This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A full understanding of the mechanism of nuclear transport requires a detailed knowledge of the NPC ultrastructure and a precise relative positioning of all NUPs, and an investigation of the interaction between the NPC and soluble transport factors. The approach of this project is to identify interactions of each single nucleoporin (NUP) with other NUPs or with transportfactors by isolating and analyzing their subcomplexes. We isolate the subcomplexes of NPC components by affinity purification of affinity-tagged versions of all known NUP's (ca. 30), and identify their composition by mass spectrometry combined with protein sequence database searching. These data, together with the known localization of each single NUP within the NPC structure, have been used to solve the molecular architecture of the yeast NPC. A paper describing these results is in preparation.
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