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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Biological Transport
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Carrier Proteins / analysis
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Carrier Proteins / chemistry
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Carrier Proteins / genetics
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Chromatography, High Pressure Liquid
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Fluorescent Antibody Technique
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Fungal Proteins / analysis*
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Fungal Proteins / chemistry
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Fungal Proteins / genetics
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Membrane Proteins / analysis*
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Membrane Proteins / chemistry
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Membrane Proteins / genetics
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Microscopy, Immunoelectron
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Models, Biological
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Molecular Weight
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Nuclear Envelope / chemistry*
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Nuclear Envelope / genetics
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Nuclear Envelope / metabolism*
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Nuclear Envelope / ultrastructure
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Nuclear Proteins / analysis*
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Recombinant Fusion Proteins / analysis
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae / ultrastructure*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Substances
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Carrier Proteins
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Fungal Proteins
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Membrane Proteins
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Nuclear Proteins
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Recombinant Fusion Proteins