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Add to Calendar 2/5/2018 1:00 pm 2/5/2018 America/Chicago CPLC Special Seminar: "Integrative Structure and Functional Anatomy of a Nuclear Pore Complex." DESCRIPTION:

Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data, including primarily stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, and tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the NPC’s central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.

\n\nSPEAKER:

Seung Joong Kim, University of California, San Francisco

276 Loomis

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CPLC Special Seminar: "Integrative Structure and Functional Anatomy of a Nuclear Pore Complex."

Speaker Seung Joong Kim, University of California, San Francisco
Date: 2/5/2018
Time: 1 p.m.
Location:

276 Loomis

Event Contact: Marjorie Gamel
217-333-3762
mgamel@illinois.edu
Sponsor:

Department of Physics

Event Type: Seminar/Symposium
 

Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data, including primarily stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, and tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the NPC’s central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.

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