Eibauer Matthias, Pellanda Mauro, Turgay Yagmur, Dubrovsky Anna, Wild Annik, Medalia Ohad
Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, Zurich 8057, Switzerland.
1] Department of Biochemistry, University of Zurich, Winterthurerstrasse 190, Zurich 8057, Switzerland [2] Department of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University, Beer-Sheva 84105, Israel.
Nat Commun. 2015 Jun 26;6:7532. doi: 10.1038/ncomms8532.
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 Å 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.
核孔复合体（NPCs）贯穿核膜，允许大分子在细胞核与细胞质之间进行交换。为了更深入地了解这种转运机制，我们通过冷冻电子断层扫描结合亚断层平均技术，从天然核膜重建非洲爪蟾卵母细胞NPC，直至20埃分辨率，分析了NPC支架和渗透屏障的结构。除了解析NPC组成成分的各个蛋白质结构域，我们还提出了其中心通道处分子门结构的模型。此外，我们将这种天然NPC结构与一种转运活性降低的结构进行了比较和对比，揭示了NPC门的空间特性。
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