PROTEIN TRANSLOCATION INTO PROTEOLIPOSOMES RECONSTITUTED FROM PURIFIED COMPONENTS OF THE ENDOPLASMIC-RETICULUM MEMBRANE
PROTEIN TRANSLOCATION INTO PROTEOLIPOSOMES RECONSTITUTED FROM PURIFIED COMPONENTS OF THE ENDOPLASMIC-RETICULUM MEMBRANE
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DOI：
10.1016/0092-8674(93)90483-7
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发表时间：
1993-11-19
期刊：
影响因子：
64.5
通讯作者：
RAPOPORT, TA
中科院分区：
文献类型：
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作者：
GORLICH, D;RAPOPORT, TA
我们已经复制了蛋白质运输的过程中，蛋白质整合到哺乳动物内质网膜通过使用蛋白脂质体重组从纯磷脂和纯化的膜蛋白。某些蛋白质的转运仅需要两种膜蛋白复合物：信号识别颗粒受体，用于将新生链靶向膜，以及一种新的复合物，Sec 61 p复合物，由Sec 61 p和两种较小的多肽组成。其他蛋白质的易位也需要易位链缔合膜（translocating chain-associated membrane，TRAM）蛋白的存在。将两种不同拓扑结构的膜蛋白整合到膜中不需要额外的组分。这些结果表明，一个令人惊讶的简单的基本易位机制。他们认为Sec 61 p复合物在易位过程中与核糖体结合，形成了假定的蛋白质传导通道。
We have reproduced the process of protein transport across and of protein integration into the mammalian endoplasmic reticulum membrane by the use of proteoliposomes reconstituted from pure phospholipids and purified membrane proteins. The transport of some proteins requires only two membrane protein complexes: the signal recognition particle receptor, needed for targeting of a nascent chain to the membrane, and a novel complex, the Sec61p complex, that consists of Sec61p and two smaller polypeptides. The translocation of other proteins also needs the presence of the translocating chain-associating membrane (TRAM) protein. The integration of two membrane proteins of different topologies into the membrane does not require additional components. These results indicate a surprising simplicity of the basic translocation machinery. They suggest that the Sec61p complex binds the ribosome during translocation and forms the postulated protein-conducting channel.