ArticleThe Biochemical journal2005
LEA proteins prevent protein aggregation due to water stress.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 260 papers.
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Who cites it
260 citing papers in PubMed, 795 citations in OpenAlex.
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- Salt-Drought Co-Stress Impairs Root Ultrastructure, Remodels Rhizosphere Bacteria, and Suppresses Peanut (Plants (Basel, Switzerland) · 2026Article
- Hyperactive ice-binding proteins stabilize cell membranes and improve resistance to dehydration stress in Caenorhabditis elegans.FEBS open bio · 2026Article
- Anhydrobiosis as a Model of Aging and Longevity: The Role of Autophagy and Metabolism in Yeast Cells.Microbial ecology · 2026Review
- Osmotic signaling governs sunscreen biosynthesis to safeguard desert cyanobacteria against desiccation.mLife · 2026Article
- An integrative defense mechanism mediated by GhBsr-d1L7 and GhERD10 confers resistance to Verticillium dahliae in cotton.BMC biology · 2026Article
- Overexpression of theInternational journal of molecular sciences · 2026Article
- Engineering a thermostable recombinantFrontiers in plant science · 2026Article
- Molecular propensity and stress tolerance of dehydrins from desert plants.Scientific reports · 2025Article
- Genome-wide identification, structural characterization and gene expression analysis of the LEA_2 gene family in faba bean (Vicia Faba L.).BMC plant biology · 2025Article
- Surviving desiccation: key factors underlying tolerance in prokaryotes and eukaryotes.Protoplasma · 2025Review
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Recovery Dynamics of Photosynthetic Performance and Antioxidant Defense in Resurrection PlantsPlants (Basel, Switzerland) · 2025Article
- A Group 6 LEA Protein Plays Key Roles in Tolerance to Water Deficit, and in Maintaining the Glassy State and Longevity of Seeds.Plant, cell & environment · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- How drought and ploidy level shape gene expression and DNA methylation in Phragmites australis.Plant cell reports · 2025Article
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- A complex interplay of genetic introgression and local adaptation during the evolutionary history of three closely related spruce species.Plant diversity · 2025Article
200 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LEA (late embryogenesis abundant) proteins in both plants and animals are associated with tolerance to water stress resulting from desiccation and cold shock. However, although various functions of LEA proteins have been proposed, their precise role has not been defined. Recent bioinformatics studies suggest that LEA proteins might behave as molecular chaperones, and the current study was undertaken to test this hypothesis. Recombinant forms of AavLEA1, a group 3 LEA protein from the anhydrobiotic nematode Aphelenchus avenae, and Em, a group 1 LEA protein from wheat, have been subjected to functional analysis. Heat-stress experiments with citrate synthase, which is susceptible to aggregation at high temperatures, suggest that LEA proteins do not behave as classical molecular chaperones, but they do exhibit a protective, synergistic effect in the presence of the so-called chemical chaperone, trehalose. In contrast, both LEA proteins can independently protect citrate synthase from aggregation due to desiccation and freezing, in keeping with a role in water-stress tolerance; similar results were obtained with lactate dehydrogenase. This is the first evidence of anti-aggregation activity of LEA proteins due to water stress. Again, a synergistic effect of LEA and trehalose was observed, which is significant given that non-reducing disaccharides are known to accumulate during dehydration in plants and nematodes. A model is proposed whereby LEA proteins might act as a novel form of molecular chaperone, or 'molecular shield', to help prevent the formation of damaging protein aggregates during water stress.
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