Clonging And Functional Analysis Of Dehydrin WDHN1 From Wheat

Dehydrins(DHNs), also known as LEA II(late embryogenesis abundant) proteins, accumulate during late seed developmental stages and in vegetative tissues subjected to dehydration, salt, and low temperature stress. DHNs are a group of intrinsically disordered proteins due to high proportions of hydrophilic amino acids. It is assumed that intrinsically disordered character of DHNs allows them to change their conformation according to the changes in their ambient microenvironment, resulting in multiple functions,In order to determine the function of YSK2 dehydrin, we cloned WDHN1 dehydrin from wheat, and investigated the expression patterns of WDHN1, the anti-aggregation effects of protein WDHN1 on E. coli viability and lactate dehydrogenase(LDH) activity during multiple abiotic stress treatments.The main results of the experiment are as following:1. The CDS of WDHN1 had a length of 491 bp, contained two exons and oneintron, encoding a protein of 133 amino acids with predicted molecular weight of 13.93 kDa, an isoelectric point(pI) of 8.81 and grand average of hydropathicity(GRAVY) index of-1.189. The deduced polypeptide is basic and hydrophilic, which has typical features of DHNs that contains one segment Y segment, one S segment and two K segments. A phylogenetic tree analysis with the related DHNs isolated from different plant species indicated that WDHN1 shared homology with EMT30992.2. Based on PLACE and PlantCARE database analysis, the abiotic stress-related elements of WDHN1 promoter were determined, which contained two ABRE, and three MBS.3. The qRT-PCR results showed that WDHN1 transcript accumulation was induced by low temperature, PEG, ABA and NaCl observably. It should be emphasized that, compared with the increases that were observed with the ABA and PEG treatments, the transcript levels reached much higher levels under low temperature and NaCl treatments, i.e., 1.5-3-fold vs. 118-80-fold increases, respectively.4. WDHN1 protein enhanced tolerance of E. coli under PEG and NaCl stress, and preserved stabilization of the LDH against dehydration and freezing stress.5. WDHN1 could perform chaperone activity via preventing protein aggregation.