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本文引用的文献

1
Structures of the scanning and engaged states of the mammalian SRP-ribosome complex.哺乳动物信号识别颗粒-核糖体复合物的扫描和结合状态的结构。
Elife. 2015 Jul 9;4:e07975. doi: 10.7554/eLife.07975.
2
Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.伴侣蛋白的调控可提高共翻译蛋白质靶向过程中的底物选择性。
Proc Natl Acad Sci U S A. 2015 Jun 23;112(25):E3169-78. doi: 10.1073/pnas.1422594112. Epub 2015 Jun 8.
3
Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.内质网Sec61转运体中Sec62/63的共翻译稳定由不同的底物驱动转运事件控制。
Mol Cell. 2015 Apr 16;58(2):269-83. doi: 10.1016/j.molcel.2015.02.018. Epub 2015 Mar 19.
4
Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.处于关闭状态的核糖体 - SRP - FtsY共翻译靶向复合体。
Proc Natl Acad Sci U S A. 2015 Mar 31;112(13):3943-8. doi: 10.1073/pnas.1424453112. Epub 2015 Mar 16.
5
Diversity and selectivity in mRNA translation on the endoplasmic reticulum.内质网上mRNA翻译的多样性与选择性
Nat Rev Mol Cell Biol. 2015 Apr;16(4):221-31. doi: 10.1038/nrm3958. Epub 2015 Mar 4.
6
Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling.通过邻近特异性核糖体分析揭示的内质网共翻译转运原理。
Science. 2014 Nov 7;346(6210):1257521. doi: 10.1126/science.1257521. Epub 2014 Nov 6.
7
Real-time observation of signal recognition particle binding to actively translating ribosomes.信号识别颗粒与正在进行翻译的核糖体结合的实时观察。
Elife. 2014 Oct 30;3:e04418. doi: 10.7554/eLife.04418.
8
Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution.哺乳动物核糖体-Sec61复合物的结构,分辨率达3.4埃。
Cell. 2014 Jun 19;157(7):1632-43. doi: 10.1016/j.cell.2014.05.024. Epub 2014 Jun 12.
9
Co-translational mechanisms of protein maturation.蛋白质成熟的共翻译机制。
Curr Opin Struct Biol. 2014 Feb;24:24-33. doi: 10.1016/j.sbi.2013.11.004. Epub 2013 Dec 12.
10
Embracing the void--how much do we really know about targeting and translocation to the endoplasmic reticulum?拥抱虚空——我们对靶向和易位到内质网的了解到底有多少?
Curr Opin Cell Biol. 2014 Aug;29:8-17. doi: 10.1016/j.ceb.2014.02.004. Epub 2014 Mar 21.

共翻译蛋白质靶向的动力学

Dynamics of co-translational protein targeting.

作者信息

Elvekrog Margaret M, Walter Peter

机构信息

The Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143, United States.

The Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California, San Francisco, San Francisco, CA 94143, United States.

出版信息

Curr Opin Chem Biol. 2015 Dec;29:79-86. doi: 10.1016/j.cbpa.2015.09.016. Epub 2015 Oct 30.

DOI:10.1016/j.cbpa.2015.09.016
PMID:26517565
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4684440/
Abstract

Most membrane and secretory proteins are delivered co-translationally to protein translocation channels in their destination membrane by the signal recognition particle (SRP) and its receptor. This co-translational molecular machinery is conserved across all kingdoms of life, though it varies in composition and function. Here we report recent progress towards understanding the mechanism of SRP function, focusing on findings about Escherichia coli SRP's conformational dynamics throughout the targeting process. These insights shed light on a key checkpoint in the targeting cycle: how SRP regulates engagement of an actively translating ribosome with the translocation machinery at the membrane.

摘要

大多数膜蛋白和分泌蛋白通过信号识别颗粒(SRP)及其受体在翻译过程中被递送至其目的地膜中的蛋白质转运通道。这种共翻译分子机制在所有生命王国中都是保守的,尽管其组成和功能有所不同。在这里,我们报告了在理解SRP功能机制方面的最新进展,重点关注关于大肠杆菌SRP在整个靶向过程中的构象动力学的研究结果。这些见解揭示了靶向循环中的一个关键检查点:SRP如何调节正在进行翻译的核糖体与膜上转运机制的结合。