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© The Rockefeller University Press, 0021-9525/2000//635 $5.00
The Journal of Cell Biology, Volume 148, Number 4, , 2000 635-652

Original Article

The Yeast Nuclear Pore Complex

: Composition, Architecture, and Transport Mechanism



Michael P. Routa, John D. Aitchisonb, Adisetyantari Supraptoa, Kelly Hjertaasb, Yingming Zhaoa, and Brian T. Chaita

a The Rockefeller University, New York, NY 10021
b Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021.(212) 327-7193(212) 327-8135

rout{at}rockvax.rockefeller.edu

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.

Key Words: nuclear pore complex • nucleoporins • nucleocytoplasmic transport • mass spectrometry • proteomics

© 2000 The Rockefeller University Press

Abbreviations used in this paper: MALDI-TOF, matrix-assisted laser desorption/ionization time of flight; NE, nuclear envelope; NPCs, nuclear pore complexes; nup, nucleoporin; ORF, open reading frame; pom, pore membrane proteins; PrA, protein A.


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