LEA proteins: IDPs with versatile functions in cellular dehydration tolerance.

@article{Hincha2012LEAPI,
  title={LEA proteins: IDPs with versatile functions in cellular dehydration tolerance.},
  author={Dirk Karl Hincha and Anja Thalhammer},
  journal={Biochemical Society transactions},
  year={2012},
  volume={40 5},
  pages={
          1000-3
        }
}
LEA (late embryogenesis abundant) proteins were originally described almost 30 years ago as accumulating late in plant seed development. They were later found to be induced in vegetative plant tissues under environmental stress conditions and also in desiccation-tolerant micro-organisms and invertebrates. Although they are widely assumed to play crucial roles in cellular dehydration tolerance, their physiological and biochemical functions are largely unknown. Most LEA proteins are predicted to… 
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The Function and Evolution of Closely Related COR/LEA (Cold-Regulated/Late Embryogenesis Abundant) Proteins in Arabidopsis thaliana
TLDR
The evolutionary relationships between LEA proteins are explored and the transcriptional networks that the encoding genes participate in are analyzed, including those of COR15A, a nuclear-encoded, cold-induced LEA_4 protein that is localized in the chloroplast stroma.
Plant Group II LEA Proteins: Intrinsically Disordered Structure for Multiple Functions in Response to Environmental Stresses
TLDR
The distribution, structural architecture, and genomic diversification of group II LEA proteins are described, with some recent investigations on their regulation and molecular expression under various abiotic stresses.
Functional characterization of selected LEA proteins from Arabidopsis thaliana in yeast and in vitro
TLDR
Expression of eight LEA genes enhanced desiccation tolerance in yeast, including two LEA_2 genes encoding atypical, stably folded proteins, which enhanced yeast survival and enhanced tolerance toward freezing, salt, osmotic or oxidative stress.
Expression, Purification, and Characterization of an Intrinsically Disordered Late Embryogenesis Abundant (LEA) Protein from Artemia franciscana Utilizing Escherichia coli and Nicotiana tabacum
TLDR
It is found, that a purified group 1 LEA protein from A. franciscana (AfrLEA 1 . 1 ) helped to retain enzyme activity after desiccation of lactate dehydrogenase (LDH) for land 7 days in the presence or absence of BSA or trehalose or other purified LEAprotein.
Late Embryogenesis Abundant (LEA) proteins confer water stress tolerance to mammalian somatic cells.
Similar Yet Different–Structural and Functional Diversity among Arabidopsis thaliana LEA_4 Proteins
TLDR
Although the six experimentally characterized LEA_4 proteins have similar structural and functional characteristics, differences concerning their folding propensity and membrane stabilization capacity during a freeze/thaw cycle are obvious and cannot be easily attributed to sequence conservation, simple physicochemical characteristics or the abundance of sequence motifs.
Late Embryogenesis Abundant (LEA) Gene Family in Maize: Identification, Evolution, and Expression Profiles
Late embryogenesis abundant (LEA) proteins are identified as a large and highly diverse group of polypeptides accumulating in response to cellular dehydration in many organisms. However, there are…
Late Embryogenesis Abundant (LEA) Gene Family in Maize: Identification, Evolution, and Expression Profiles
  • X. Li, J. Cao
  • Biology
    Plant Molecular Biology Reporter
  • 2015
TLDR
This study will provide comprehensive information for maize LEA gene family and may pave the way for deciphering their functions in further studies.
Late Embryogenesis Abundant (LEA) proteins confer water stress tolerance to mammalian somatic cells
TLDR
It is shown that natural xeroprotectants (LEA proteins) transiently expressed in somatic cells confer them desiccation tolerance, and plasmalemma, cytoskeleton and mitochondria appeared unaffected in LEA-expressing cells, confirming their protective action during the entire desICcation and rehydration process.
Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo
TLDR
The results suggest that the structural plasticity of XsLEAs is essential for their protective activity to avoid damage of various subcellular components caused by water deficit stress.
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References

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TLDR
Evaluation of the expression, subcellular localization, biochemical properties, and potential functions of LEA proteins in animal species during water stress shows they are targeted to multiple cellular locations, including mitochondria, and evidence supports that LEA protein stabilize vitrified sugar glasses thought to be important in the dried state.
The continuing conundrum of the LEA proteins
TLDR
This review presents some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlights several possible functions, including roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields.
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TLDR
A genome-wide analysis of LEA proteins and their encoding genes in Arabidopsis thaliana indicates a wide range of sequence diversity, intracellular localizations, and expression patterns and indicates that they confer an evolutionary advantage for an organism under varying stressful environmental conditions.
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TLDR
First evidence of anti-aggregation activity of LEA proteins due to water stress is found, which is significant given that non-reducing disaccharides are known to accumulate during dehydration in plants and nematodes.
A mitochondrial late embryogenesis abundant protein stabilizes model membranes in the dry state.
Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine‐dependent protein aggregation
LEA Proteins: Versatility of Form and Function
TLDR
Findings suggest that LEA proteins play various, possibly multiple, roles in the drying cell: they are implicated in the homeostasis of proteins and nucleic acids, in stabilizing cell membranes, in redox balancing and in the formation and stability of the glassy state.
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TLDR
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TLDR
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