The plant dehydrin Lti30 stabilizes lipid lamellar structures in varying hydration conditions

• DOI: 10.1194/jlr.ra120000624
• Publication Date: 2020-05-13T17:46:59Z
• Authors: Jenny Marie Ander...; Quoc Dat Pham; Helena Mateos; Sylvia Eriksson; Pia Harryson; Emma Sparr
• Keywords: 0301 basic medicine; trimethylamine N-oxide; osmolytes; Cell Membrane; Lipid Bilayers; Arabidopsis; Water; self-assembly; urea; QD415-436; Lipid Metabolism; Biochemistry; 6. Clean water; desiccation; 03 medical and health sciences; protein; Research Articles; Plant Proteins

A major challenge to plant growth and survival are changes in temperature diminishing water supply. During acute stress, plants often express stress proteins, such as dehydrins, which intrinsically disordered hydrophilic proteins. In this article, we investigated how the dehydrin Lti30 from Arabidopsis thaliana stabilizes membrane systems that exposed large hydration. We also compared effects of on membranes with those simple osmolytes urea trimethylamine N-oxide. Using X-ray diffraction solid-state NMR, studied lipid-protein self-assembly at varying hydration levels. made following observations: 1) association anionic relies electrostatic attraction, protein is located bilayer interfacial region; 2) can stabilize lamellar multilayer structure, making it insensitive variations content; 3) lipid a composition similar present some seeds plants, prevent formation nonlamellar phases upon drying, may be crucial for maintaining integrity; 4) structures both high low contents, whereas small osmolyte molecules mainly dehydration-induced transitions. These results corroborate idea dehydrins part sensitive multifaceted regulatory mechanism protects cells against stress.