ArticleScientific reports2024
Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 12 citations in OpenAlex.
- Diversifying particle-orientation distributions in cryo-EM with LEA protein additives.bioRxiv : the preprint server for biology · 2026Article
- Haplotype-resolved genome assembly of 'Manhattan' perennial ryegrass (Lolium perenne L.) and characterization of drought responsive late embryogenesis abundant genes.BMC genomics · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Effects of Temperature and Salt Stress onBiology · 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
- Exogenous LEA proteins expression enhances cold tolerance in mammalian cells by reducing oxidative stress.Scientific reports · 2025Article
- ThePlants (Basel, Switzerland) · 2025Article
- LEA proteins and ABA signaling: reciprocal regulation in stress adaptation.Frontiers in plant science · 2025Review
- Self-association and multimer formation in AtLEA4-5, a desiccation-induced intrinsically disordered protein from plants.Protein science : a publication of the Protein Society · 2024Article
- SCL15 Promotes Seed Longevity Acquisition in Arabidopsis thaliana by Enhancing Antioxidant and Repair Mechanisms During Maturation.Physiologia plantarumArticle
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Late Embryogenesis Abundant (LEA) proteins are a group of intrinsically disordered proteins implicated in plant responses to water deficit. In vitro studies revealed that LEA proteins protect reporter enzymes from inactivation during low water availability. Group 4 LEA proteins constitute a conserved protein family, displaying in vitro protective capabilities. Under water deficiency or macromolecular crowding, the N-terminal of these proteins adopts an alpha-helix conformation. This region has been identified as responsible for the protein in vitro protective activity. This study investigates whether the attainment of alpha-helix conformation and/or particular amino acid residues are required for the in vitro protective activity. The LEA4-5 protein from Arabidopsis thaliana was used to generate mutant proteins. The mutations altered conserved residues, deleted specific conserved regions, or introduced prolines to hinder alpha-helix formation. The results indicate that conserved residues are not essential for LEA4-5 protective function. Interestingly, the C-terminal region was found to contribute to this function. Moreover, alpha-helix conformation is necessary for the protective activity only when the C-terminal region is deleted. Overall, LEA4-5 shows the ability to adopt alternative functional conformations under the tested conditions. These findings shed light on the in vitro mechanisms by which LEA proteins protect against water deficit stress.
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