OsCYP21-4, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice
| Autor: | Hye Sun Cho, Hyun Soon Kim, Areum Lee, Won Yong Jung, Byung-Ryun Kim, Jun Cheul Ahn, Hyun Ji Park, Young Nim You, Dae Hwa Yoon, Sang Sook Lee |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
golgi-resident protein
Nicotiana benthamiana Plant Science Isomerase lcsh:Plant culture Biology Mitochondrion salinity tolerance symbols.namesake chemistry.chemical_compound Arabidopsis oxidative stress lcsh:SB1-1110 Abscisic acid Cyclophilin Original Research peroxidase activity Golgi apparatus biology.organism_classification chemistry Biochemistry cyclophilin PPIase symbols biology.protein Peroxidase |
| Zdroj: | Frontiers in Plant Science Frontiers in Plant Science, Vol 6 (2015) |
| ISSN: | 1664-462X |
| DOI: | 10.3389/fpls.2015.00797 |
| Popis: | OsCYP21-4 is a rice cyclophilin protein that binds to cyclosporine A, an immunosuppressant drug. CYP21-4s in Arabidopsis and rice were previously shown to function as mitochondrial cyclophilins, as determined by TargetP analysis. In the current study, we found that OsCYP21-4-GFP localized to the Golgi, rather than mitochondria, in Nicotiana benthamiana leaves, which was confirmed based on its co-localization with cis Golgi α-ManI-mCherry protein. OsCYP21-4 transcript levels increased in response to treatments with various abiotic stresses and the phytohormone abscisic acid, revealing its stress-responsiveness. CYP21-4 homologs do not possess key peptidyl prolyl cis/trans isomerase (PPIase) activity/cyclosporine A (CsA) binding residues, and recombinant OsCYP21-4 protein did not convert the synthetic substrate Suc-AAPF-pNA via cis- trans- isomerization in vitro. In addition, transgenic plants overexpressing OsCYP21-4 exhibited increased tolerance to salinity and hydrogen peroxide treatment, along with increased peroxidase activity. These results demonstrate that OsCYP21-4 is a novel Golgi-localized cyclophilin that plays a role in oxidative stress tolerance, possibly by regulating peroxidase activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|