ArticleCell stress & chaperones2019
Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana.
Article in Cell stress & chaperones, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Surviving desiccation: key factors underlying tolerance in prokaryotes and eukaryotes.Protoplasma · 2025Review
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Co-opted and canonical glycerol channels play a major role during anhydrobiosis of an extremophile crustacean.BMC biology · 2025Article
- LEA_4 motifs function alone and in conjunction with synergistic cosolutes to protect a labile enzyme during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Crowding in Anhydrobiosis.Sub-cellular biochemistry · 2025Review
- The genome of the extremophile Artemia provides insight into strategies to cope with extreme environments.BMC genomics · 2021Article
- Article
- Liquid-liquid phase separation promotes animal desiccation tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- What Do We Know About the Genetic Basis of Seed Desiccation Tolerance and Longevity?International journal of molecular sciences · 2020Review
- Mechanisms of Desiccation Tolerance: Themes and Variations in Brine Shrimp, Roundworms, and Tardigrades.Frontiers in physiology · 2020Review
- New insights into anhydrobiosis using cellular dielectrophoresis-based characterization.Biomicrofluidics · 2019Article
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5 authors.
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Abstract
Late embryogenesis abundant (LEA) proteins are intrinsically disordered proteins (IDPs) commonly found in anhydrobiotic organisms and are frequently correlated with desiccation tolerance. Herein we report new findings on AfrLEA6, a novel group 6 LEA protein from embryos of Artemia franciscana. Assessment of secondary structure in aqueous and dried states with circular dichroism (CD) reveals 89% random coil in the aqueous state, thus supporting classification of AfrLEA6 as an IDP. Removal of water from the protein by drying or exposure to trifluoroethanol (a chemical de-solvating agent) promotes a large gain in secondary structure of AfrLEA6, predominated by α-helix and exhibiting minimal β-sheet structure. We evaluated the impact of physiological concentrations (up to 400 mM) of the disaccharide trehalose on the folding of LEA proteins in solution. CD spectra for AfrLEA2, AfrLEA3m, and AfrLEA6 are unaffected by this organic solute noted for its ability to drive protein folding. AfrLEA6 exhibits its highest concentration in vivo during embryonic diapause, drops acutely at diapause termination, and then declines during development to undetectable values at the larval stage. Maximum cellular titer of AfrLEA6 was 10-fold lower than for AfrLEA2 or AfrLEA3, both group 3 LEA proteins. Acute termination of diapause with H
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