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

  • The plant stress protein COR15A stabilizes chloroplast membranes during freezing. COR15A is an intrinsically disordered protein (IDP) in aqueous solution, but acquires an alpha-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 importanceThe plant stress protein COR15A stabilizes chloroplast membranes during freezing. COR15A is an intrinsically disordered protein (IDP) in aqueous solution, but acquires an alpha-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.zeige mehrzeige weniger

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Metadaten
Verfasserangaben:Keyun Shou, Anne BremerGND, Tobias RindfleischORCiD, Patrick Knox-BrownORCiD, Mitsuhiro HiraiORCiD, Agata Rekas, Christopher J. GarveyORCiD, Dirk K. HinchaORCiDGND, Andreas M. Stadler, Anja ThalhammerORCiDGND
DOI:https://doi.org/10.1039/c9cp01768b
ISSN:1463-9076
ISSN:1463-9084
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/31424463
Titel des übergeordneten Werks (Englisch):Physical chemistry, chemical physics : a journal of European Chemical Societies
Verlag:Royal Society of Chemistry
Verlagsort:Cambridge
Publikationstyp:Wissenschaftlicher Artikel
Sprache:Englisch
Datum der Erstveröffentlichung:09.07.2019
Erscheinungsjahr:2019
Datum der Freischaltung:09.11.2020
Band:21
Ausgabe:34
Seitenanzahl:14
Erste Seite:18727
Letzte Seite:18740
Fördernde Institution:Program Advisory Committee of the Japan Synchrotron Radiation Research Institute [2016B1039]; University of Potsdam
Organisationseinheiten:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie
DDC-Klassifikation:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
Peer Review:Referiert
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