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LEA Proteins

Bdelloid Rotifer stained with LEA antibody
Bdelloid rotifer A. ricciae with DNA stained blue and LEA protein stained red.
LEA (Late Embryogenesis Abundant) proteins were identified more than twenty years ago in plant seeds where their expression is associated with acquisition of desiccation tolerance. Three major Groups (numbered 1, 2 and 3) of LEA proteins have been described subsequently in a range of different plants and plant tissues. Homologues of Group 1 and 3 proteins have also been found in bacteria and certain invertebrates. Their precise molecular function has been unclear, however.

We have focussed on the potential function of LEA proteins as protein stabilisers, but it has also been proposed that they act as as antioxidants, as membrane stabilisers, as ion sinks or hydration buffers. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as “space fillers” to prevent cellular collapse at low water activities. Such multifunctional capacity of the LEA proteins could be attributable in part to their structural plasticity, since they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. These potential functions are reviewed in Tunnacliffe & Wise (2007).

LEA Protein Research Topics:


Browne, J., Tunnacliffe, A. and Burnell, A. (2002) Plant desiccation gene found in a nematode. Nature 416: 38.

Browne, J. A., Dolan, K. M., Tyson, T., Goyal, K., Tunnacliffe, A. and Burnell, A. M. (2004) Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae. Eukaryot. Cell 3: 966-975.

Chakrabortee, S., Boschetti, C., Walton, L. J., Sarkar, S., Rubinsztein, D. C. and Tunnacliffe, A. (2007) Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function. Proc. Natl. Acad. Sci. USA 104: 18073-18078.

Goyal, K., Tisi, L., Basran, A., Browne, J., Burnell, A., Zurdo, J. and Tunnacliffe, A. (2003) Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J. Biol. Chem. 278: 12977-12984.

Goyal, K., Walton, L. and Tunnacliffe, A. (2005) LEA proteins prevent aggregation due to water stress. Biochem J. 388: 151-157.

Goyal, K., Pinelli, C., Maslen, S. L., Rastogi, R. K., Stephens, E. and Tunnacliffe, A. (2005) Dehydration-regulated processing of late embryogenesis abundant protein in a desiccation-tolerant nematode. FEBS Lett. 579: 4093-4098.

Tunnacliffe, A., Lapinski, J. and McGee, B. (2005) A putative LEA protein, but no trehalose, is present in anhydrobiotic bdelloid rotifers. Hydrobiologia 546: 315-321.

Tunnacliffe, A. and Wise, M. J. (2007) The continuing conundrum of the LEA proteins. Naturwissenschaften 94: 791-812.

Wise, M. J. and Tunnacliffe, A. (2004) POPP the question: what do LEA proteins do? Trends Plant Sci. 9: 13-17.