Mitchell C, Blaho J A, Roizman B
Marjorie B. Kovler Viral Oncology Laboratories, University of Chicago, IL 60637.
Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11864-8. doi: 10.1073/pnas.91.25.11864.
An earlier report has shown that eight viral proteins with a common amino acid sequence (R/P)RA(P/S)R are nucleotidylyated in vitro by nuclear extracts from cells infected with herpes simplex virus 1. One, the product of the alpha 22 gene, is nucleotidylylated in the absence of viral proteins made late in infection. A chimeric protein (GST22P) consisting of amino acids 50-200 of the alpha 22 coding sequence fused to the C terminus of the glutathione S-transferase was nucleotidylylated by enzymes in nuclear extracts of infected or mock-infected cells and also by a casein kinase II enzyme purified from the sea star. The enzyme did not nucleotidylylate common casein kinase II substrates (casein, phosvitin) and the reaction was inhibited by heparin. The results are consistent with the hypothesis that nucleotidylylation of the eight viral proteins involves casein kinase II.
一项较早的报告显示,具有共同氨基酸序列(R/P)RA(P/S)R的八种病毒蛋白在体外被感染单纯疱疹病毒1的细胞的核提取物进行核苷酸化。其中一种,即α22基因的产物,在没有感染后期产生的病毒蛋白的情况下被核苷酸化。一种嵌合蛋白(GST22P),由α22编码序列的50-200个氨基酸与谷胱甘肽S-转移酶的C末端融合而成,被感染或 mock 感染细胞的核提取物中的酶以及从海星纯化的酪蛋白激酶II酶进行核苷酸化。该酶不会对常见的酪蛋白激酶II底物(酪蛋白、卵黄高磷蛋白)进行核苷酸化,并且该反应受到肝素的抑制。这些结果与八种病毒蛋白的核苷酸化涉及酪蛋白激酶II的假设一致。