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使转运与翻译解偶联:对蛋白质跨膜转运的影响。

Uncoupling translocation from translation: implications for transport of proteins across membranes.

作者信息

Perara E, Rothman R E, Lingappa V R

出版信息

Science. 1986 Apr 18;232(4748):348-52. doi: 10.1126/science.3961485.

DOI:10.1126/science.3961485
PMID:3961485
Abstract

The segregation of secretory proteins into the cisternae of the endoplasmic reticulum (ER) is normally tightly coupled to their synthesis. This feature distinguishes their biogenesis from that of proteins targeted to many other organelles. In the examples presented, translocation across the ER membrane is dissociated from translation. Transport, which is normally cotranslational, may proceed in the absence of chain elongation. Moreover, translocation across the ER membrane does not proceed spontaneously since, even in the absence of protein synthesis, energy substrates are required for translocation. These conclusions have been extended to the cotranslational integration of newly synthesized transmembrane proteins.

摘要

分泌蛋白在内质网(ER)潴泡中的分隔通常与其合成紧密偶联。这一特性使其生物发生过程有别于靶向许多其他细胞器的蛋白质。在给出的例子中,跨内质网膜的转运与翻译解离。通常为共翻译过程的转运,在缺乏链延伸的情况下也可能进行。此外,跨内质网膜的转运并非自发进行,因为即使在没有蛋白质合成的情况下,转运也需要能量底物。这些结论已扩展到新合成跨膜蛋白的共翻译整合。

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