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First published online March 21, 2008; 10.1104/pp.108.118208 Plant Physiology 147:381-390 (2008) © 2008 American Society of Plant Biologists OPEN ACCESS ARTICLE
Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins1,[OA]Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary H–1113 (D.K., P.T.); Department of Medical Chemistry, Molecular Biology, and Pathobiochemistry, Semmelweis University, Budapest, Hungary H–1088 (E.K.); and Institute of Biochemistry, Biological Research Center, H–6701 Szeged, Hungary (Z.T.)
ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana). Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. Membrane binding is strongly influenced by ionic strength. Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.
1 This work was supported by the Hungarian Scientific Research Fund (grant no. K60694), the Ministry of Health of Hungary (grant no. ETT 245/2006), and an International Senior Research Fellowship from the Wellcome Trust (grant no. ISRF 067595). The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Peter Tompa (tompa{at}enzim.hu). [OA] Open Access articles can be viewed online without a subscription. www.plantphysiol.org/cgi/doi/10.1104/pp.108.118208 * Corresponding author; e-mail tompa{at}enzim.hu. Received February 21, 2008; accepted March 10, 2008; published March 21, 2008.
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