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Published 22 November 2004. doi:10.1083/jcb.200407156
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 167, Number 4, 583-590
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 The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo

Bryan Zeitler and Karsten Weis

Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720

Correspondence to Karsten Weis: kweis{at}berkeley.edu


Abstract
Nucleocytoplasmic transport occurs through gigantic proteinaceous channels called nuclear pore complexes (NPCs). Translocation through the NPC is exquisitely selective and is mediated by interactions between soluble transport carriers and insoluble NPC proteins that contain phenylalanine-glycine (FG) repeats. Although most FG nucleoporins (Nups) are organized symmetrically about the planar axis of the nuclear envelope, very few localize exclusively to one side of the NPC. We constructed Saccharomyces cerevisiae mutants with asymmetric FG repeats either deleted or swapped to generate NPCs with inverted FG asymmetry. The mutant Nups localize properly within the NPC and exhibit exchanged binding specificity for the export factor Xpo1. Surprisingly, we were unable to detect any defects in the Kap95, Kap121, Xpo1, or mRNA transport pathways in cells expressing the mutant FG Nups. These findings suggest that the biased distribution of FG repeats is not required for major nucleocytoplasmic trafficking events across the NPC.

Abbreviations used in this paper: cNLS, classical NLS; EB, extraction buffer; FG, phenylalanine-glycine; NES, nuclear export signal; NPC, nuclear pore complex; Nup, nucleoporin; RFP, red fluorescent protein.


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