文献类型: 外文期刊
作者: Ou, Xiaomin 1 ; Ma, Chengying 1 ; Sun, Dongjie 1 ; Xu, Jinkun 1 ; Wang, Yang 2 ; Wu, Xiaofei 1 ; Wang, Dali 2 ; Yang, Song 2 ; Gao, Ning 1 ; Song, Chen 2 ; Li, Long 1 ;
作者机构: 1.Peking Univ, Peking Tsinghua Ctr Life Sci, Sch Life Sci, State Key Lab Membrane Biol, Beijing, Peoples R China
2.Peking Univ, Acad Adv Interdisciplinary Studies, Ctr Quantitat Biol, Beijing, Peoples R China
3.Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing, Peoples R China
4.Peking Univ, Natl Biomed Imaging Ctr, Beijing Adv Ctr RNA Biol BEACON, Beijing 100871, Peoples R China
5.Changping Lab, Beijing, Peoples R China
6.Chinese Acad Agr Sci, Inst Anim Sci, Beijing, Peoples R China
7.Peking Univ, Sch Basic Med Sci, Beijing, Peoples R China
8.Univ Chinese Acad Sci, Ctr Biomed Phys, Wenzhou Inst, Wenzhou Key Lab Biomed Imaging, Wenzhou, Zhejiang, Peoples R China
9.Binzhou Med Univ, Sch Basic Med Sci, Yantai, Shandong, Peoples R China
10.Fuzhou Univ, Sch Med, Fuzhou, Fujian, Peoples R China
期刊名称:CELL ( 影响因子:42.5; 五年影响因子:48.9 )
ISSN: 0092-8674
年卷期: 2025 年 188 卷 7 期
页码:
收录情况: SCI
摘要: The Sec translocon is vital for guiding membrane protein insertion into lipid bilayers. The insertion and folding processes of membrane proteins are poorly understood. Here, we report cryo-electron microscopy structures of multi-spanning membrane proteins inserting through the SecY channel, the Sec translocon in prokaryotes. The high-resolution structures illustrate how bulky amino acids pass the narrow channel restriction. Comparison of different translocation states reveals that the cytoplasmic and extracellular cavities of the channel create distinct environments for promoting the unfolding and folding of transmembrane segments (TMs), respectively. Released substrate TMs are either flexible or stabilized by an unexpected hydrophilic groove between TM3 and TM4 of SecY. Disruption of the groove causes global defects in the folding of the membrane proteome. These findings demonstrate that beyond its role as a passive protein-conducting channel, the SecY translocon actively serves as a chaperone, employing multiple mechanisms to promote membrane protein insertion and folding.
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