ArticlePlant signaling & behavior2017
Group 4 late embryogenesis abundant proteins as a model to study intrinsically disordered proteins in plants.
Article in Plant signaling & behavior, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.
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Who cites it
21 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Proline concentrations in seedlings of woody plants change with drought stress duration and are mediated by seed characteristics: a meta-analysis.Scientific reports · 2023Pooled it
- Overexpression of theInternational journal of molecular sciences · 2026Article
- Evolutionary constraint on a core winter proteome across independently cold-adapted PACMAD grasses.PloS one · 2026Article
- Haplotype-resolved genome assembly of 'Manhattan' perennial ryegrass (Lolium perenne L.) and characterization of drought responsive late embryogenesis abundant genes.BMC genomics · 2025Article
- Group 1 LEA Proteins in Durum Wheat: Evolution, Expression, and Roles in Abiotic Stress Tolerance.Plants (Basel, Switzerland) · 2025Article
- Grass Rhizome Proteomics Reveals Convergent Freezing-Tolerance Strategies.bioRxiv : the preprint server for biology · 2025Article
- Article
- Chayote Fruit (Plants (Basel, Switzerland) · 2022Article
- Desiccation Tolerance inPlants (Basel, Switzerland) · 2022Article
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- The Orthodox Dry Seeds Are Alive: A Clear Example of Desiccation Tolerance.Plants (Basel, Switzerland) · 2021Review
- Newly defined allergens in the WHO/IUIS Allergen Nomenclature Database during 01/2019-03/2021.Allergy · 2021Review
- Transcriptomic and Proteomic Analysis of Drought Stress Response in Opium Poppy Plants during the First Week of Germination.Plants (Basel, Switzerland) · 2021Article
- Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance inInternational journal of molecular sciences · 2021Article
- Lysine, Lysine-Rich, Serine, and Serine-Rich Proteins: Link Between Metabolism, Development, and Abiotic Stress Tolerance and the Role of ncRNAs in Their Regulation.Frontiers in plant science · 2020Review
- Dissecting the Genomic Diversification of Late Embryogenesis Abundant (LEA) Protein Gene Families in Plants.Genome biology and evolution · 2019Article
- Structural Plasticity of Intrinsically Disordered LEA Proteins fromFrontiers in plant science · 2019Article
- Intrinsically disordered proteins in crowded milieu: when chaos prevails within the cellular gumbo.Cellular and molecular life sciences : CMLS · 2018Review
- Structural and Functional Dynamics of Dehydrins: A Plant Protector Protein under Abiotic Stress.International journal of molecular sciences · 2018Review
- Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Late Embryogenesis Abundant (LEA) proteins comprise a heterogeneous group of proteins that accumulate to high levels in the dry seed and in vegetative plant tissues under water deficit. We recently reported that group 4 LEA proteins from Arabidopsis thaliana, regardless of their structural disorder prevalent in aqueous solution, are able to fold into α-helix when subjected to water deficit and/or macromolecular crowding environments. Interestingly, the ability to gain structure under water limiting conditions is circumscribed to the N-terminal conserved region. This environment- driven conformational plasticity has a functional impact because the conserved N-terminal region is necessary and sufficient to prevent the inactivation and/or aggregation of reporter enzymes, when they are subjected to partial dehydration or freeze-thaw treatments. In this addendum we present a broader analysis of the data and propose that the mechanism by which group 4 LEA proteins exert their chaperone-like activity occurs via a selection of particular LEA structural conformations favored by water deficit environments. In addition, we include further observations regarding the abundance and conservation of histidine residues in LEA proteins of this group, particularly at the C-terminal variable region, supporting the presence of an additional function in the same polypeptides as metal ion sequesters. The structural characteristics of group 4 LEA proteins together with their conceivable multifunctionality, a widespread feature in Intrinsically Disordered Proteins (IDPs), raises the possibility of using this set of proteins as a model to investigate the structure-function relationship of IDPs in plants.
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