• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Herpes simplex virus 1 α regulatory protein ICPO functionally interacts with cellular transcription factor BMAL1
【24h】

Herpes simplex virus 1 α regulatory protein ICPO functionally interacts with cellular transcription factor BMAL1

机译：单纯疱疹病毒1α调节蛋白ICPO在功能上与细胞转录因子BMAL1相互作用

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The infected cell protein no. 0 (ICP0) of herpes simplex virus 1 (HSV-1) is a promiscuous transactivator shown to enhance the expression of gene introduced into cells by infection or transfec- tion. At the molecular level, ICP0 is a 77S-aa ring finger protein localized initially in the nucleus and late in infection in the cyto- plasm and mediates the degradation of several proteins and stabilization of others. None of the known functions at the mo- lecular level account for the apparent activity of ICP0 as a trans- activator. Here we report that ICP0 functionally interacts with cellular transcription factor BMAL1, a member of the basic helix- loop--helix PER-ARNT-SIM (PAS) super family of transcriptional regulators. Specifically, sequences mapped to the exon Ⅱ of ICP0 interacted with BMAL1 in the yeast two-hybrid system and in reciprocal pull-down experiments in vitro. Moreover, the enhance- ment of transcription of a luciferase reporter construct whose promoter contained multiple BMAL1-binding sites by ICP0 and BMAL1 was significantly greater than that observed by ICP0 or BMAL1 alone. Although the level of BMAL1 present in nuclei of infected cells remained unchanged between 3 and 8 h after infection, the level of cytoplasmic BMAL1 was reduced at 8 h after infection. The reduction of cytoplasmic BMAL1 was significantly greater in cells infected with the ICP0-null mutant than in the wild-type virus-infected cells, suggesting that ICP0 mediates partial stabilization of the protein. These results indicate that ICP0 inter- acts physically and functionally with at least one cellular transcrip- tion-regulatory factor.
机译：感染的细胞蛋白编号单纯疱疹病毒1（HSV-1）的0（ICP0）是一种混杂的反式激活因子，可增强通过感染或转染引入细胞的基因的表达。在分子水平上，ICP0是一种77S-aa无名指蛋白，最初位于细胞核内，而在细胞质感染后期才定位，并介导了几种蛋白质的降解和其他蛋白质的稳定化。分子水平上的已知功能均无法解释ICP0作为反式激活剂的表观活性。在这里我们报道ICP0在功能上与细胞转录因子BMAL1相互作用，BMAL1是基本螺旋环-螺旋PER-ARNT-SIM（PAS）转录调节子超家族的成员。具体而言，在酵母双杂交系统中以及在相互的下拉实验中，定位到ICP0外显子Ⅱ的序列与BMAL1相互作用。此外，萤光素酶报告基因构建体的转录增强作用，其启动子通过ICP0和BMAL1包含多个BMAL1结合位点，明显比单独使用ICP0或BMAL1观察到的增强。尽管在感染后3至8小时内存在于被感染细胞核中的BMAL1水平保持不变，但在感染后8 h细胞质BMAL1水平却降低了。在ICP0-null突变体感染的细胞中，胞质BMAL1的减少明显大于野生型病毒感染的细胞，这表明ICP0介导了蛋白质的部分稳定。这些结果表明，ICP0与至少一种细胞转录调节因子在物理和功能上相互作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号