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噬菌体M13外壳蛋白的体外合成及其在膜中的组装。

Synthesis of phage M13 coat protein and its assembly into membranes in vitro.

作者信息

Wickner W, Mandel G, Zwizinski C, Bates M, Killick T

出版信息

Proc Natl Acad Sci U S A. 1978 Apr;75(4):1754-8. doi: 10.1073/pnas.75.4.1754.

Abstract

The coat protein (gene 8 product) of coliphage M1O is an integral protein of the host cell membrane at all stages of virus infection. This protein, when made in a cell-free reaction, has been shown by others to have an additional NH2-terminal peptide region and is referred to as "procoat." It is initially not membrane-bound but, upon exposure to Escherichia coli membrane vesicles or to liposomes prepared from E. coli lipids, it assembles into the bilayer in an integral fashion. Much of this protein is shown to be exposed on the inner surface of the liposome. We suggest that refolding of procoat as it encounters the bilayer is sufficient to transport large segments of the peptide chain through the apolar hydrocarbon core.

摘要

大肠杆菌噬菌体M1O的外壳蛋白(基因8产物)在病毒感染的各个阶段都是宿主细胞膜的整合蛋白。其他人已经证明,这种蛋白在无细胞反应中产生时,具有一个额外的NH2末端肽区域,被称为“前衣壳”。它最初不与膜结合,但在暴露于大肠杆菌膜泡或由大肠杆菌脂质制备的脂质体时,它以整合的方式组装到双层膜中。这种蛋白的大部分被证明暴露在脂质体的内表面。我们认为,前衣壳在遇到双层膜时的重新折叠足以将肽链的大部分片段运输通过非极性烃核心。

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