ArticleBiophysical journal2017
Intrinsically Disordered Stress Protein COR15A Resides at the Membrane Surface during Dehydration.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- GhCOR27 confers Verticillium wilt resistance in cotton by relieving the GhASIL1-GhERF114-mediated repression of lignin accumulation.Plant physiology · 2026Article
- Graph statistics theory of individualized quantitative genetics under haplotype-resolved genome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- When Warm Breaks Cold: Understanding Deacclimations and Reacclimations Cycles as a Key to Winter Crop Resilience.International journal of molecular sciences · 2025Review
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Role ofInternational journal of molecular sciences · 2025Article
- Analysis of physiological characteristics and gene co-expression networks inFrontiers in plant science · 2025Article
- Article
- Review
- Molecular Mechanisms Underlying Freezing Tolerance in Plants: Implications for Cryopreservation.International journal of molecular sciences · 2024Review
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Identification and expression analysis of LEA gene family members in pepper (Capsicum annuum L.).FEBS open bio · 2023Article
- Transcription FactorPlants (Basel, Switzerland) · 2023Article
- Genetic Mechanisms of Cold Signaling in Wheat (Life (Basel, Switzerland) · 2022Review
- The network centered on ICEs play roles in plant cold tolerance, growth and development.Planta · 2022Review
- ICE-CBF-COR Signaling Cascade and Its Regulation in Plants Responding to Cold Stress.International journal of molecular sciences · 2022Review
- Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status.Frontiers in plant science · 2022Article
- Transcriptomic profiling of wheat stem during meiosis in response to freezing stress.Frontiers in plant science · 2022Article
- Enhancement of plant cold tolerance by soybean RCC1 family gene GmTCF1a.BMC plant biology · 2021Article
- Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins fromBiomolecules · 2021Article
- Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plants from temperate climate zones are able to increase their freezing tolerance during exposure to low, above-zero temperatures in a process termed cold acclimation. During this process, several cold-regulated (COR) proteins are accumulated in the cells. One of them is COR15A, a small, intrinsically disordered protein that contributes to leaf freezing tolerance by stabilizing cellular membranes. The isolated protein folds into amphipathic α-helices in response to increased crowding conditions, such as high concentrations of glycerol. Although there is evidence for direct COR15A-membrane interactions, the orientation and depth of protein insertion were unknown. In addition, although folding due to high osmolyte concentrations had been established, the folding response of the protein under conditions of gradual dehydration had not been investigated. Here we show, using Fourier transform infrared spectroscopy, that COR15A starts to fold into α-helices already under mild dehydration conditions (97% relative humidity (RH), corresponding to freezing at -3°C) and that folding gradually increases with decreasing RH. Neutron diffraction experiments at 97 and 75% RH established that the presence of COR15A had no significant influence on the structure of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membranes. However, using deuterated POPC we could clearly establish that COR15A interacts with the membranes and penetrates below the headgroup region into the upper part of the fatty acyl chain region. This localization is in agreement with our hypothesis that COR15A-membrane interaction is at least, in part, driven by a hydrophobic interaction between the lipids and the hydrophobic face of the amphipathic protein α-helix.
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