Structure and gating of the nuclear pore complex

被引:135
作者
Eibauer, Matthias [1 ]
Pellanda, Mauro [1 ]
Turgay, Yagmur [1 ]
Dubrovsky, Anna [1 ]
Wild, Annik [1 ]
Medalia, Ohad [1 ,2 ,3 ]
机构
[1] Univ Zurich, Dept Biochem, CH-8057 Zurich, Switzerland
[2] Ben Gurion Univ Negev, Dept Life Sci, IL-84105 Beer Sheva, Israel
[3] Ben Gurion Univ Negev, Natl Inst Biotechnol, IL-84105 Beer Sheva, Israel
来源
NATURE COMMUNICATIONS | 2015年 / 6卷
基金
瑞士国家科学基金会;
关键词
SUPERRESOLUTION MICROSCOPY; MOLECULAR ARCHITECTURE; TRANSPORT; NUCLEOPORINS; TOMOGRAPHY; HYDROGEL; PROTEINS; CELLS;
D O I
10.1038/ncomms8532
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Nuclear pore complexes (NPCs) perforate the nuclear envelope and allow the exchange of macromolecules between the nucleus and the cytoplasm. To acquire a deeper understanding of this transport mechanism, we analyse the structure of the NPC scaffold and permeability barrier, by reconstructing the Xenopus laevis oocyte NPC from native nuclear envelopes up to 20 angstrom resolution by cryo-electron tomography in conjunction with subtomogram averaging. In addition to resolving individual protein domains of the NPC constituents, we propose a model for the architecture of the molecular gate at its central channel. Furthermore, we compare and contrast this native NPC structure to one that exhibits reduced transport activity and unveil the spatial properties of the NPC gate.
引用
收藏
页数:9
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