...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Molecular and Cellular Biology >Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic.
【24h】

Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic.

机译：鉴定和表征脊椎动物的多梳子组蛋白BMI1和人类多同源同系物之间的相互作用。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In Drosophila melanogaster, the Polycomb-group (PcG) genes have been identified as repressors of gene expression. They are part of a cellular memory system that is responsible for the stable transmission of gene activity to progeny cells. PcG proteins form a large multimeric, chromatin-associated protein complex, but the identity of its components is largely unknown. Here, we identify two human proteins, HPH1 and HPH2, that are associated with the vertebrate PcG protein BMI1. HPH1 and HPH2 coimmunoprecipitate and cofractionate with each other and with BMI1. They also colocalize with BMI1 in interphase nuclei of U-2 OS human osteosarcoma and SW480 human colorectal adenocarcinoma cells. HPH1 and HPH2 have little sequence homology with each other, except in two highly conserved domains, designated homology domains I and II. They share these homology domains I and II with the Drosophila PcG protein Polyhomeotic (Ph), and we, therefore, have named the novel proteins HPH1 and HPH2. HPH1, HPH2, and BMI1 show distinct, although overlapping expression patterns in different tissues and cell lines. Two-hybrid analysis shows that homology domain II of HPH1 interacts with both homology domains I and II of HPH2. In contrast, homology domain I of HPH1 interacts only with homology domain II of HPH2, but not with homology domain I of HPH2. Furthermore, BMI1 does not interact with the individual homology domains. Instead, both intact homology domains I and II need to be present for interactions with BMI1. These data demonstrate the involvement of homology domains I and II in protein-protein interactions and indicate that HPH1 and HPH2 are able to heterodimerize.
机译：在果蝇中，Polycomb-group（PcG）基因已被鉴定为基因表达的阻遏物。它们是细胞记忆系统的一部分，负责将基因活性稳定地传递给子代细胞。 PcG蛋白形成了大型的多聚体，与染色质相关的蛋白复合物，但是其成分的身份在很大程度上尚不清楚。在这里，我们确定了两个人类蛋白，HPH1和HPH2，它们与脊椎动物PcG蛋白BMI1相关。 HPH1和HPH2相互之间以及与BMI1共免疫沉淀和共馏分。它们还与BMI1在U-2 OS人类骨肉瘤和SW480人类结直肠腺癌细胞的间期核中共定位。 HPH1和HPH2彼此之间几乎没有序列同源性，除了在两个高度保守的域中，称为同源性域I和II。他们与果蝇PcG蛋白Polyhomeotic（Ph）共享这些同源结构域I和II，因此，我们将其命名为新型蛋白HPH1和HPH2。尽管在不同的组织和细胞系中有重叠的表达模式，但HPH1，HPH2和BMI1表现出不同的特征。两杂交分析表明，HPH1的同源域II与HPH2的同源域I和II相互作用。相反，HPH1的同源结构域I仅与HPH2的同源结构域II相互作用，而与HPH2的同源结构域I不相互作用。此外，BMI1不与各个同源域相互作用。取而代之的是，与BMI1的相互作用都需要同时存在完整的同源域I和II。这些数据表明同源域I和II参与蛋白质-蛋白质相互作用，并表明HPH1和HPH2能够异源二聚化。

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