The Yeast Nuclear Pore Complex: Composition, Architecture, and Transport Mechanism

doi:10.1083/jcb.148.4.635

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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. Rout^a, John D. Aitchison^b, Adisetyantari Suprapto^a, Kelly Hjertaas^b, Yingming Zhao^a, and Brian T. Chait^a

^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) mediatesnucleocytoplasmic exchange requires a comprehensive inventoryof the molecular components of the NPC and a knowledge of howeach component contributes to the overall structure of thislarge molecular translocation machine. Therefore, we have takena comprehensive approach to classify all components of the yeastNPC (nucleoporins). This involved identifying all the proteinspresent in a highly enriched NPC fraction, determining whichof these proteins were nucleoporins, and localizing each nucleoporinwithin the NPC. Using these data, we present a map of the moleculararchitecture of the yeast NPC and provide evidence for a Brownianaffinity gating mechanism for nucleocytoplasmic transport.

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

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

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