...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20
【24h】

Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20

机译：线粒体外膜受体Tom20的N端靶向信号结合域的表征

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

hTom20 is an outer mitochondrial membrane receptor involved in protein translocation. The cytosolic domain (aa30-145) and selected truncated versions of this domain were overexpressed and purified to study the structure-function relationship of this protein. Our studies reveal that the secondary structure of the cytosolic domain is very resistant to unfolding by guanidine-HCl and urea and is stabilized mainly by hydrophobic interactions. However, the tertiary structure of the N-terminal targeting signal binding domain (aa30-90) is more flexible. The first 30 amino acids of the cytosolic domain (aa30-60) are involved in recognizing N-terminal targeting signals and in stabilizing the cytosolic domain on the lipid surface. Moreover, we show that specifically aa30-48 interact with the membrane surface; a construct containing aa48-145 will only bind to the membrane surface in the presence of an N-terminal targeting signal peptide. The C-terminal region of hTom20 (aa141-145) interacts with the N-terminal region of hTom20, helping to stabilize the proper conformation of the N-terminal targeting signal binding domain. Finally, hTom20 interacts with the N-terminal targeting signal of preornithine carbamyl transferase fused to dihydrofolate reductase very weakly (K-d = 8 mu M), as would be expected if this interaction was the first in a series orchestrated by the import receptor complex to draw the targeted protein into the mitochondrion. [References: 29]
机译：hTom20是参与蛋白质易位的线粒体外膜受体。细胞质结构域（aa30-145）和此结构域的选定的截短版本被过表达和纯化，以研究该蛋白的结构-功能关系。我们的研究表明，胞质结构域的二级结构对胍盐酸盐和尿素的解折叠非常有抵抗力，并且主要通过疏水相互作用来稳定。然而，N末端靶向信号结合结构域（aa30-90）的三级结构更灵活。胞质结构域的前30个氨基酸（aa30-60）参与识别N端靶向信号并稳定脂质表面上的胞质结构域。此外，我们显示了aa30-48与膜表面的相互作用。含有aa48-145的构建体仅在N末端靶向信号肽存在下结合至膜表面。 hTom20的C末端区域（aa141-145）与hTom20的N末端区域相互作用，有助于稳定N末端靶向信号结合域的正确构象。最后，hTom20与融合到二氢叶酸还原酶的鸟氨酸氨基甲酰氨基转移酶的N端靶向信号相互作用非常弱（Kd = 8μM），如果这种相互作用是由进口受体复合物精心绘制的一系列序列中的第一个相互作用靶向蛋白质进入线粒体。 [参考：29]

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