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Issue 12, 2014
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Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering

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Abstract

The assembly kinetics of intermediate filament (IF) proteins from tetrameric complexes to single filaments and networks depends on the protein concentration, temperature and the ionic composition of their environment. We systematically investigate how changes in the concentration of monovalent potassium and divalent magnesium ions affect the internal organization of the resulting filaments. Small angle X-ray scattering (SAXS) is very sensitive to changes in the filament cross-section such as diameter or compactness. Our measurements reveal that filaments formed in the presence of magnesium chloride differ distinctly from filaments formed in the presence of potassium chloride. The principle multi-step assembly mechanism from tetramers via unit-length filaments (ULF) to elongated filaments is not changed by the valency of ions. However, the observed differences indicate that the magnesium ions free the head domains of tetramers from unproductive interactions to allow assembly but at the same time mediate strong inter-tetrameric interactions that impede longitudinal annealing of unit-length filaments considerably, thus slowing down filament growth.

Graphical abstract: Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering

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Supplementary files

Article information


Submitted
27 Sep 2013
Accepted
09 Dec 2013
First published
08 Jan 2014

Soft Matter, 2014,10, 2059-2068
Article type
Paper

Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering

M. E. Brennich, S. Bauch, U. Vainio, T. Wedig, H. Herrmann and S. Köster, Soft Matter, 2014, 10, 2059
DOI: 10.1039/C3SM52532E

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