ArticleThe Journal of biological chemistry2014
A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Design, Structural Stability, Membrane Binding, and Antibacterial Activity of Novel Antimicrobial Peptides Derived from Wuchuanin-A1.Life (Basel, Switzerland) · 2025Article
- A Group 6 LEA Protein Plays Key Roles in Tolerance to Water Deficit, and in Maintaining the Glassy State and Longevity of Seeds.Plant, cell & environment · 2025Article
- Functional diversity of Arabidopsis late embryogenesis abundant proteins in response to changes in the physicochemical environment.bioRxiv : the preprint server for biology · 2025Article
- 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
- Mechanosensitive ion channels MSL8, MSL9, and MSL10 have environmentally sensitive intrinsically disordered regions with distinct biophysical characteristics in vitro.Plant direct · 2023Article
- Article
- Subcellular Localization of Seed-Expressed LEA_4 Proteins Reveals Liquid-Liquid Phase Separation for LEA9 and for LEA48 Homo- and LEA42-LEA48 Heterodimers.Biomolecules · 2021Article
- Folding and self-assembly of short intrinsically disordered peptides and protein regions.Nanoscale advances · 2021Review
- Structural properties and enzyme stabilization function of the intrinsically disordered LEA_4 protein TdLEA3 from wheat.Scientific reports · 2019Article
- Structural Plasticity of Intrinsically Disordered LEA Proteins fromFrontiers in plant science · 2019Article
- The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer.International journal of molecular sciences · 2018Article
- Article
- In vivo evidence for homo- and heterodimeric interactions of Arabidopsis thaliana dehydrins AtCOR47, AtERD10, and AtRAB18.Scientific reports · 2017Article
- Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017Review
- Group 4 late embryogenesis abundant proteins as a model to study intrinsically disordered proteins in plants.Plant signaling & behavior · 2017Article
- Insights on Structure and Function of a Late Embryogenesis Abundant Protein fromFrontiers in plant science · 2017Article
- 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.The Journal of biological chemistry · 2016Article
- Review
- Multiple copies of a novel amphipathic α-helix forming segment in Physcomitrella patens dehydrin play a key role in abiotic stress mitigation.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Late embryogenesis-abundant proteins accumulate to high levels in dry seeds. Some of them also accumulate in response to water deficit in vegetative tissues, which leads to a remarkable association between their presence and low water availability conditions. A major sub-group of these proteins, also known as typical LEA proteins, shows high hydrophilicity and a high percentage of glycine and other small amino acid residues, distinctive physicochemical properties that predict a high content of structural disorder. Although all typical LEA proteins share these characteristics, seven groups can be distinguished by sequence similarity, indicating structural and functional diversity among them. Some of these groups have been extensively studied; however, others require a more detailed analysis to advance in their functional understanding. In this work, we report the structural characterization of a group 6 LEA protein from a common bean (Phaseolus vulgaris L.) (PvLEA6) by circular dichroism and nuclear magnetic resonance showing that it is a disordered protein in aqueous solution. Using the same techniques, we show that despite its unstructured nature, the addition of trifluoroethanol exhibited an intrinsic potential in this protein to gain helicity. This property was also promoted by high osmotic potentials or molecular crowding. Furthermore, we demonstrate that PvLEA6 protein is able to form soluble homo-oligomeric complexes that also show high levels of structural disorder. The association between PvLEA6 monomers to form dimers was shown to occur in plant cells by bimolecular fluorescence complementation, pointing to the in vivo functional relevance of this association.
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