Nuclear Pore Membrane Proteins Self-Assemble into Nanopores

Nuclear Pore Membrane Proteins Self-Assemble into Nanopores

Large multiprotein nanopores remain difficult to reconstitute in vitro, such as, for instance, the nuclear pore complex (NPC) that regulates macromolecular transport between the nucleus and cytoplasm in cells. Here, we report that two NPC pore membrane proteins self-assemble into ∼20 nm diameter nan...

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Veröffentlicht in:Biochemistry (Easton) 2019-02, Vol.58 (6), p.484-488
Hauptverfasser: Panatala, Radhakrishnan, Barbato, Suncica, Kozai, Toshiya, Luo, Jinghui, Kapinos, Larisa E, Lim, Roderick Y. H
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container_end_page 488
container_issue 6
container_start_page 484
container_title Biochemistry (Easton)
container_volume 58
creator Panatala, Radhakrishnan
Barbato, Suncica
Kozai, Toshiya
Luo, Jinghui
Kapinos, Larisa E
Lim, Roderick Y. H
description Large multiprotein nanopores remain difficult to reconstitute in vitro, such as, for instance, the nuclear pore complex (NPC) that regulates macromolecular transport between the nucleus and cytoplasm in cells. Here, we report that two NPC pore membrane proteins self-assemble into ∼20 nm diameter nanopores following in vitro reconstitution into lipid bilayers. Pore formation follows from the assembly of Pom121 and Ndc1 oligomers, which arrange into ringlike membrane structures that encircle aqueous, electrically conductive pores. This represents a key step toward reconstituting membrane-embedded NPC mimics for biological studies and biotechnological applications.
doi_str_mv 10.1021/acs.biochem.8b01179
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