251. The yeast nuclear pore complex: composition, architecture, and transport mechanism.
- Author
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Rout MP, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, and Chait BT
- Subjects
- Biological Transport, Carrier Proteins analysis, Carrier Proteins chemistry, Carrier Proteins genetics, Chromatography, High Pressure Liquid, Fluorescent Antibody Technique, Fungal Proteins chemistry, Fungal Proteins genetics, Membrane Proteins chemistry, Membrane Proteins genetics, Microscopy, Immunoelectron, Models, Biological, Molecular Weight, Nuclear Envelope genetics, Nuclear Envelope ultrastructure, Nuclear Proteins chemistry, Nuclear Proteins genetics, Recombinant Fusion Proteins analysis, Recombinant Fusion Proteins chemistry, Recombinant Fusion Proteins genetics, Saccharomyces cerevisiae chemistry, Saccharomyces cerevisiae metabolism, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Fungal Proteins analysis, Membrane Proteins analysis, Nuclear Envelope chemistry, Nuclear Envelope metabolism, Nuclear Proteins analysis, Saccharomyces cerevisiae ultrastructure
- 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.
- Published
- 2000
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