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 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.