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新生成的分泌蛋白可能以伸展链的形式穿过核糖体/内质网转位酶复合体。

A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain.

作者信息

Whitley P, Nilsson I M, von Heijne G

机构信息

Department of Biochemistry, Stockholm University, Sweden.

出版信息

J Biol Chem. 1996 Mar 15;271(11):6241-4. doi: 10.1074/jbc.271.11.6241.

DOI:10.1074/jbc.271.11.6241
PMID:8626416
Abstract

We have measured the minimum number of residues in a translocating polypeptide required to bridge the distance between the P-site in endoplasmic reticulum-bound ribosomes and the lumenally disposed active site of the oligosaccharyl transferase. The results suggest that a nascent chain may traverse the ribosome/translocase complex in a largely extended conformation, and that hydrophobic stop-transfer segments have a more compact, possibly alpha-helical conformation in the translocase.

摘要

我们已经测量了转运多肽中跨越内质网结合核糖体的P位点与腔面寡糖基转移酶活性位点之间距离所需的最小残基数。结果表明,新生肽链可能以大体伸展的构象穿过核糖体/转位酶复合物,并且疏水的停止转移片段在转位酶中具有更紧密的构象,可能是α-螺旋构象。

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1
A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain.新生成的分泌蛋白可能以伸展链的形式穿过核糖体/内质网转位酶复合体。
J Biol Chem. 1996 Mar 15;271(11):6241-4. doi: 10.1074/jbc.271.11.6241.
2
Different conformations of nascent polypeptides during translocation across the ER membrane.新生多肽在跨内质网膜转运过程中的不同构象。
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The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase.内部信号序列和信号锚定序列的羧基末端在内质网转位酶中的定位不同。
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Nascent secretory polypeptides synthesized on Escherichia coli ribosomes are not translocated across mammalian endoplasmic reticulum.在大肠杆菌核糖体上合成的新生分泌性多肽不会转运穿过哺乳动物内质网。
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Nascent polypeptide-associated complex protein prevents mistargeting of nascent chains to the endoplasmic reticulum.新生多肽相关复合体蛋白可防止新生肽链错误靶向内质网。
Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5411-5. doi: 10.1073/pnas.92.12.5411.
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A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation.在转运过程中,SECP61和SECYp的哺乳动物同源物与核糖体和新生多肽相关联。
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Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins.新生膜蛋白和分泌蛋白在核糖体内部深处通过荧光共振能量转移(FRET)检测到的折叠情况以及它们与核糖体蛋白的接触情况方面存在差异。
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Stop-and-move of a marginally hydrophobic segment translocating across the endoplasmic reticulum membrane.边缘疏水性片段在穿过内质网膜时的停止-移动。
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Regulation of ribosome detachment from the mammalian endoplasmic reticulum membrane.核糖体从哺乳动物内质网膜上脱离的调控
J Biol Chem. 2000 Oct 27;275(43):33828-35. doi: 10.1074/jbc.M005294200.

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