Expression of multi-domain type III antifreeze proteins from the Antarctic eelpout (Lycodichths dearborni) in transgenic tobacco plants improves cold resistance
| Autor: | C L Peng, Liangbiao Chen, Hui zhu, Ruiqin Hu, Qiao Huang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Proline
Globular protein Transgene MDA Genetically modified crops Aquatic Science Cold tolerance lcsh:Aquaculture. Fisheries. Angling Eelpout 03 medical and health sciences Tetramer Antifreeze protein Multidomain proteins Gene Ecology Evolution Behavior and Systematics 030304 developmental biology chemistry.chemical_classification lcsh:SH1-691 0303 health sciences Electrolyte leakage Ecology biology food and beverages 04 agricultural and veterinary sciences biology.organism_classification chemistry Biochemistry Type III antifreeze proteins 040102 fisheries 0401 agriculture forestry and fisheries |
| Zdroj: | Aquaculture and Fisheries, Vol 6, Iss 2, Pp 186-191 (2021) |
| Popis: | Type III antifreeze proteins (AFPIIIs) are a group of small globular proteins found in some polar fishes to protect them against freezing damage. Transgenic expression of AFPs has been shown to confer cold tolerance to commercially important plants and animals. We have previously isolated multiple AFPIII genes in the Antarctic eelpout (Lycodichthys dearborni) that encode larger AFPIII isoforms with up to 12 of the conventional domains. Here we have introduced the fish AFPIII genes that encode for the monomer (ld1), dimer (ld2), trimer (ld3) and tetramer (ld4) AFPIII isoforms in tobacco plants. Pot-grown 4-week-old transgenic tobacco plants were exposed to cold stress at 4 °C for 30 days and the results show that ld1, ld2, ld3 and ld4 transgenic plants present relatively lower electrolyte leakage and lower content of malondialdehyde (MDA), but accumulated higher content of proline when compared to control plants. This indicates considerable improved membrane integrity under low temperature stress and improvement of the plant cold resistance. The plants transformed with the AFPIII tetramer- and trimer-domains demonstrated a higher cold-tolerant levels when compared with plants transformed with the dimer- and monomer AFPIII domains. Our study further supports that fish AFPIIIs, especially the multidomain proteins, protect cells from non-freezing hypothermic stresses, apart from there well-known function as ice inhibitors molecules at freezing temperature. |
| Databáze: | OpenAIRE |
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