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  • Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex.

Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex.

Cell (2017-10-17)
Evgeny Onischenko, Jeffrey H Tang, Kasper R Andersen, Kevin E Knockenhauer, Pascal Vallotton, Carina P Derrer, Annemarie Kralt, Christopher F Mugler, Leon Y Chan, Thomas U Schwartz, Karsten Weis
초록

Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 nucleoporins (Nups). One-third of these Nups contain phenylalanine-glycine (FG)-rich repeats, forming a diffusion barrier, which is selectively permeable for nuclear transport receptors that interact with these repeats. Here, we identify an additional function of FG repeats in the structure and biogenesis of the yeast NPC. We demonstrate that GLFG-containing FG repeats directly bind to multiple scaffold Nups in vitro and act as NPC-targeting determinants in vivo. Furthermore, we show that the GLFG repeats of Nup116 function in a redundant manner with Nup188, a nonessential scaffold Nup, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly. Our results reveal a previously unanticipated structural role for natively unfolded GLFG repeats as Velcro to link NPC subcomplexes and thus add a new layer of connections to current models of the NPC architecture.

MATERIALS
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제품 설명

Sigma-Aldrich
Lectin from Triticum vulgaris (wheat), lyophilized powder
Sigma-Aldrich
Protease Inhibitor Cocktail, for use with fungal and yeast extracts, DMSO solution
Sigma-Aldrich
Ribonuclease S from bovine pancreas, Grade XII-S
Sigma-Aldrich
IgG from rabbit serum, reagent grade, ≥95% (SDS-PAGE), essentially salt-free, lyophilized powder