Journal
FRONTIERS IN PLANT SCIENCE
Volume 6, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fpls.2015.00797
Keywords
cyclophilin; golgi-resident protein; oxidative stress; peroxidase activity; PPIase; salinity tolerance
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Funding
- National Research Foundation of Korea (NRF) - Korea government (MEST) [NRF-2012R1A1A2044517]
- Cabbage Genomics assisted breeding supporting center (CGC) research programs
- Agricultural Biotechnology Developmental Program - Ministry of Agriculture, Food and Rural Affair [114061-3]
- KRIBB Initiative Program
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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 bentharniana leaves, which was confirmed based on its co-localization with cis Golgi alpha-Manl-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 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.
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