Abstract
Translocation 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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Active Transport, Cell Nucleus / genetics*
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Cell Membrane Permeability / genetics
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Cell Survival / genetics
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Cells, Cultured
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Gene Deletion
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Karyopherins / genetics
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Karyopherins / metabolism
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Mutation / genetics
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Nuclear Pore / genetics
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Nuclear Pore / metabolism*
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Nuclear Pore Complex Proteins / deficiency*
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Nuclear Pore Complex Proteins / genetics
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Protein Structure, Tertiary / genetics
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Protein Transport / genetics*
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Repetitive Sequences, Amino Acid / physiology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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beta Karyopherins / genetics
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beta Karyopherins / metabolism
Substances
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KAP104 protein, S cerevisiae
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Karyopherins
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Nuclear Pore Complex Proteins
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Saccharomyces cerevisiae Proteins
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beta Karyopherins