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The Yeast Nuclear Pore Complex

The Journal of Cell Biology · 2000 · Vol. 148(4) · pp. 635–652
Michael P. RoutJohn D. AitchisonAdisetyantari SupraptoKelly HjertaasYingming ZhaoBrian T. Chait

Abstract

An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

Nuclear Structure and FunctionRNA Research and SplicingGenomics and Chromatin DynamicsNucleoporinNuclear poreNuclear transportYeastComponent (thermodynamics)Cell biologyComputational biologyBiologyChemistryCytoplasm

MeSH terms

Biological TransportCarrier ProteinsChromatography, High Pressure LiquidFluorescent Antibody TechniqueFungal ProteinsMembrane ProteinsModels, BiologicalMolecular WeightNuclear EnvelopeNuclear ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMicroscopy, ImmunoelectronSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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