ArticleProceedings of the National Academy of Sciences of the United States of America2007
Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.
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Who cites it
118 citing papers in PubMed, 319 citations in OpenAlex.
- Desiccation tolerance as a driver of environmental persistence and transmission in nosocomial bacterial pathogens.Infection and immunity · 2026Review
- Screening of Xeroprotectants for Efficient Mammalian Cell Structural Preservation in Dry Conditions.ACS omega · 2026Article
- Haplotype-resolved telomere-to-telomere genome ofGenome research · 2026Article
- Overexpression of theInternational journal of molecular sciences · 2026Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Large protein databases reveal structural complementarity and functional locality.Nature communications · 2025Article
- Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic-abundant heat-soluble proteins during drying.Protein science : a publication of the Protein Society · 2025Article
- Insights into the diversity of CAHS protein function: Response to "Diversity in the protective role(s) of the conserved motif 1 from tardigrade cytoplasmic abundant heat soluble proteins during drying".Protein science : a publication of the Protein Society · 2025Article
- A bacterial expression cloning screen reveals single-stranded DNA-binding proteins as potent desicco-protectants.Cell reports · 2024Article
- Auxin and carbohydrate control flower bud development in Anthurium andraeanum during early stage of sexual reproduction.BMC plant biology · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Dynamic conformational changes of a tardigrade group-3 late embryogenesis abundant protein modulate membrane biophysical properties.PNAS nexus · 2024Article
- Liquid-Liquid Phase Separation and Protective Protein Aggregates in Bacteria.Molecules (Basel, Switzerland) · 2023Review
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Overexpression of OsHAD3, a Member of HAD Superfamily, Decreases Drought Tolerance of Rice.Rice (New York, N.Y.) · 2023Article
- The Moonlighting Function of Soybean Disordered Methyl-CpG-Binding Domain 10c Protein.International journal of molecular sciences · 2023Article
- Article
- In vivo expression vector derived from anhydrobiotic tardigrade genome enables live imaging in Eutardigrada.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Tardigrade small heat shock proteins can limit desiccation-induced protein aggregation.Communications biology · 2023Article
- Article
58 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The ability of certain plants, invertebrates, and microorganisms to survive almost complete loss of water has long been recognized, but the molecular mechanisms of this phenomenon remain to be defined. One phylogenetically widespread adaptation is the presence of abundant, highly hydrophilic proteins in desiccation-tolerant organisms. The best characterized of these polypeptides are the late embryogenesis abundant (LEA) proteins, first described in plant seeds >20 years ago but recently identified in invertebrates and bacteria. The function of these largely unstructured proteins has been unclear, but we now show that a group 3 LEA protein from the desiccation-tolerant nematode Aphelenchus avenae is able to prevent aggregation of a wide range of other proteins both in vitro and in vivo. The presence of water is essential for maintenance of the structure of many proteins, and therefore desiccation stress induces unfolding and aggregation. The nematode LEA protein is able to abrogate desiccation-induced aggregation of the water-soluble proteomes from nematodes and mammalian cells and affords protection during both dehydration and rehydration. Furthermore, when coexpressed in a human cell line, the LEA protein reduces the propensity of polyglutamine and polyalanine expansion proteins associated with neurodegenerative diseases to form aggregates, demonstrating in vivo function of an LEA protein as an antiaggregant. Finally, human cells expressing LEA protein exhibit increased survival of dehydration imposed by osmotic upshift, consistent with a broad protein stabilization function of LEA proteins under conditions of water stress.
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