黄瓜花叶病毒RNA聚合酶2a蛋白的磷酸化抑制复制酶复合体的形成。
Phosphorylation of cucumber mosaic virus RNA polymerase 2a protein inhibits formation of replicase complex.
作者信息
Kim Sang Hyon, Palukaitis Peter, Park Young In
机构信息
Division of Life Sciences, and Graduate School of Biotechnology, Korea University, 1, 5-ga, Anam-dong, Sungbuk-gu, Seoul 136-701, Korea.
出版信息
EMBO J. 2002 May 1;21(9):2292-300. doi: 10.1093/emboj/21.9.2292.
Abstract
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.
摘要
黄瓜花叶病毒（CMV）的2a（聚合酶）蛋白在体内和体外均被证明可发生磷酸化。使用2a蛋白突变体和烟草蛋白激酶进行的体外试验表明，2a蛋白至少有三个磷酸化位点，其中一个位于N端126个氨基酸区域内。该区域对于与CMV 1a蛋白相互作用至关重要且足够。当在体外进行磷酸化时，2a蛋白的N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端区域的磷酸化在体内对这种相互作用产生负调节作用，并且可能在病毒感染中直接发挥调节作用。
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