The NH2 terminus of the herpes simplex virus type 1 regulatory protein ICP0 contains a promoter-specific transcription activation domain.
The NH2 terminus of the herpes simplex virus type 1 regulatory protein ICP0 contains a promoter-specific transcription activation domain.
复制标题
单纯疱疹病毒 1 型调节蛋白 ICP0 的 NH2 末端含有启动子特异性转录激活结构域。
DOI：
10.1128/jvi.72.10.7785-7795.1998
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发表时间：
1998
影响因子：
5.4
通讯作者：
Silverstein,SJ
中科院分区：
文献类型：
--
作者：
Lium,EK;Panagiotidis,CA;Wen,X;Silverstein,SJ
The transcriptional program of herpes simplex virus is regulated by the concerted action of three immediate-early (α) proteins, ICP4, ICP27, and ICP0. The experiments described in this study examine the role of the acidic amino terminus (amino acids 1 to 103) of ICP0 in gene activation. When tethered to a DNA binding domain, this sequence activates transcription in the yeastSaccharomyces cerevisiae. Deletion of these amino acids affects the ability of ICP0 to activate α-gene promoter reporters in transient expression assays, while it has little or no effect on a β- and a γ-gene reporter in the same assay. Viruses that express the deleted form of ICP0 (ICP0-NX) have a small-plaque phenotype on both Vero cells and the complementing cell line L7. Transient expression and immunofluorescence analyses demonstrate that ICP0-NX is a dominant negative form of ICP0. Immunoprecipitation of ICP0 from cells coinfected with viruses expressing ICP0-NX and ICP0 revealed that ICP0 oligomerizes in infected cells. These data, in conjunction with the finding that ICP0-N/X is dominant negative, provide both biochemical and genetic evidence that ICP0 functions as a multimer in infected cells.
