RRC ID 64560
Author Shou K, Bremer A, Rindfleisch T, Knox-Brown P, Hirai M, Rekas A, Garvey CJ, Hincha DK, Stadler AM, Thalhammer A.
Title Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity - an X-ray and light scattering study.
Journal Phys Chem Chem Phys
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.
Volume 21(34)
Pages 18727-18740
Published 2019-8-28
DOI 10.1039/c9cp01768b
PMID 31424463
IF 3.567
Resource
Arabidopsis / Cultured plant cells, genes pda06312