THE C-TERMINAL 79 AMINO-ACIDS OF THE HERPES-SIMPLEX VIRUS REGULATORY PROTEIN, VMW65, EFFICIENTLY ACTIVATE TRANSCRIPTION IN YEAST AND MAMMALIAN-CELLS IN CHIMERIC DNA-BINDING PROTEINS
THE C-TERMINAL 79 AMINO-ACIDS OF THE HERPES-SIMPLEX VIRUS REGULATORY PROTEIN, VMW65, EFFICIENTLY ACTIVATE TRANSCRIPTION IN YEAST AND MAMMALIAN-CELLS IN CHIMERIC DNA-BINDING PROTEINS
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DOI：
10.1002/j.1460-2075.1989.tb08361.x
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发表时间：
1989-08-01
期刊：
影响因子：
11.4
通讯作者：
OHARE, P
中科院分区：
文献类型：
--
作者：
COUSENS, DJ;GREAVES, R;OHARE, P
单纯疱疹病毒即刻早期基因表达的激活通常需要病毒反式激活剂Vmw65、细胞八聚体结合蛋白TRF和顺式作用靶序列TAATGARAT基序之间形成三元复合体。我们报道，Vmw65的C端79个氨基酸含有一个潜在的酸性两亲性螺旋，当与酵母转录因子GAL4的DNA结合域融合时，可以在没有TRF相互作用的情况下激活酵母和哺乳动物细胞的转录。结合我们以前的报道，表明Vmw65将TRF募集到DNA中不足以激活转录，这些结果表明八聚体结合蛋白可能不直接参与Vmw65介导的转录诱导。因此，TRF-Vmw65复合体可能代表了一类新的转录激活剂，其中负责序列特异性DNA结合的蛋白质结构域位于TRF中，而Vmw65中诱导转录所需的蛋白质结构域位于不同的蛋白质上。这些结果被参考组合转录调控和八聚体结合蛋白在其他系统中的作用进行了讨论。
Activation of herpes simplex virus immediate early gene expression normally requires the formation of a ternary complex between a virus trans-activator, Vmw65, a cellular octamer-binding protein, TRF and the cis-acting target sequence, the TAATGARAT motif. We report that the C-terminal 79 amino acids of Vmw65, which contain a potential acidic amphipathic helix, can activate transcription in both yeast and mammalian cells in the absence of TRF interaction when fused to the DNA-binding domain of the yeast transcription factor, GAL4. Together with our previous report which showed that the recruitment of TRF to the DNA by Vmw65 insufficient for transcription activation, these results indicate that the octamer binding protein may not be directly involved in transcriptional induction mediated by Vmw65. The TRF-Vmw65 complex may therefore represent a novel class of transcription activator in which the protein domain responsible for sequence-specific DNA binding, present in TRF, and that necessary for induction of transcription, within Vmw65, are located on separate proteins. These results are discussed with reference to combinatorial transcriptional control and the role of octamer-binding proteins in other systems.