The transactivation and DNA binding domains of the BPV-1 E2 protein have different roles in cooperative origin binding with the E1 protein
The transactivation and DNA binding domains of the BPV-1 E2 protein have different roles in cooperative origin binding with the E1 protein
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DOI：
10.1006/viro.1996.0351
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发表时间：
1996-07-01
期刊：
影响因子：
3.7
通讯作者：
McBride, AA
中科院分区：
文献类型：
--
作者：
Winokur, PL;McBride, AA
牛乳头瘤病毒E2反式激活蛋白增强了E1蛋白与病毒复制起点结合的能力，病毒复制起点包含一个E1结合位点，两侧有两个E2结合位点。为了确定E2蛋白的哪些区域和功能对这种合作相互作用是重要的，我们检测了一系列突变的E2蛋白增强E1来源特异性结合的能力。协同起始结合需要至少一个E2DNA结合位点、一个完整的功能性E2DNA结合域和一个完整的反式激活结构域。对于这种活性，E2蛋白的铰链区是不必要的。为了进一步研究E2C末端结构域的作用，用酵母GAL4DNA结合域取代了E2DNA结合域，构建了一系列嵌合蛋白。这些嵌合蛋白能够协同结合到一个含有GAL4结合位点而不是E2结合位点的杂交起源，这些研究表明，E2反式激活结构域足以与E1蛋白相互作用，而E2 DNA结合结构域是与原始DNA序列相互作用所必需的。(C)1996年学术出版社
The bovine papillomavirus E2 transactivator protein enhances the ability of the E1 protein to bind to the viral origin of replication which contains an E1 binding site flanked by two E2 binding sites. To determine which regions and functions of the E2 protein are important for this cooperative interaction, a series of mutated E2 proteins were assayed for their ability to enhance E1 origin-specific binding. Cooperative origin binding required at least one E2 DNA binding site, an intact functional E2 DNA binding domain, and an intact transactivation domain. The hinge region of the E2 proteins was dispensable for this activity. To further examine the role of the E2 C-terminal domain, a series of chimeric proteins were generated that substituted the yeast GAL4 DNA binding domain for the E2 DNA binding domain. These chimeric proteins were able to cooperatively bind to a hybrid origin that contained GAL4 binding sites in place of the E2 binding sites, These studies indicate that the E2 transactivation domain is sufficient for interaction with the E1 protein and that the E2 DNA binding domain is required for interaction with origin DNA sequences. (C) 1996 Academic Press, Inc