|Title||Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins.|
|Publication Type||Journal Article|
|Year of Publication||2008|
|Authors||Kovacs, D., E. Kalmar, Z. Torok, and P. Tompa|
|Date Published||2008 May|
|Type of Article||idp|
|Keywords||Alcohol Dehydrogenase, Arabidopsis, Arabidopsis Proteins, Citrate (si)-Synthase, Hot Temperature, Intracellular Membranes, Luciferases, Firefly, Molecular Chaperones, Muramidase, Plant Proteins, Substrate Specificity, Water|
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.
|Alternate Journal||Plant Physiol.|
|PubMed Central ID||PMC2330285|
|Grant List||ISRF 067595 / / Wellcome Trust / United Kingdom|
Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins.