Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana
- The LEA (late embryogenesis abundant) proteins COR15A and COR15B from Arabidopsis thaliana are intrinsically disordered under fully hydrated conditions, but obtain alpha-helical structure during dehydration, which is reversible upon rehydration. To understand this unusual structural transition, both proteins were investigated by circular dichroism (CD) and molecular dynamics (MD) approaches. MD simulations showed unfolding of the proteins in water, in agreement with CD data obtained with both HIS-tagged and untagged recombinant proteins. Mainly intramolecular hydrogen bonds (H-bonds) formed by the protein backbone were replaced by H-bonds with water molecules. As COR15 proteins function in vivo as protectants in leaves partially dehydrated by freezing, unfolding was further assessed under crowded conditions. Glycerol reduced (40%) or prevented (100%) unfolding during MD simulations, in agreement with CD spectroscopy results. H-bonding analysis indicated that preferential exclusion of glycerol from the protein backbone increasedThe LEA (late embryogenesis abundant) proteins COR15A and COR15B from Arabidopsis thaliana are intrinsically disordered under fully hydrated conditions, but obtain alpha-helical structure during dehydration, which is reversible upon rehydration. To understand this unusual structural transition, both proteins were investigated by circular dichroism (CD) and molecular dynamics (MD) approaches. MD simulations showed unfolding of the proteins in water, in agreement with CD data obtained with both HIS-tagged and untagged recombinant proteins. Mainly intramolecular hydrogen bonds (H-bonds) formed by the protein backbone were replaced by H-bonds with water molecules. As COR15 proteins function in vivo as protectants in leaves partially dehydrated by freezing, unfolding was further assessed under crowded conditions. Glycerol reduced (40%) or prevented (100%) unfolding during MD simulations, in agreement with CD spectroscopy results. H-bonding analysis indicated that preferential exclusion of glycerol from the protein backbone increased stability of the folded state.…
| Author details: | Carlos Navarro-RetamalORCiD, Anne BremerGND, Jans H. Alzate-Morales, Julio CaballeroORCiD, Dirk K. HinchaORCiDGND, Wendy GonzalezORCiD, Anja ThalhammerORCiDGND |
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| DOI: | https://doi.org/10.1039/c6cp02272c |
| ISSN: | 1463-9076 |
| ISSN: | 1463-9084 |
| Pubmed ID: | https://pubmed.ncbi.nlm.nih.gov/27255148 |
| Title of parent work (English): | Physical chemistry, chemical physics : a journal of European Chemical Societies |
| Publisher: | Royal Society of Chemistry |
| Place of publishing: | Cambridge |
| Publication type: | Article |
| Language: | English |
| Year of first publication: | 2016 |
| Publication year: | 2016 |
| Release date: | 2020/03/22 |
| Volume: | 18 |
| Number of pages: | 11 |
| First page: | 25806 |
| Last Page: | 25816 |
| Funding institution: | Chilean National Commission for Scientific and Technological Research (CONICYT) [REDES 120019]; Fondecyt [1140624]; Max-Planck Society; University of Potsdam; Government of Chile through CONICYT |
| Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
| Peer review: | Referiert |
