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Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex.

Parthasarathy Sampathkumar1, Seung Joong Kim, Paula Upla

  • 1Department of Biochemistry, Ullmann Building, Room 409, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.

Structure (London, England : 1993)
|March 19, 2013
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Summary

The crystal structure of Saccharomyces cerevisiae Nup192 reveals its three-domain α-helical fold and conformational flexibility. This finding suggests Nup192 modulates nuclear pore complex permeability, impacting nucleocytoplasmic transport.

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Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Nuclear pore complexes (NPCs) regulate nucleocytoplasmic transport in eukaryotes.
  • Nup192 is a key protein component of the NPC's inner ring structure.

Purpose of the Study:

  • Determine the crystal structure of Saccharomyces cerevisiae Nup192 (ScNup192) residues 2-960.
  • Investigate the conformational dynamics and evolutionary origins of Nup192.
  • Elucidate the role of Nup192 in NPC function and nuclear transport.

Main Methods:

  • X-ray crystallography to determine the structure of ScNup192(2-960).
  • Small-angle X-ray scattering (SAXS) and electron microscopy (EM) to study conformational transitions.
  • Homology modeling and evolutionary analyses to build a full-length ScNup192 model and infer evolutionary relationships.

Main Results:

  • The crystal structure of ScNup192(2-960) revealed a three-domain α-helical fold.
  • SAXS and EM studies demonstrated that ScNup192(2-960) can transition between open and closed conformations.
  • Evolutionary analysis suggests a common ancestor for NPCs and vesicle-coating complexes.
  • Suppression of Nup192 expression impaired nuclear transport.

Conclusions:

  • ScNup192 exhibits conformational flexibility, potentially regulating NPC central channel permeability.
  • Nup192 plays a crucial role in maintaining efficient nucleocytoplasmic transport.
  • The findings provide insights into the structural basis and evolutionary history of the nuclear pore complex.