Dehydrins: Emergence of a biochemical role of a family of plant dehydration proteins

TLDR

Plants accumulate a variety of proteins in response to dehydration‑related stresses such as drought, cold, salinity, and seed maturation, with dehydrins—members of the LEA D‑II family—being the most frequently induced yet poorly understood at the biochemical level. Recent studies employ immunolocalization and in‑vitro biochemical assays, drawing analogies to better characterized proteins, to elucidate dehydrin function. Dehydrins act as structure stabilizers with detergent‑ and chaperone‑like properties, targeting nuclear and cytoplasmic components, and genetic mapping of dhn genes linked to freezing tolerance in barley and related species implicates them as key players in dehydration tolerance.

Abstract

A number of proteins have been identified that typically accumulate in plants in response to any environmental stimulus that has a dehydrative component or is temporally associated with dehydration. This includes drought, low temperature, salinity and seed maturation. Among the induced proteins, dehydrins (late embryogenesis abundant [LEA] D‐II family) have been the most commonly observed, yet we still have an incomplete knowledge of their fundamental biochemical role in the cell. Current research trends are changing this situation: immunolocalization and in vitro biochemical analyses are, through analogies to other more fully characterized proteins and molecules, shaping our understanding. In brief, dehydrins may be structure stabilizers with detergent and chaperone‐like properties and an array of nuclear and cytoplasmic targets. Recent progress on the mapping of dhn genes and the inheritance of freezing tolerance in barley and other Triticeae species tentatively points to dehydrins as key components of dehydration tolerance.