InterPro domain: IPR000167

Dehydrin has been classified as part of the LEA family (D-11 from Dure, or group 2 from Bray) [ 1 ]. Dehydrins contribute to freezing stress tolerance in plants and it was suggested that this could be partly due to their protective effect on membranes [ 2 ].

Dehydrins share a number of structural features. One of the most notablefeatures is the presence, in their central region, of a continuous run offive to nine serines followed by a cluster of charged residues. Such a regionhas been found in all known dehydrins so far with the exception of peadehydrins. A second conserved feature is the presence of two copies of alysine-rich octapeptide; the first copy is located just after the clusterof charged residues that follows the poly-serine region and the second copyis found at the C-terminal extremity.

LEA (late embryogenesis abundant) proteins were first identified in land plants. Plant LEA proteins have been found to accumulate to high levels during the last stage of seed formation (when a natural desiccation of the seed tissues takes place) and during periods of water deficit in vegetative organs. Later, LEA homologues have also been found in various species [ 3 , 4 ]. They have been classified into several subgroups in Pfam and according to Bray and Dure [ 5 ].

1. LEA (late embryogenesis abundant) proteins and their encoding genes in Arabidopsis thaliana. BMC Genomics 9, 118
2. Overexpression of multiple dehydrin genes enhances tolerance to freezing stress in Arabidopsis. Plant Mol. Biol. 54, 743-53
3. LEA proteins during water stress: not just for plants anymore. Annu. Rev. Physiol. 73, 115-34
4. Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J. Biol. Chem. 275, 5668-74