ArticlePlant physiology2013
The importance of size and disorder in the cryoprotective effects of dehydrins.
Article in Plant physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- A novel natural variation in the promoter of TaDHN4D1 confers salt tolerance in wheat.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025Article
- Whole-Genome Identification of the Flax Fatty Acid Desaturase Gene Family and Functional Analysis of the LuFAD2.1 Gene Under Cold Stress Conditions.Plant, cell & environment · 2025Article
- Prokaryotic expression, purification, and the in vitro and in vivo protection study of dehydrin WDHN2 from Triticum aestivum.Protoplasma · 2024Article
- Novel Apoplastic Antifreeze Proteins ofBiomolecules · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Plant dehydrins and dehydrin-like proteins: characterization and participation in abiotic stress response.Frontiers in plant science · 2023Review
- Overexpression ofInternational journal of molecular sciences · 2022Article
- The Effect of Positive Charge Distribution on the Cryoprotective Activity of Dehydrins.Biomolecules · 2022Article
- Evaluation of a bacterial group 1 LEA protein as an enzyme protectant from stress-induced inactivation.Applied microbiology and biotechnology · 2022Article
- The Halophyte Dehydrin Sequence Landscape.Biomolecules · 2022Article
- The Disordered Dehydrin and Its Role in Plant Protection: A Biochemical Perspective.Biomolecules · 2022Review
- Comparative Genomics, Evolution, and Drought-Induced Expression of Dehydrin Genes in ModelPlants (Basel, Switzerland) · 2021Article
- Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers.Biomolecules · 2021Article
- Antifreeze protein from Ammopiptanthus nanus functions in temperature-stress through domain A.Scientific reports · 2021Article
- Article
- The in vitro structure and functions of the disordered late embryogenesis abundant three proteins.Protein science : a publication of the Protein Society · 2021Article
- Functional Characteristics Analysis of Dehydrins inInternational journal of molecular sciences · 2021Article
- Heterologous Expression of ThreePlants (Basel, Switzerland) · 2020Article
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8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dehydrins protect plant proteins and membranes from damage during drought and cold. Vitis riparia K2 is a 48-residue protein that can protect lactate dehydrogenase from freeze-thaw damage by preventing the aggregation and denaturation of the enzyme. To further elucidate its mechanism, we used a series of V. riparia K2 concatemers (K4, K6, K8, and K10) and natural dehydrins (V. riparia YSK2, 60 kilodalton peach dehydrin [PCA60], barley dehydrin5 [Dhn5], Thellungiella salsuginea dehydrin2 [TsDHN-2], and Opuntia streptacantha dehydrin1 [OpsDHN-1]) to test the effect of the number of K-segments and dehydrin size on their ability to protect lactate dehydrogenase from freeze-thaw damage. The results show that the larger the hydrodynamic radius of the dehydrin, the more effective the cryoprotection. A similar trend is observed with polyethylene glycol, which would suggest that the protection is simply a nonspecific volume exclusion effect that can be manifested by any protein. However, structured proteins of a similar range of sizes did not show the same pattern and level of cryoprotection. Our results suggest that with respect to enzyme protection, dehydrins function primarily as molecular shields and that their intrinsic disorder is required for them to be an effective cryoprotectant. Lastly, we show that the cryoprotection by a dehydrin is not due to any antifreeze protein-like activity, as has been reported previously.
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