Formation of the complex of bovine papillomavirus E1 and E2 proteins is modulated by E2 phosphorylation and depends upon sequences within the carboxyl terminus of E1.
Formation of the complex of bovine papillomavirus E1 and E2 proteins is modulated by E2 phosphorylation and depends upon sequences within the carboxyl terminus of E1.
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DOI：
10.1073/pnas.88.14.6363
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发表时间：
1991-07
影响因子：
11.1
通讯作者：
M. Lusky;E. Fontane
中科院分区：
文献类型：
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作者：
M. Lusky;E. Fontane
68 kDa 牛乳头瘤病毒 (BPV) 1 型复制蛋白 E1 和 48 kDa 反式激活蛋白 E2 形成特异性结合 DNA 的复合物 [Mohr, I.J., Clark, R., Sun, S., Androphy, E.J., MacPherson, P. & Botchan, M.R. (1990) Science 250, 1694-1699]。我们证实了这一观察结果，并表明 E1-E2 复合物与含有 BPV 质粒维持序列 1 和双向 BPV DNA 合成起始位点的 DNA 片段结合。发现 E1 蛋白优先与非磷酸化或磷酸化不足的 E2 种类结合，表明 E2 的磷酸化状态调节两种蛋白的结合。羧基末端有单个氨基酸取代和缺失的复制缺陷型 E1 突变体无法与 E2 相互作用，表明 E1 羧基末端的一个区域是 E1 与 E2 相互作用所必需的。我们的结果表明，一些 E1 突变体的复制缺陷反映了它们无法与 E2 结合。
The 68-kDa bovine papillomavirus (BPV) type 1 replication protein E1 and the 48-kDa transactivator protein E2 form a complex that specifically binds DNA [Mohr, I.J., Clark, R., Sun, S., Androphy, E.J., MacPherson, P. & Botchan, M.R. (1990) Science 250, 1694-1699]. We have confirmed this observation and shown that the E1-E2 complex binds to DNA fragments that contain the BPV plasmid maintenance sequence 1 and a site for the initiation of bidirectional BPV DNA synthesis. The E1 protein was found to bind preferentially to non- or underphosphorylated species of E2, suggesting that the phosphorylation state of E2 modulates the association of the two proteins. Replication-deficient E1 mutants with single amino acid substitutions and deletions in the carboxyl terminus failed to interact with E2, indicating that a region in the E1 carboxyl terminus is required for E1 to interact with E2. Our results suggest that the replication deficiency of some E1 mutants reflects their inability to associate with E2.