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LEA Proteins during Water Stress: Not Just for Plants Anymore
Annual Reviews of Physiology (2011)
  • Steven C. Hand, Louisiana State University
  • Michael A Menze, University of Louisville
  • Mehmet Toner, Harvard Medical School
  • Leaf Boswell, Louisiana State University
  • Daniel Moore, Louisiana State University
Late embryogenesis abundant (LEA) proteins are extremely hydrophilic proteins that were first identified in land plants. Intracellular accumulation is tightly correlated with acquisition of desiccation tolerance, and data support their capacity to stabilize other proteins and membranes during drying, especially in the presence of sugars like trehalose. Exciting reports now show LEA proteins are not restricted to plants; multiple forms are expressed in desiccation-tolerant animals from at least four phyla. We evaluate here the expression, subcellular localization, biochemical properties and potential functions of LEA proteins in animal species during water stress. LEA proteins are intrinsically unstructured in aqueous solution, but surprisingly, many only assume their native conformation during drying. They are targeted to multiple cellular locations, including mitochondria, and evidence supports that LEA proteins stabilize vitrified sugar glasses thought to be important in the dried state. More in vivo experimentation will be necessary to fully unravel the multiple functional properties of these macromolecules during water stress.
  • desiccation tolerance,
  • anhydrobiosis,
  • osmolytes,
  • trehalose,
  • intrinsically disordered proteins
Publication Date
Publisher Statement
This manuscript was accepted for publication in the Annual Review of Physiology. The final published version may be found here:
Citation Information
Steven C. Hand, Michael A Menze, Mehmet Toner, Leaf Boswell, et al.. "LEA Proteins during Water Stress: Not Just for Plants Anymore" Annual Reviews of Physiology Vol. 73 (2011)
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