This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.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. This work has been published (M.P. Rout, J.D. Aitchison, A. Suprapto, K. Hjertaas, Y-M. Zhao, B.T. Chait, J. Cell. Biol. 148 (2000) 635-651)and M.P. Rout, J.D. Aitchison, M.O. Magnasco, B.T. Chait, Trends Cell Biology 13(2003)622-628. We are currently testing our model for nuclear transport.
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