中文摘要：

原子蛋白质经常形成 punctiform 结构，而是精确机制因为这个过程是未知的。作为初步的研究，我们立即早调查了 HSV-1 的聚集蛋白质，感染房间的蛋白质 22 (ICP22 ) ，在由观察 ICP22-EGFP 的本地化的原子核熔化蛋白质。结果证明处于高级表示条件， ICP22-EGFP 逐渐地在原子核专注，没有崩溃，全部甚至在房间部门阶段坚持房间周期，并且对女儿房间最后分布式。我们随后构造了一个哺乳动物的房间表示系统，它有四圜素依赖者 transcriptional 管理者。因而，在原子核的 ICP22-EGFP 的地点随着不同正式就职条件变化了。这建议 ICP22 的细胞的地点被倡导者规定也影响，除了它的自己的结构。我们的调查结果为病毒的基因的 transcriptional 规定的调查提供新线索。另外，我们构造了的非朊酶记者系统能被利用在 transcriptional 规定上评估内部核糖体入口地点(怒火) 的角色。关键词疱疹单一的病毒 1 (HSV-1 )- ICP22 - Transcriptional 规定 - 细胞的本地化 - 原子功能的领域基础项目：中国的国家自然科学基础(30670094， 30700028 ) 并且中国(2006-0023008 ) 的教育部的博士程序基础相等的贡献作者。

英文摘要：

Nuclear proteins often form punctiform structures, but the precise mechanism for this process is unknown. As a preliminary study, we investigated the aggregation of an HSV-1 immediate-early protein, infected-cell protein 22 （ICP22）, in the nucleus by observing the localization of ICP22-EGFP fusion protein Results showed that, in high-level expression conditions, ICP22-EGFP gradually concentrates in the nucleus, persists throughout the cell cycle without disaggregation even in the cell division phase, and is finally distributed to daughter cells. We subsequently constructed a mammalian cell expression system, which had tetracycline- dependent transcriptional regulators. Consequently, the location of ICP22-EGFP in the nucleus changed with distinct induction conditions. This suggests that the cellular location of ICP22 is also influenced by promoter regulation, in addition to its own structure. Our findings provide new clues for the investigation of transcriptional regulation of viral genes. In addition, the non-protease reporter system we constructed could be utilized to evaluate the role of intemal ribosome entry sites （IRES） on transcriptional regulation.