ArticleProtein science : a publication of the Protein Society2021
The in vitro structure and functions of the disordered late embryogenesis abundant three proteins.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 9 citations in OpenAlex.
- Evolutionary constraint on a core winter proteome across independently cold-adapted PACMAD grasses.PloS one · 2026Article
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Grass Rhizome Proteomics Reveals Convergent Freezing-Tolerance Strategies.bioRxiv : the preprint server for biology · 2025Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Artificial Proteins Designed from G3LEA Contribute to Enhancement of Oxidation Tolerance inAntioxidants (Basel, Switzerland) · 2023Article
- The in vitro structure and functions of the disordered late embryogenesis abundant three proteins.Protein science : a publication of the Protein Society · 2021Article
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2 authors at 1 institution in 1 country.
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Abstract
Late embryogenesis abundant (LEA) proteins are produced during seed embryogenesis and in vegetative tissue in response to various abiotic stressors. A correlation has been established between LEA expression and stress tolerance, yet their precise biochemical mechanism remains elusive. LEA proteins are very rich in hydrophilic amino acids, and they have been found to be intrinsically disordered proteins (IDPs) in vitro. Here, we perform biochemical and structural analyses of the four LEA3 proteins from Arabidopsis thaliana (AtLEA3). We show that the LEA3 proteins are disordered in solution but have regions with propensity for order. All LEA3 proteins were effective cryoprotectants of LDH in the freeze/thaw assays, while only one member, AtLEA3-4, was shown to bind Cu
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