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Article Addendum

Disordered plant LEA proteins as molecular chaperones

Denes Kovacs, Bianka Agoston and Peter Tompa

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Plants often respond to abiotic stresses by the increased expression of LEA (late embryogenesis abundant) proteins, so called because they also accompany seed formation. Whereas the cellular function of LEA proteins in mitigating the damage caused by stress is clear, the molecular mechanisms of their action are rather enigmatic. Several models have been developed, based on their putative activities as ion sinks, stabilizers of membrane structure, buffers of hydrate water, antioxidants, and/or chaperones. Due to their known structural flexibility, this latter idea has received little experimental attention thus far. Recently, however, it has been suggested that intrinsically disordered proteins (IDPs) may exert chaperone activity by an “entropy transfer” mechanism. In our subsequent study published in the May issue of Plant Physiology, we provided evidence that two group 2 LEA proteins, ERD (early response to dehydration) 10 and 14, are potent molecular chaperones. This observation may have far-reaching implications, as it may explain how LEA proteins of ill-defined structures protect plant cells during dehydration, and it may also lead to the general experimental validation of the entropy transfer model of disordered chaperones.

Addendum to: Kovacs D, Kalmar E, Torok Z, Tompa P. Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol. 2008; 147: 381–390.

Authors

Denes Kovacs

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, Hungary

Bianka Agoston

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, Hungary

Peter Tompa

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, 1518 Budapest, Hungary

Purchase article for $19

Subscribe to this journal for $79/year