Nature Cell Biology
6, 197 - 206 (2004)
Published online: 22 February 2004; | doi:10.1038/ncb1097
Minimal nuclear pore complexes define FG repeat domains essential for transportLisa A. Strawn1, Tianxiang Shen1, 3, Nataliya Shulga2, David S. Goldfarb2
& Susan R. Wente11
Department of Cell and Developmental Biology, Vanderbilt University Medical Center, 3120A MRBIII, 465 21st Avenue South, Nashville, TN 37232-8240 USA. 2
Department of Biology, University of Rochester, Rochester, NY 14627 USA. 3
Current address: Department of Pathology, Washington University School of Medicine, 660 S. Euclid, St. Louis, MO 63110, USA.
Correspondence should be addressed to Susan R. Wente susan.wente@vanderbilt.eduTranslocation through nuclear pore complexes (NPCs) requires interactions between receptor−cargo complexes and phenylalanine-glycine (FG) repeats in multiple FG domain-containing NPC proteins (FG-Nups). We have systematically deleted the FG domains of 11 Saccharomyces cerevisiae FG-Nups in various combinations. All five asymmetrically localized FG domains deleted together were non-essential. However, specific combinations of symmetrically localized FG domains were essential. Over half the total mass of FG domains could be deleted without loss of viability or the NPC's normal permeability barrier. Significantly, symmetric deletions caused mild reductions in Kap95−Kap60-mediated import rates, but virtually abolished Kap104 import. These results suggest the existence of multiple translocation pathways.
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