Plant Growth Regulation

, Volume 62, Issue 3, pp 241–255

Desiccation tolerant plants as model systems to study redox regulation of protein thiols

Authors

  • Louise Colville
    • Seed Conservation DepartmentRoyal Botanic Gardens Kew
    • Seed Conservation DepartmentRoyal Botanic Gardens Kew
SI Plant Desiccation Stress

DOI: 10.1007/s10725-010-9482-9

Cite this article as:
Colville, L. & Kranner, I. Plant Growth Regul (2010) 62: 241. doi:10.1007/s10725-010-9482-9

Abstract

While the majority of plants and animals succumb to water loss, desiccation tolerant organisms can lose almost all of their intracellular water and revive upon rehydration. Only about 300 ‘resurrection’ angiosperms and very few animals are desiccation tolerant. By contrast, many bryophytes and most lichens are desiccation tolerant and so are the seeds and pollen grains of most flowering plants. The current literature reveals that the extreme fluctuations in water content experienced by desiccation tolerant organisms are accompanied by equally extreme changes in cellular redox state. Strongly oxidizing conditions upon desiccation can cause irreversible oxidation of free cysteine residues of proteins, which can change protein structure and function, and contribute to protein denaturation. It appears likely that reversible formation of disulphide bonds, in particular through protein glutathionylation, contributes to the set of protection mechanisms that confer desiccation tolerance. Upon rehydration, de-glutathionylation can be catalyzed by glutaredoxins (GRXs) and protein disulphide bonds can be reduced through NADPH-dependent thioredoxins (TRXs). Due to their ability to survive severe oxidative stress, desiccation tolerant plants and seeds are excellent models to study protein redox regulation, which may provide tools for enhancing tolerance to drought and more generally, to oxidative stress, in crops.

Keywords

DesiccationGlutaredoxinGlutathioneGlutathionylationThiolThioredoxin

Copyright information

© Springer Science+Business Media B.V. 2010