Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro

Abstract

BackgroundDehydrins play positive roles in regulating plant abiotic stress responses. The objective of this study was to characterize two dehydrin genes, CdDHN4-L and CdDHN4-S, generated by alternative splicing of CdDHN4 in bermudagrass.ResultsOverexpression of CdDHN4-L with φ-segment and CdDHN4-S lacking of φ-segment in Arabidopsis significantly increased tolerance against abiotic stresses. The growth phenotype of Arabidopsis exposed to NaCl at 100 mM was better in plants overexpressing CdDHN4-L than those overexpressing CdDHN4-S, as well as better in E.coli cells overexpressing CdDHN4-L than those overexpressing CdDHN4-S in 300 and 400 mM NaCl, and under extreme temperature conditions at − 20 °C and 50 °C. The CdDHN4-L had higher disordered characterization on structures than CdDHN4-S at temperatures from 10 to 90 °C. The recovery activities of lactic dehydrogenase (LDH) and alcohol dehydrogenase (ADH) in presence of CdDHN4-L and CdDHN4-S were higher than that of LDH and ADH alone under freeze-thaw damage and heat. Protein-binding and bimolecular fluorescence complementation showed that both proteins could bind to proteins with positive isoelectric point via electrostatic forces.ConclusionsThese results indicate that CdDHN4-L has higher protective ability against abiotic stresses due to its higher flexible unfolded structure and thermostability in comparison with CdDHN4-S. These provided direct evidence of the function of the φ-segment in dehydrins for protecting plants against abiotic stress and to show the electrostatic interaction between dehydrins and client proteins.Electronic supplementary materialThe online version of this article (10.1186/s12870-018-1511-2) contains supplementary material, which is available to authorized users.

The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

“…The results show that all four proteins possess similar CD spectra; a large negative minimum ellipticity is observed at ~200 nm, and a small negative signal is seen after 212 nm (Figure 1(c)), suggesting that these proteins are largely disordered when alone in solution. These results agree with what has been reported for other LEA proteins 21,45–47 …”

Dehydrins: an overview of current approaches and advancement

“…In this study, it was found that DHNs not only act as drought-resistant protein, but also interact with FK506 binding protein in the nucleus and acts as regulatory protein for drought tolerance by regulating the ABA responsive signaling pathway (Tiwari et al, 2019). DHNs have been recognized as molecular protectors for functionality of some proteins such as lactate dehydrogenase and malate dehydrogenase in response to environmental stresses, as supported by previous studies (Zhou et al, 2017;Lv et al, 2018). Misfolding of proteins that are toxic to plants is triggered by drought stress, so protein quality control is critical to plant quality.…”

Cross Tolerance to Drought and low Phosphorus Stress in Mungbean is Regulated by Improved Antioxidant Capacity, Biological N2-Fixation, and Differential Transcript Accumulation

“…The DSI gene, VrDHN3, was induced under drought and combined stresses and during drought recovery in leaves of IC333090 and petioles of IC488526. DHNs are unfolded proteins functioning as protective molecular chaperones for enzymes and phospholipids, enhancing plant tolerance to abiotic stresses (Lv et al 2018). Expression of DHN3 and DHN44 were highly correlated with yield in barley under drought stress (Park et al 2006).…”