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Nascent polypeptide chains emerge from the exit domain of the large ribosomal subunit: immune mapping of the nascent chain.

机译:新生的多肽链从大核糖体亚基的出口结构域出现:新生链的免疫作图。

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摘要

The site of the nascent polypeptide chain as it leaves the ribosome has been localized on the "exit domain" of the Escherichia coli ribosome by using IgG antibodies directed against the enzyme beta-galactosidase (EC 3.2.1.23). Thus, a functional site has been mapped on intact 70S ribosomes. The exit site is on the large subunit, approximately 70 A from the interface between subunits and nearly 150 A from the central protuberance, the likely site of peptide transfer. It is adjacent to the region corresponding to the rough endoplasmic membrane binding region of the eukaryotic ribosome but distant from ribosomal components participating in mRNA recognition and polypeptide elongation (i.e., distant from the "translational domain"). These results, together with the protease protection experiments of others, provide evidence that the nascent protein chain probably passes through the ribosome in an unfolded, fully extended conformation.
机译:通过使用针对酶β-半乳糖苷酶(EC 3.2.1.23)的IgG抗体,新生多肽链离开核糖体时的位点已位于大肠杆菌核糖体的“出口域”上。因此,功能位点已定位在完整的70S核糖体上。出口位点在大的亚基上,距亚基之间的界面约70 A,距中央突起(肽转移的可能部位)约150A。它与对应于真核生物核糖体的粗糙内质膜结合区的区域相邻,但与参与mRNA识别和多肽延伸的核糖体组分相距较远(即与“翻译结构域”相距较远)。这些结果以及其他的蛋白酶保护实验提供了证据,表明新生的蛋白质链可能以未折叠的,完全延伸的构象穿过核糖体。

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  • 作者

    Bernabeu, C; Lake, J A;

  • 作者单位
  • 年度 1982
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  • 原文格式 PDF
  • 正文语种 en
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