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

Aimin Lv, Liantai Su, Xingchen Liu, Qiang Xing, Bingru Huang, Yuan An, Peng Zhou

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Background: Dehydrins 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. Results: Overexpression 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 100mM 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 400mM 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. Conclusions: These 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.

Original languageEnglish (US)
Article number299
JournalBMC plant biology
Issue number1
StatePublished - Nov 26 2018

All Science Journal Classification (ASJC) codes

  • Plant Science


  • Abiotic stress
  • Dehydrin
  • Intrinsic disorder protein
  • Molecular chaperone
  • Protein interaction
  • ϕ-Segment


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