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© The Rockefeller University Press, 0021-9525/2000/2/635/ $5.00
The Journal of Cell Biology, Volume 148, Number 4, February 21, 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

Correspondence to: Michael P. Rout, Laboratory of Cellular and Structural Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021. Tel:(212) 327-8135 Fax:(212) 327-7193 E-mail: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


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