ArticleProtein science : a publication of the Protein Society2024
Self-association and multimer formation in AtLEA4-5, a desiccation-induced intrinsically disordered protein from plants.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Evolutionary constraint on a core winter proteome across independently cold-adapted PACMAD grasses.PloS one · 2026Article
- A Coding SNP in GmPM30 Enhances Soybean Salinity Tolerance and Yield through the GmLEA1-GmPM30-GmLEC1 Module.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- Genome-Wide Identification of theGenes · 2025Article
- 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
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Abstract
During seed maturation, plants may experience severe desiccation, leading to the accumulation of late embryogenesis abundant (LEA) proteins. These intrinsically disordered proteins also accumulate in plant tissues under water deficit. Functional roles of LEA proteins have been proposed based on in vitro studies, where monomers are considered as the functional units. However, the potential formation of homo-oligomers has been little explored. In this work, we investigated the potential self-association of Arabidopsis thaliana group 4 LEA proteins (AtLEA4) using in vitro and in vivo approaches. LEA4 proteins represent a compelling case of study due to their high conservation throughout the plant kingdom. This protein family is characterized by a conserved N-terminal region, with a high alpha-helix propensity and invitro protective activity, as compared to the highly disordered and low-conserved C-terminal region. Our findings revealed that full-length AtLEA4 proteins oligomerize and that both terminal regions are sufficient for self-association in vitro. However, the ability of both amino and carboxy regions of AtLEA4-5 to self-associate invivo is significantly lower than that of the entire protein. Using high-resolution and quantitative fluorescence microscopy, we were able to disclose the unreported ability of LEA proteins to form high-order oligomers in planta. Additionally, we found that high-order complexes require the simultaneous engagement of both terminal regions, indicating that the entire protein is needed to attain such structural organization. This research provides valuable insights into the self-association of LEA proteins in plants and emphasizes the role of protein oligomer formation.
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