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带有OmpA前导序列或大型羧基末端延伸的M13原衣壳重组形式保持其对secY功能的独立性。

Recombinant forms of M13 procoat with an OmpA leader sequence or a large carboxy-terminal extension retain their independence of secY function.

作者信息

Kuhn A, Kreil G, Wickner W

出版信息

EMBO J. 1987 Feb;6(2):501-5. doi: 10.1002/j.1460-2075.1987.tb04781.x.

DOI:10.1002/j.1460-2075.1987.tb04781.x
PMID:3034592
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC553422/
Abstract

The assembly of phage M13 procoat protein into the plasma membrane of Escherichia coli is independent of the secY protein. To test whether this is caused by the unusually small size of procoat, we fused DNA encoding 103 amino acids to the carboxy-terminal end of the procoat gene. The resulting fusion protein, which attains the same membrane-spanning conformation as mature coat protein, still does not require the secY function for membrane assembly. To determine whether the leader sequence governs interaction with the secY protein, we genetically exchanged the leader peptides between procoat and pro-OmpA, a protein which does require secY for its membrane assembly. Each of the resulting hybrid proteins assembles across the plasma membrane, though at a reduced rate. Membrane assembly of the fusion of procoat leader and OmpA required secY function, whereas assembly of the pro-OmpA leader/coat protein fusion was independent of secY. Properties of the entire procoat molecule, rather than its small size or a specific property of its leader peptide determines its mode of membrane assembly.

摘要

噬菌体M13前衣壳蛋白组装到大肠杆菌质膜中的过程不依赖于secY蛋白。为了测试这是否是由于前衣壳异常小的尺寸所致,我们将编码103个氨基酸的DNA融合到前衣壳基因的羧基末端。所得的融合蛋白与成熟衣壳蛋白具有相同的跨膜构象,但在膜组装过程中仍然不需要secY功能。为了确定前导序列是否控制与secY蛋白的相互作用,我们通过基因手段在前衣壳和前OmpA之间交换前导肽,前OmpA蛋白在膜组装过程中确实需要secY。尽管速率降低,但每个所得的杂合蛋白都能跨质膜组装。前衣壳前导肽与OmpA的融合体的膜组装需要secY功能,而前OmpA前导肽/衣壳蛋白融合体的组装则不依赖于secY。前衣壳分子的整体特性,而非其小尺寸或前导肽的特定特性,决定了其膜组装方式。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/b5bce74dd385/emboj00242-0209-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/24da940dc9b0/emboj00242-0206-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/27d297ff6905/emboj00242-0208-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/8daa80cc6383/emboj00242-0208-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/68c3ace65155/emboj00242-0209-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/b5bce74dd385/emboj00242-0209-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/24da940dc9b0/emboj00242-0206-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/27d297ff6905/emboj00242-0208-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/8daa80cc6383/emboj00242-0208-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/68c3ace65155/emboj00242-0209-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6f82/553422/b5bce74dd385/emboj00242-0209-b.jpg

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本文引用的文献

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The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism.带负电荷残基跨膜转运是由电化学势驱动的:类电泳膜转运机制的证据。
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ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle.纯化的大肠杆菌触发因子或犬信号识别颗粒可使ProOmpA稳定以进行膜转运。
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