷酸化负向调节体内相互作用，并且可能在病毒感染中直接发挥调节作用。
The 2a (polymerase) protein of cucumber mosaic virus (CMV) was shown to be phosphorylated both in vivo and in vitro. In vitro assays using 2a protein mutants and tobacco protein kinases showed that the 2a protein has at least three phosphorylation sites, one of which is located within the N-terminal 126 amino acid region. This region is essential and sufficient for interaction with the CMV 1a protein. When phosphorylated in vitro, the 2a protein N-terminal region failed to interact with the 1a protein. Since the 1a-2a interaction is essential for the replication of CMV, this suggests that phosphorylation of the N-terminal region of the 2a protein negatively modulates the interaction in vivo, and may have a regulatory role acting directly in viral infection.