OsCYP21, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice

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OsCYP21, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice
Sang Sook Lee; Hyun Ji Park; Won Yong Jung; Areum Lee; Dae Hwa Yoon; Young Nim You; Hyun Soon Kim; B G Kim; J C Ahn; Hye Sun Cho
Bibliographic Citation
Frontiers in Plant Science, vol. 6, pp. 797-797
Publication Year
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.
CyclophilinGolgi-resident proteinOxidative stressPeroxidase activityPPIaseSalinity tolerance
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Division of Research on National Challenges > Plant Systems Engineering Research > 1. Journal Articles
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