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Updated: May 17, 2025

Detection of Histone Modifications in Plant Leaves
Published on: September 23, 2011
Ethylene Signaling Modulates Dehydrin Expression in Arabidopsis thaliana Under Prolonged Dehydration
Irina I Vaseva1, Heorhii Balzhyk1, Maria Trailova1
1Institute of Plant Physiology and Genetics, Bulgarian Academy of Sciences, Acad. Georgi Bonchev Street, Bldg. 21, 1113 Sofia, Bulgaria.
Abstract:
Dehydrins are stress-inducible proteins with protective functions, characterized by high hydrophilicity, thermostability, and a low degree of secondary structure. They stabilize cellular membranes, preserve macromolecule conformation, and support enzymatic and structural protein functions. Their accumulation in plant tissues under drought is regulated by abscisic acid (ABA)-dependent and ABA-independent pathways. Ethylene plays a key role in stress adaptation, but its relationship with dehydrin accumulation remains unclear. This study investigates how ethylene influences dehydrin expression in Arabidopsis thaliana during prolonged dehydration using transcript profiling and immunodetection in wild-type (Col-0), ethylene-constitutive (ctr1-1), and ethylene-insensitive (ein3eil1) mutants. Comparative analyses showed increased survival of ctr1-1 plants under dehydration stress, likely due to reduced oxidative damage. Analysis of dehydrin-coding genes identified multiple Ethylene Response Factor (ERF) binding sites, flanking the transcription start sites, which suggests a fine-tuned ethylene-dependent regulation. The ability of ethylene signaling to either suppress or stabilize particular dehydrins was demonstrated by RT-qPCR and immunodetection experiments. Under drought stress, ethylene signaling appeared to suppress root-specific dehydrins. A Y-segment-containing protein with approximate molecular weight of 20 kDa showed decreased levels in ctr1-1 and higher accumulation in ein3eil1, indicating that ethylene signaling acts as a negative regulator. These results provide new information on the dual role of ethylene in dehydrin control, highlighting its function as a molecular switch in stress adaptive responses.
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