Nuclear Pore Membrane Proteins Self-Assemble into Nanopores

Panatala, Radhakrishnan and Barbato, Suncica and Kozai, Toshiya and Luo, Jinghui and Kapinos, Larisa E. and Lim, Roderick Y. H.. (2019) Nuclear Pore Membrane Proteins Self-Assemble into Nanopores. Biochemistry, 58 (6). pp. 484-488.

Full text not available from this repository.

Official URL: https://edoc.unibas.ch/68204/

Downloads: Statistics Overview


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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nanobiology Argovia (Lim)
UniBasel Contributors:Lim, Roderick Y.H. and Panatala Narendranath, Radhakrishnan and Barbato, Suncica and Kozai, Toshiya and Kapinos Schneider, Larisa E. E
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Chemical Society
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:03 Aug 2020 15:27
Deposited On:03 Aug 2020 15:27

Repository Staff Only: item control page