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FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties
Steffen Frey,1,2Ralf P. Richter,3,4Dirk Görlich1,2*
Nuclear pore complexes permit rapid passage of cargoes boundto nuclear transport receptors, but otherwise suppress nucleocytoplasmicfluxes of inert macromolecules 30 kilodaltons. To explain thisselectivity, a sieve structure of the permeability barrier hasbeen proposed that is created through reversible cross-linkingbetween Phe and Gly (FG)rich nucleoporin repeats. Accordingto this model, nuclear transport receptors overcome the sizelimit of the sieve and catalyze their own nuclear pore-passageby a competitive disruption of adjacent inter-repeat contacts,which transiently opens adjoining meshes. Here, we found thatphenylalanine-mediated inter-repeat interactions indeed cross-linkFG-repeat domains into elastic and reversible hydrogels. Furthermore,we obtained evidence that such hydrogel formation is requiredfor viability in yeast.
1 Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany. 2 Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany. 3 Institut für Physikalische Chemie, Universität Heidelberg, INF253, D-69120 Heidelberg, Germany. 4 Max-Planck-Institut für Metallforschung, Heisenbergstrasse 3, D-70569 Stuttgart, Germany.
* To whom correspondence should be addressed. E-mail: dg{at}zmbh.uni-heidelberg.de
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