OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) OA All Versions of this Article: 147/1/381    most recent pp.108.118208v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (11) Citing Articles via Google Scholar Google Scholar Articles by Kovacs, D. Articles by Tompa, P. Search for Related Content PubMed PubMed Citation Articles by Kovacs, D. Articles by Tompa, P. Agricola Articles by Kovacs, D. Articles by Tompa, P.

ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins^1,[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.

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.

This article has been cited by other articles:

				S. Teotia and R. S. Lamb The Paralogous Genes RADICAL-INDUCED CELL DEATH1 and SIMILAR TO RCD ONE1 Have Partially Redundant Functions during Arabidopsis Development Plant Physiology, September 1, 2009; 151(1): 180 - 198. [Abstract] [Full Text] [PDF]

				M.-C. Koag, S. Wilkens, R. D. Fenton, J. Resnik, E. Vo, and T. J. Close The K-Segment of Maize DHN1 Mediates Binding to Anionic Phospholipid Vesicles and Concomitant Structural Changes Plant Physiology, July 1, 2009; 150(3): 1503 - 1514. [Abstract] [Full Text] [PDF]

				J. Erales, S. Lignon, and B. Gontero CP12 from Chlamydomonas reinhardtii, a Permanent Specific "Chaperone-like" Protein of Glyceraldehyde-3-phosphate Dehydrogenase J. Biol. Chem., May 8, 2009; 284(19): 12735 - 12744. [Abstract] [Full Text] [PDF]

				J.-M. Mouillon, S. K. Eriksson, and P. Harryson Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse Plant Physiology, December 1, 2008; 148(4): 1925 - 1937. [Abstract] [Full Text] [PDF]

				M. Battaglia, Y. Olvera-Carrillo, A. Garciarrubio, F. Campos, and A. A. Covarrubias The Enigmatic LEA Proteins and Other Hydrophilins Plant Physiology, September 1, 2008; 148(1): 6 - 24. [Full Text] [PDF]