Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography
Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography
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通过 X 射线晶体学揭示 Sec Translocon 和 YidC 的结构基础
DOI：
10.1007/s10930-019-09830-x
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Tsukazaki Tomoya
中科院分区：
文献类型：
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作者：
Heungjin Ryu;David A Hill;Tetsuya Sakamaki;Cintia Garai;Nahoko Tokuyama;Takeshi Furuichi;Tsukazaki Tomoya
蛋白质转运和膜整合是基本的、保守的过程。在核糖体蛋白质合成后或合成过程中，含有N-末端信号序列的前体蛋白被定向到真核细胞内质网膜或细菌细胞质膜上的一个保守的膜蛋白复合体，称为SEC转位蛋白(也称为SEC转位酶)。SEC转运子由真核细胞中的Sec61复合体或细菌中的SecY复合体组成，介导底物蛋白的跨膜/入膜转运。几种膜蛋白与SEC转运子相关。在大肠杆菌中，膜蛋白YidC不仅与SEC转位蛋白一起作为膜蛋白生物发生的伴侣，而且还作为一种独立的膜蛋白插入酶发挥作用。为了了解膜上这些动态过程背后的分子机制，需要这些蛋白质的高分辨率结构模型。本文综述了SEC易位子和YIDC的X射线结晶学分析，并讨论了蛋白质转运和整合的结构基础。
Protein translocation and membrane integration are fundamental, conserved processes. After or during ribosomal protein synthesis, precursor proteins containing an N-terminal signal sequence are directed to a conserved membrane protein complex called the Sec translocon (also known as the Sec translocase) in the endoplasmic reticulum membrane in eukaryotic cells, or the cytoplasmic membrane in bacteria. The Sec translocon comprises the Sec61 complex in eukaryotic cells, or the SecY complex in bacteria, and mediates translocation of substrate proteins across/into the membrane. Several membrane proteins are associated with the Sec translocon. InEscherichia coli, the membrane protein YidC functions not only as a chaperone for membrane protein biogenesis along with the Sec translocon, but also as an independent membrane protein insertase. To understand the molecular mechanism underlying these dynamic processes at the membrane, high-resolution structural models of these proteins are needed. This review focuses on X-ray crystallographic analyses of the Sec translocon and YidC and discusses the structural basis for protein translocation and integration.