ArticleThe Biochemical journal2019
Preferential adsorption to air-water interfaces: a novel cryoprotective mechanism for LEA proteins.
Article in The Biochemical journal, 2019. 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.
- Diversifying particle-orientation distributions in cryo-EM with LEA protein additives.bioRxiv : the preprint server for biology · 2026Article
- Review
- Evaluation of a bacterial group 1 LEA protein as an enzyme protectant from stress-induced inactivation.Applied microbiology and biotechnology · 2022Article
- In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance inInternational journal of molecular sciences · 2022Article
- Article
- Generic nature of the condensed states of proteins.Nature cell biology · 2021Review
- New group of transmembrane proteins associated with desiccation tolerance in the anhydrobiotic midge Polypedilum vanderplanki.Scientific reports · 2020Article
- Late Embryogenesis Abundant Protein-Client Protein Interactions.Plants (Basel, Switzerland) · 2020Review
- Mechanisms of Desiccation Tolerance: Themes and Variations in Brine Shrimp, Roundworms, and Tardigrades.Frontiers in physiology · 2020Review
- Structural properties and cellular expression of AfrLEA6, a group 6 late embryogenesis abundant protein from embryos of Artemia franciscana.Cell stress & chaperones · 2019Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Late embryogenesis abundant (LEA) proteins comprise a diverse family whose members play a key role in abiotic stress tolerance. As intrinsically disordered proteins, LEA proteins are highly hydrophilic and inherently stress tolerant. They have been shown to stabilise multiple client proteins under a variety of stresses, but current hypotheses do not fully explain how such broad range stabilisation is achieved. Here, using neutron reflection and surface tension experiments, we examine in detail the mechanism by which model LEA proteins, AavLEA1 and ERD10, protect the enzyme citrate synthase (CS) from aggregation during freeze-thaw. We find that a major contributing factor to CS aggregation is the formation of air bubbles during the freeze-thaw process. This greatly increases the air-water interfacial area, which is known to be detrimental to folded protein stability. Both model LEA proteins preferentially adsorb to this interface and compete with CS, thereby reducing surface-induced aggregation. This novel surface activity provides a general mechanism by which diverse members of the LEA protein family might function to provide aggregation protection that is not specific to the client protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.