Structural characterization of nanoscale meshworks within a nucleoporin FG hydrogel

Biomacromolecules
Marcel PetriSimone Techert

Abstract

The permeability barrier of nuclear pore complexes (NPCs) controls all exchange of macromolecules between the cytoplasm and the cell nucleus. It consists of phenylalanine-glycine (FG) repeat domains apparently organized as an FG hydrogel. It has previously been demonstrated that an FG hydrogel derived from the yeast nucleoporin Nsp1p reproduces the selectivity of authentic NPCs. Here we combined time-resolved optical spectroscopy and X-ray scattering techniques to characterize such a gel. The data suggest a hierarchy of structures that form during gelation at the expense of unstructured elements. On the largest scale, protein-rich domains with a correlation length of ~16.5 nm are evident. On a smaller length scale, aqueous channels with an average diameter of ~3 nm have been found, which possibly represent the physical structures accounting for the passive sieving effect of nuclear pores. The protein-rich domains contain characteristic β-structures with typical inter-β-strand and inter-β-sheet distances of 1.3 and 0.47 nm, respectively. During gelation, the formation of oligomeric associates is accompanied by the transfer of phenylalanines into a hydrophobic microenvironment, supporting the view that this process is driven by a...Continue Reading

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Citations

Aug 21, 2014·International Journal of Molecular Sciences·Joseph M Kelich, Weidong Yang
Dec 27, 2015·Trends in Biochemical Sciences·H Broder Schmidt, Dirk Görlich
Dec 4, 2012·The EMBO Journal·Aksana A LabokhaDirk Görlich
May 6, 2015·Current Opinion in Cell Biology·Lian Zhu, Clifford P Brangwynne
Dec 15, 2012·EMBO Reports·Sigrid MillesEdward A Lemke
Feb 7, 2021·International Journal of Biological Macromolecules·Denzelle Lee LyngdohTimir Tripathi

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