中文摘要：

疱疹的功能单一的病毒类型 1 (HSV-1 ) UL4 蛋白质仍然是逃犯的。我们的目的是调查 UL4 蛋白质的 subcellular 运输机制。在这研究，荧光显微镜学被采用调查 UL4 的 subcellular 本地化并且在生活房间描绘运输机制。由构造与提高的黄熔化的一系列删除异种荧光灯蛋白质(EYFP ) ， UL4 的原子出口信号(NES ) 第一次被印射到氨基酸残余 178 ～ 186。另外， N 终端 19 氨基酸被识别为 UL4 的像小粒的细胞质的模式被要求。而且， UL4 蛋白质被表明在 chromosomal 区域维护通过 NES 被出口到细胞质 1 (CRM1 ) 依赖举止包含 RanGTP 水解作用。

英文摘要：

The function of the herpes simplex virus type 1 （HSV-1） UL4 protein is still elusive. Our objective is to investigate the subcellular transport mechanism of the UL4 protein. In this study, fluorescence microscopy was employed to investigate the subcellular localization of UL4 and characterize the transport mechanism in living cells. By constructing a series of deletion mutants fused with enhanced yellow fluorescent protein （EYFP）, the nuclear export signals （NES） of UL4 were for the first time mapped to amino acid residues 178 to 186. In addition, the N-terminal 19 amino acids are identified to be required for the granule-like cytoplasmic pattem of UL4. Furthermore, the UL4 protein was demonstrated to be exported to the cytoplasm through the NES in a chromosomal region maintenance 1 （CRM1）-dependent manner involving RanGTP hydrolysis