Journal
CELL
Volume 174, Issue 1, Pages 202-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2018.05.045
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Funding
- Max-Planck-Gesellschaft
- Deutsche Forschungsgemeinschaft [SFB1190]
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Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-p interactions between arginines and FG-phenylalanines may explain this apparent paradox. Application of these principles to redesign the surface of GFP resulted in variants that show a wide span of transit rates, ranging from 35-fold slower than wild-type to similar to 500 times faster, with the latter outpacing even naturally occurring nuclear transport receptors (NTRs). The structure of a fast and particularly FG-specific GFP NTR variant illustrates how NTRs can expose multiple regions for binding hydrophobic FG motifs while evading nonspecific aggregation. Finally, we document that even for NTR-mediated transport, the surface-properties of the passively carried'' cargo can strikingly affect the translocation rate.
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