ArticlePlanta2014
Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro.
Article in Planta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 68 citations in OpenAlex.
- Prokaryotic expression, purification, and the in vitro and in vivo protection study of dehydrin WDHN2 from Triticum aestivum.Protoplasma · 2024Article
- Protective roles of highly conserved motif 1 in tardigrade cytosolic-abundant heat soluble protein in extreme environments.Protein science : a publication of the Protein Society · 2024Article
- Protein Disorder in Plant Stress Adaptation: From Late Embryogenesis Abundant to Other Intrinsically Disordered Proteins.International journal of molecular sciences · 2024Review
- Plants use molecular mechanisms mediated by biomolecular condensates to integrate environmental cues with development.The Plant cell · 2023Review
- Genomic Analysis ofLife (Basel, Switzerland) · 2022Article
- Genome-wide identification, evolutionary and expression analyses of LEA gene family in peanut (Arachis hypogaea L.).BMC plant biology · 2022Article
- Chromosome-condensed G1 phase yeast cells are tolerant to desiccation stress.Microbial cell (Graz, Austria) · 2022Article
- Genome-wide identification and analysis ofFrontiers in plant science · 2022Article
- Article
- Characterization of the Heat-Stable Proteome during Seed Germination in Arabidopsis with Special Focus on LEA Proteins.International journal of molecular sciences · 2021Article
- Article
- The N-Terminal Region of Soybean PM1 Protein Protects Liposomes during Freeze-Thaw.International journal of molecular sciences · 2020Article
- Similar Yet Different-Structural and Functional Diversity amongInternational journal of molecular sciences · 2020Article
- Common Functions of Disordered Proteins across Evolutionary Distant Organisms.International journal of molecular sciences · 2020Review
- Isolation and characterization of an atypical LEA gene (IpLEA) from Ipomoea pes-caprae conferring salt/drought and oxidative stress tolerance.Scientific reports · 2019Article
- Protecting Enzymes from Stress-Induced Inactivation.Biochemistry · 2019Review
- Genome-wide identification of and functional insights into the late embryogenesis abundant (LEA) gene family in bread wheat (Triticum aestivum).Scientific reports · 2019Article
- A beetle antifreeze protein protects lactate dehydrogenase under freeze-thawing.International journal of biological macromolecules · 2019Article
- Sequence composition versus sequence order in the cryoprotective function of an intrinsically disordered stress-response protein.Protein science : a publication of the Protein Society · 2019Article
- Protecting activity of desiccated enzymes.Protein science : a publication of the Protein Society · 2019Article
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MAIN
conclusionExpression of eight LEA genes enhanced desiccation tolerance in yeast, including two LEA_2 genes encoding atypical, stably folded proteins. The recombinant proteins showed enzyme, but not membrane protection during drying. To screen for possible functions of late embryogenesis abundant (LEA) proteins in cellular stress tolerance, 15 candidate genes from six Arabidopsis thaliana LEA protein families were expressed in Saccharomyces cerevisiae as a genetically amenable eukaryotic model organism. Desiccation stress experiments showed that eight of the 15 LEA proteins significantly enhanced yeast survival. While none of the proteins belonging to the LEA_1, LEA_5 or AtM families provided protection to yeast cells, two of three LEA_2 proteins, all three LEA_4 proteins and three of four dehydrins were effective. However, no significantly enhanced tolerance toward freezing, salt, osmotic or oxidative stress was observed. While most LEA proteins are highly hydrophilic and intrinsically disordered, LEA_2 proteins are "atypical", since they are more hydrophobic and possess a stable folded structure in solution. Because nothing was known about the functional properties of LEA_2 proteins, we expressed the three Arabidopsis proteins LEA1, LEA26 and LEA27 in Escherichia coli. The bacteria expressed all three proteins in inclusion bodies from which they could be purified and refolded. Correct folding was ascertained by Fourier transform Infrared (FTIR) spectroscopy. None of the proteins was able to stabilize liposomes during freezing or drying, but they were all able to protect the enzyme lactate dehydrogenase (LDH) from inactivation during freezing. Significantly, only LEA1 and LEA27, which also protected yeast cells during drying, were able to stabilize LDH during desiccation and subsequent rehydration.
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