Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro
Abstract 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 an...
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
BMC
2018-11-01
|
| Series: | BMC Plant Biology |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s12870-018-1511-2 |
| _version_ | 1811204657594236928 |
|---|---|
| author | Aimin Lv Liantai Su Xingchen Liu Qiang Xing Bingru Huang Yuan An Peng Zhou |
| author_facet | Aimin Lv Liantai Su Xingchen Liu Qiang Xing Bingru Huang Yuan An Peng Zhou |
| author_sort | Aimin Lv |
| collection | DOAJ |
| description | Abstract 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 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. 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. |
| first_indexed | 2024-04-12T03:17:12Z |
| format | Article |
| id | doaj.art-2b921279e38644e1964bd6a3e546773e |
| institution | Directory Open Access Journal |
| issn | 1471-2229 |
| language | English |
| last_indexed | 2024-04-12T03:17:12Z |
| publishDate | 2018-11-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Plant Biology |
| spelling | doaj.art-2b921279e38644e1964bd6a3e546773e2022-12-22T03:50:03ZengBMCBMC Plant Biology1471-22292018-11-0118111310.1186/s12870-018-1511-2Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitroAimin Lv0Liantai Su1Xingchen Liu2Qiang Xing3Bingru Huang4Yuan An5Peng Zhou6School of Agriculture and Biology, Shanghai Jiao Tong UniversitySchool of Agriculture and Biology, Shanghai Jiao Tong UniversitySchool of Agriculture and Biology, Shanghai Jiao Tong UniversityShanghai Chenshan Botanical GardenDepartment of Plant Biology and Pathology, Rutgers, the State University of New JerseySchool of Agriculture and Biology, Shanghai Jiao Tong UniversitySchool of Agriculture and Biology, Shanghai Jiao Tong UniversityAbstract 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 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. 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.http://link.springer.com/article/10.1186/s12870-018-1511-2Abiotic stressDehydrinIntrinsic disorder proteinMolecular chaperoneProtein interactionφ-Segment |
| spellingShingle | Aimin Lv Liantai Su Xingchen Liu Qiang Xing Bingru Huang Yuan An Peng Zhou Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro BMC Plant Biology Abiotic stress Dehydrin Intrinsic disorder protein Molecular chaperone Protein interaction φ-Segment |
| title | Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro |
| title_full | Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro |
| title_fullStr | Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro |
| title_full_unstemmed | Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro |
| title_short | Characterization of Dehydrin protein, CdDHN4-L and CdDHN4-S, and their differential protective roles against abiotic stress in vitro |
| title_sort | characterization of dehydrin protein cddhn4 l and cddhn4 s and their differential protective roles against abiotic stress in vitro |
| topic | Abiotic stress Dehydrin Intrinsic disorder protein Molecular chaperone Protein interaction φ-Segment |
| url | http://link.springer.com/article/10.1186/s12870-018-1511-2 |
| work_keys_str_mv | AT aiminlv characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT liantaisu characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT xingchenliu characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT qiangxing characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT bingruhuang characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT yuanan characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro AT pengzhou characterizationofdehydrinproteincddhn4landcddhn4sandtheirdifferentialprotectiverolesagainstabioticstressinvitro |