Biosynthesis and phosphorylation of vaccinia virus structural protein VP11.
Biosynthesis and phosphorylation of vaccinia virus structural protein VP11.
复制标题
痘苗病毒结构蛋白VP11的生物合成和磷酸化。
DOI：
10.1016/0042-6822(87)90479-x
复制
发表时间：
1987
期刊：
影响因子：
3.7
通讯作者：
Bauer,WR
中科院分区：
文献类型：
--
作者：
Kao,SY;Bauer,WR
痘苗病毒中包含的主要 DNA 结合蛋白之一是 11-kDA 物种，称为 VP11。 VP11（一种晚期多肽）的生物合成发生在病毒 DNA 复制开始后。特别是，VP11 的合成被阿糖胞苷（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和病毒感染细胞的细胞质中。动力学分析表明，磷酸化 VP11 种类的总量迅速增加，并在感染后长达 17 小时内保持大致恒定。磷酸化发生在两个不同的丝氨酸残基处，从任一位点单独进展为二磷酸化产物。在稳态条件下，痘苗病毒感染细胞提取物中磷酸化衍生物约占总 VP11 的 85%。尽管细胞提取物中 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。
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.