ArticleThe Journal of biological chemistry2016
The Unstructured N-terminal Region of Arabidopsis Group 4 Late Embryogenesis Abundant (LEA) Proteins Is Required for Folding and for Chaperone-like Activity under Water Deficit.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed.
- Cross-species transcriptomics uncovers shared responses to water deficiency in plants.The plant genome · 2026Article
- Review
- Overexpression of theInternational journal of molecular sciences · 2026Article
- Structural flexibility of a recombinant intrinsically disordered LEA protein from Ramonda serbica.Scientific reports · 2025Article
- A phase transition modulates the protective function of a tardigrade disordered protein during desiccation.Protein science : a publication of the Protein Society · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Biomolecular condensates-Prerequisites for anhydrobiosis?Protein science : a publication of the Protein Society · 2025Review
- Disordered proteins interact with the chemical environment to tune their protective function during drying.eLife · 2024Article
- 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
- Insights into Genes Encoding LEA_1 Domain-Containing Proteins inPlants (Basel, Switzerland) · 2024Article
- Alternative conformations of a group 4 Late Embryogenesis Abundant protein associated to its in vitro protective activity.Scientific reports · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
- Intrinsically disordered regions are poised to act as sensors of cellular chemistry.Trends in biochemical sciences · 2023Review
- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- When Phased without Water: Biophysics of Cellular Desiccation, from Biomolecules to Condensates.Chemical reviews · 2023Review
- Transcriptome Analysis of Differentially Expressed Genes Associated with Salt Stress in Cowpea (International journal of molecular sciences · 2023Article
- Yeast osmoregulation - glycerol still in pole position.FEMS yeast research · 2022Review
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- Landscape of biomolecular condensates in heat stress responses.Frontiers in plant science · 2022Review
- Plant Protein Disorder: Spatial Regulation, Broad Specificity, Switch of Signaling and Physiological Status.Frontiers in plant science · 2022Article
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4 authors.
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Abstract
Late embryogenesis abundant (LEA) proteins are a conserved group of proteins widely distributed in the plant kingdom that participate in the tolerance to water deficit of different plant species. In silico analyses indicate that most LEA proteins are structurally disordered. The structural plasticity of these proteins opens the question of whether water deficit modulates their conformation and whether these possible changes are related to their function. In this work, we characterized the secondary structure of Arabidopsis group 4 LEA proteins. We found that they are disordered in aqueous solution, with high intrinsic potential to fold into α-helix. We demonstrate that complete dehydration is not required for these proteins to sample ordered structures because milder water deficit and macromolecular crowding induce high α-helix levels in vitro, suggesting that prevalent conditions under water deficit modulate their conformation. We also show that the N-terminal region, conserved across all group 4 LEA proteins, is necessary and sufficient for conformational transitions and that their protective function is confined to this region, suggesting that folding into α-helix is required for chaperone-like activity under water limitation. We propose that these proteins can exist as different conformers, favoring functional diversity, a moonlighting property arising from their structural dynamics.
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