Kao S Y, Bauer W R
Virology. 1987 Aug;159(2):399-407. doi: 10.1016/0042-6822(87)90479-x.
One of the major DNA binding proteins contained in vaccinia virus is an 11-kDA species denoted VP11. The biosynthesis of VP11, a late polypeptide, occurs subsequent to the initiation of viral DNA replication. In particular, VP11 synthesis is blocked by cytosine arabinoside, a specific inhibitor of DNA synthesis. We show here that VP11 is specifically phosphorylated subsequent to translation. Phosphorylated VP11 is present both in viral core particles and in the cytoplasm of virus-infected cells. Kinetic analysis reveals that the total amount of phosphorylated VP11 species increases rapidly and remains approximately constant for as long as 17 hr postinfection. Phosphorylation occurs at two different serine residues, progressing from either site singly to the diphosphorylated product. Under steady-state conditions, the phosphorylated derivative constitutes approximately 85% of total VP11 in extracts of vaccinia virus-infected cells. Even though 15% of the VP11 remains unphosphorylated in cell extracts, only phosphorylated VP11 is found in mature viral cores.
痘苗病毒中含有的一种主要DNA结合蛋白是一种11 kDa的蛋白，称为VP11。VP11是一种晚期多肽，其生物合成发生在病毒DNA复制起始之后。特别地，VP11的合成被阿糖胞苷（一种DNA合成的特异性抑制剂）所阻断。我们在此表明，VP11在翻译后被特异性磷酸化。磷酸化的VP11存在于病毒核心颗粒以及病毒感染细胞的细胞质中。动力学分析表明，磷酸化VP11的总量迅速增加，并在感染后长达17小时内大致保持恒定。磷酸化发生在两个不同的丝氨酸残基上，从任一单一位点进展到双磷酸化产物。在稳态条件下，磷酸化衍生物在痘苗病毒感染细胞提取物中占总VP11的约85%。尽管在细胞提取物中15%的VP11仍未磷酸化，但在成熟病毒核心中仅发现磷酸化的VP11。
