Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity - an X-ray and light scattering study.

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ID: 13054
2019
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Ranked #46 of 184 articles by views in Physical chemistry chemical physics : PCCP

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Abstract
The plant stress protein COR15A stabilizes chloroplast membranes during freezing. COR15A is an intrinsically disordered protein (IDP) in aqueous solution, but acquires an α-helical structure during dehydration or the increase of solution osmolarity. We have used small- and wide-angle X-ray scattering (SAXS/WAXS) combined with static and dynamic light scattering (SLS/DLS) to investigate the structural and hydrodynamic properties of COR15A in response to increasing solution osmolarity. Coarse-grained ensemble modelling allowed a structure-based interpretation of the SAXS data. Our results demonstrate that COR15A behaves as a biomacromolecule with polymer-like properties which strongly depend on solution osmolarity. Biomacromolecular self-assembly occurring at high solvent osmolarity is initiated by the occurrence of two specific structural subpopulations of the COR15A monomer. The osmolarity dependent structural selection mechanism is an elegant way for conformational regulation and assembly of COR15A. It highlights the importance of the polymer-like properties of IDPs for their associated biological function.
Reference Key
shou2019conformationalphysical Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Shou, Keyun;Bremer, Anne;Rindfleisch, Tobias;Knox-Brown, Patrick;Hirai, Mitsuhiro;Rekas, Agata;Garvey, Christopher J;Hincha, Dirk K;Stadler, Andreas M;Thalhammer, Anja;
Journal Physical chemistry chemical physics : PCCP
Year 2019
DOI
10.1039/c9cp01768b
URL
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