ArticleScientific reports2019
Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Deciphering the PgLEA2-50 interactome: implications for abiotic stress responses inPlant signaling & behavior · 2026Article
- Evolutionary constraint on a core winter proteome across independently cold-adapted PACMAD grasses.PloS one · 2026Article
- Molecular propensity and stress tolerance of dehydrins from desert plants.Scientific reports · 2025Article
- Grass Rhizome Proteomics Reveals Convergent Freezing-Tolerance Strategies.bioRxiv : the preprint server for biology · 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
- 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
- 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
- Molecular Mechanisms Underlying Freezing Tolerance in Plants: Implications for Cryopreservation.International journal of molecular sciences · 2024Review
- Structural adaptability and surface activity of peptides derived from tardigrade proteins.Protein science : a publication of the Protein Society · 2024Article
- Genome-wide characterization of LEA gene family reveals a positive role of BnaA.LEA6.a in freezing tolerance in rapeseed (Brassica napus L.).BMC plant biology · 2024Article
- Article
- Protective roles of highly conserved motif 1 in tardigrade cytosolic-abundant heat soluble protein in extreme environments.Protein science : a publication of the Protein Society · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
- Genetic diversity of durum wheat (Triticum turgidum ssp. durum) to mitigate abiotic stress: Drought, heat, and their combination.PloS one · 2024Article
- Study of the genetic variability of durum wheat (AoB PLANTS · 2024Article
- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- Enzyme stabilization and thermotolerance function of the intrinsically disordered LEA2 proteins from date palm.Scientific reports · 2023Article
- The tardigrade protein CAHS D interacts with, but does not retain, water in hydrated and desiccated systems.Scientific reports · 2023Article
- Anaerobic demethylation of guaiacyl-derived monolignols enabled by a designed artificial cobalamin methyltransferase fusion enzyme.RSC advances · 2023Article
- Stress-dependent cell stiffening by tardigrade tolerance proteins that reversibly form a filamentous network and gel.PLoS biology · 2022Article
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4 authors.
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Abstract
Late Embryogenesis Abundant (LEA) proteins are mostly predicted to be intrinsically disordered proteins (IDPs) that are induced under conditions of cellular dehydration. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been investigated in a small number of proteins. Here, we have characterized the wheat LEA protein TdLEA3, which has sequence homology with the group of LEA_4 proteins that are characterized by the 11-mer repeat motif TAQAAKEKAXE. TdLEA3 has five repeats of this imperfectly conserved 11-mer amino acid motif. To investigate the structure of the protein, we used circular dichroism (CD) and Fourier-transform infrared (FTIR) spectroscopy. The data show that TdLEA3 was largely disordered under fully hydrated conditions and acquired α-helical structure upon drying and in the presence of trifluoroethanol (TFE). Moreover, the addition of increasing glycerol concentrations to the protein solution induced a progressive gain in α-helix content. Activity assays indicated that TdLEA3 was able to prevent the inactivation of lactate dehydrogenase (LDH) under heat, dehydration-rehydration and freeze-thaw treatments. In addition, TdLEA3 reduced aggregate formation in the enzyme during these treatments.
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