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Published on March 21, 2008; 10.1104/pp.108.118208

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Received February 21, 2008
Accepted March 10, 2008

Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins

Denes Kovacs , Eva Kalmar , Zsolt Torok , and Peter Tompa *

Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, Budapest, Hungary, H-1113; Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, Puskin utca 9., Budapest, Hungary, H-1088; Institute of Biochemistry, Biological Research Center, POB 521, 6701 Szeged, Hungary

* Corresponding author; email: tompa{at}enzim.hu.

ERD10 and ERD14 (early response to dehydration, ERD) proteins are members of the dehydrin (DHN) family which accumulate in response to abiotic environmental stresses, such as high salinity, drought and low temperature, in Arabidopsis thaliana. Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remain poorly understood. Here detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins (IDPs), 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, though. Membrane binding is strongly influenced by ionic strength. Our results show that these IDPs have chaperone activity of rather wide substrate specificity, and 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.




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