Intrinsically disordered nuclear pore proteins show ideal-polymer morphologies and dynamics
- 27 February 2020
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review E
- Vol. 101 (2), 022420
- https://doi.org/10.1103/PhysRevE.101.022420
Abstract
In the nuclear pore complex, intrinsically disordered nuclear pore proteins (FG Nups) form a selective barrier for transport into and out of the cell nucleus, in a way that remains poorly understood. The collective FG Nup behavior has long been conceptualized either as a polymer brush, dominated by entropic and excluded-volume (repulsive) interactions, or as a hydrogel, dominated by cohesive (attractive) interactions between FG Nups. Here we compare mesoscale computational simulations with a wide range of experimental data to demonstrate that FG Nups are at the crossover point between these two regimes. Specifically, we find that repulsive and attractive interactions are balanced, resulting in morphologies and dynamics that are close to those of ideal polymer chains. We demonstrate that this property of FG Nups yields sufficient cohesion to seal the transport barrier, and yet maintains fast dynamics at the molecular scale, permitting the rapid polymer rearrangements needed for transport events.Funding Information
- Engineering and Physical Sciences Research Council (EP/L504889/1)
- Royal Society
This publication has 50 references indexed in Scilit:
- Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complexProceedings of the National Academy of Sciences of the United States of America, 2013
- Systematic analysis of barrier-forming FG hydrogels from Xenopus nuclear pore complexesThe EMBO Journal, 2012
- Nuclear transport receptor binding avidity triggers a self-healing collapse transition in FG-nucleoporin molecular brushesProceedings of the National Academy of Sciences of the United States of America, 2012
- Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopyProceedings of the National Academy of Sciences of the United States of America, 2012
- The Permeability of Reconstituted Nuclear Pores Provides Direct Evidence for the Selective Phase ModelCell, 2012
- Determining equilibrium constants for dimerization reactions from molecular dynamics simulationsJournal of Computational Chemistry, 2011
- A Bimodal Distribution of Two Distinct Categories of Intrinsically Disordered Structures with Separate Functions in FG NucleoporinsMolecular & Cellular Proteomics, 2010
- Fundamental measure theory for hard-sphere mixtures: a reviewJournal of Physics: Condensed Matter, 2010
- Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transportProceedings of the National Academy of Sciences of the United States of America, 2006
- Molecular Dynamics Simulations of the Ala-Pro Dipeptide in Water: Conformational Dynamics of Trans and Cis Isomers Using Different Water ModelsThe Journal of Physical Chemistry B, 2001