Determining the architecture of nuclear ring of Xenopus laevis nuclear pore complex using integrated approaches

He Ren; Linhua Tai; Yun Zhu; Chun Chan; Qun Zhao; Jiashu Xu; Xiangyang Wang; Xinyao Ma; Lili Zhao; Xiaojun Huang; Guoliang Yin; Mingkang Jia; Xiaohong Zhu; Yuxin An; Zhao Gan; Changxiong Huang; Lihua Zhang; Jun Fan; Fei Sun; Chuanmao Zhang

doi:10.1101/2021.11.10.468004

Molecular BiologybioRxivNov 10, 2021

Preprint

Determining the architecture of nuclear ring of Xenopus laevis nuclear pore complex using integrated approaches

He Ren iD, Linhua Tai iD, Yun Zhu iD, Chun Chan iD, Qun Zhao iD, Jiashu Xu iD, Xiangyang Wang iD, Xinyao Ma iD, Lili Zhao iD, Xiaojun Huang iD, Guoliang Yin iD, Mingkang Jia, Xiaohong Zhu iD, Yuxin An iD, Zhao Gan iD, Changxiong Huang iD, Lihua Zhang iD, Jun Fan iD, Fei Sun iD, Chuanmao Zhang iD

Abstract

The nuclear pore complexes (NPCs) are large protein assemblies as a physical gate to regulate nucleocytoplasmic transport. Here, using integrated approaches including cryo-electron microscopy, hybrid homology modeling and cell experiment, we determined the architecture of the nuclear ring (NR) from Xenopus laevis oocytes NPC at subnanometer resolution. In addition to the improvement of the Y complex model, eight copies of Nup205 and ELYS were assigned in NR. Nup205 connects the inner and outer Y complexes and contributes to the assembly and stability of the NR. By interacting with both the inner Nup160 and the nuclear envelope (NE), the N-terminal {beta}-propeller and -solenoid domains of ELYS were found to be essential for accurate assembly of the NPC on the NE.

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