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Dehydrins in plant stress responses

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Dehydrins, which belong to group 2 LEA (Late Embryogenesis Abundant) proteins, are a family of intrinsically unstructured plant proteins that accumulate during the late stages of embryogenesis, and play an important role in plant responses and adaptation to stress. ...

Dehydrins, which belong to group 2 LEA (Late Embryogenesis Abundant) proteins, are a family of intrinsically unstructured plant proteins that accumulate during the late stages of embryogenesis, and play an important role in plant responses and adaptation to stress.
Dehydrins are composed of several typical domains, designated as K, S and Y segments. The K segment is a lysine-rich consensus region of 15 amino acids, which forms an amphipathic α –helix, found in all dehydrins. The S-segment comprises 4 to 10 serine residues, the phosphorylation of this domain has been associated with the nuclear transport of the DHNs. The Y-segment shares homology with the nucleotide binding site of plants and bacterial chaperones. According to the appearance, number and distribution of these three segments, DHNs are subdivided into the following classes: SKn, YnSKn, YnKn, KnS. However, the precise functions of each subtype of DHNs are unknown. In vitro studies reveal common functions of cryoprotection to proteins and membranes.
Recently, the presence of other segments in dehydrins has been described. These include histidine-rich regions (H-X3-H, HH, and Hn), that allow to form complexes with metal ions, lysine rich sequences known as Poly-K or KEKE motif (KKKKKKEKKK), which can function as a polar zipper which interacts with polar KEKE motif present in other proteins or with DNA. The presence of these new segments suggests novel functions for dehydrins, such as chelators and DNA binding proteins.
This Research Topic will focus on molecular studies of dehydrins in plant stress responses with potential topics include, but are not limited to: structural, binding to molecules, biochemical and physico-chemical characterization and, bioinformatics and functional characterization of plant dehydrins.


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