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Folding and Lipid Composition Determine Membrane Interaction of the Disordered Protein COR15A

  • Plants from temperate climates, such as the model plant Arabidopsis thaliana, are challenged with seasonal low temperatures that lead to increased freezing tolerance in fall in a process termed cold acclimation. Among other adaptations, this involves the accumulation of cold-regulated (COR) proteins, such as the intrinsically disordered chloroplast-localized protein COR15A. Together with its close homolog COR15B, it stabilizes chloroplast membranes during freezing. COR15A folds into amphipathic alpha-helices in the presence of high concentrations of low-molecular-mass crowders or upon dehydration. Under these conditions, the (partially) folded protein binds peripherally to membranes. In our study, we have used coarse-grained molecular dynamics simulations to elucidate the details of COR15A-membrane binding and its effects on membrane structure and dynamics. Simulation results indicate that at least partial folding of COR15A and the presence of highly unsaturated galactolipids in the membranes are necessary for efficient membranePlants from temperate climates, such as the model plant Arabidopsis thaliana, are challenged with seasonal low temperatures that lead to increased freezing tolerance in fall in a process termed cold acclimation. Among other adaptations, this involves the accumulation of cold-regulated (COR) proteins, such as the intrinsically disordered chloroplast-localized protein COR15A. Together with its close homolog COR15B, it stabilizes chloroplast membranes during freezing. COR15A folds into amphipathic alpha-helices in the presence of high concentrations of low-molecular-mass crowders or upon dehydration. Under these conditions, the (partially) folded protein binds peripherally to membranes. In our study, we have used coarse-grained molecular dynamics simulations to elucidate the details of COR15A-membrane binding and its effects on membrane structure and dynamics. Simulation results indicate that at least partial folding of COR15A and the presence of highly unsaturated galactolipids in the membranes are necessary for efficient membrane binding. The bound protein is stabilized on the membrane by interactions of charged and polar amino acids with galactolipid headgroups and by interactions of hydrophobic amino acids with the upper part of the fatty acyl chains. Experimentally, the presence of liposomes made from a mixture of lipids mimicking chloroplast membranes induces additional folding in COR15A under conditions of partial dehydration, in agreement with the simulation results.show moreshow less

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Author details:Carlos Navarro-RetamalORCiD, Anne BremerGND, Helgi I. Ingolfsson, Jans Alzate-Morales, Julio CaballeroORCiD, Anja ThalhammerORCiDGND, Wendy GonzalezORCiD, Dirk K. HinchaORCiDGND
DOI:https://doi.org/10.1016/j.bpj.2018.08.014
ISSN:0006-3495
ISSN:1542-0086
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/30195939
Title of parent work (English):Biophysical journal
Publisher:Cell Press
Place of publishing:Cambridge
Publication type:Article
Language:English
Year of first publication:2018
Publication year:2018
Release date:2021/09/27
Volume:115
Issue:6
Number of pages:13
First page:968
Last Page:980
Funding institution:Chilean National Commission for Scientific and Technological Research [REDES 120019]; Max-Planck SocietyMax Planck Society; University of Potsdam; Government of Chile (Fondecyt) through the Chilean National Commission for Scientific and Technological Research [3170434]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
DDC classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Peer review:Referiert
Publishing method:Open Access / Bronze Open-Access
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