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OsCYP21-4, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice.

Lee SS, Park HJ, Jung WY, Lee A, Yoon DH, You YN, Kim HS, Kim BG, Ahn JC, Cho HS - Front Plant Sci (2015)

Bottom Line: 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.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.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.

View Article: PubMed Central - PubMed

Affiliation: Sustainable Bioresource Research Center, Korea Research Institute of Bioscience and Biotechnology Daejeon, South Korea.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus

Multiple sequence alignment and phylogenetic relationship between OsCYP21-4 and CYP21-4 homologs from various plants. (A) Sequence comparison of OsCYP21-4 protein with selected CYP21-4 homologs from various plant species. The amino acids necessary for PPIase activity/CsA binding and are marked by asterisks. The degree of background shading indicates amino acid identity and similarity (black: identity >50%, gray: similarity > 50%). (B) Phylogenetic distance between OsCYP21-4 and other homologs.
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Figure 1: Multiple sequence alignment and phylogenetic relationship between OsCYP21-4 and CYP21-4 homologs from various plants. (A) Sequence comparison of OsCYP21-4 protein with selected CYP21-4 homologs from various plant species. The amino acids necessary for PPIase activity/CsA binding and are marked by asterisks. The degree of background shading indicates amino acid identity and similarity (black: identity >50%, gray: similarity > 50%). (B) Phylogenetic distance between OsCYP21-4 and other homologs.

Mentions: OsCYP21-4 (Os07g29390) is a rice cyclophilin protein containing 235 amino acids with a molecular mass of 26.4 kDa. It contains a single CYP domain (amino acids 80–230). By searching NCBI (http://www.ncbi.nlm.nih.gov/BLAST/) using the OsCYP21-4 sequence as a query, we identified OsCYP21-4 homologs in three monocot and seven dicot plants (Figure 1A). Multiple amino acid sequence alignments showed that OsCYP21-4 shares high similarity with its homologs from monocots (84% similarity with B. distachyon, 81% with H. vulgare, and 81% with Z. mays) and less conserved sequence homology with CYP21-4 homologs from dicots (76% similarity with V. vinifera, 70% with Arabidopsis, 69% with C. sativa, and Brassica, and 67% with S. lycopersicum). Moreover, the results of phylogenetic tree analysis based on the full-length sequences of these homologs are good in agreement with the evolutionary relationships among these species (Figure 1B): OsCYP21-4 has a closer evolutionary relationship with CYP21-4 homologs from monocots than from dicots.


OsCYP21-4, a novel Golgi-resident cyclophilin, increases oxidative stress tolerance in rice.

Lee SS, Park HJ, Jung WY, Lee A, Yoon DH, You YN, Kim HS, Kim BG, Ahn JC, Cho HS - Front Plant Sci (2015)

Multiple sequence alignment and phylogenetic relationship between OsCYP21-4 and CYP21-4 homologs from various plants. (A) Sequence comparison of OsCYP21-4 protein with selected CYP21-4 homologs from various plant species. The amino acids necessary for PPIase activity/CsA binding and are marked by asterisks. The degree of background shading indicates amino acid identity and similarity (black: identity >50%, gray: similarity > 50%). (B) Phylogenetic distance between OsCYP21-4 and other homologs.
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Related In: Results  -  Collection

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Figure 1: Multiple sequence alignment and phylogenetic relationship between OsCYP21-4 and CYP21-4 homologs from various plants. (A) Sequence comparison of OsCYP21-4 protein with selected CYP21-4 homologs from various plant species. The amino acids necessary for PPIase activity/CsA binding and are marked by asterisks. The degree of background shading indicates amino acid identity and similarity (black: identity >50%, gray: similarity > 50%). (B) Phylogenetic distance between OsCYP21-4 and other homologs.
Mentions: OsCYP21-4 (Os07g29390) is a rice cyclophilin protein containing 235 amino acids with a molecular mass of 26.4 kDa. It contains a single CYP domain (amino acids 80–230). By searching NCBI (http://www.ncbi.nlm.nih.gov/BLAST/) using the OsCYP21-4 sequence as a query, we identified OsCYP21-4 homologs in three monocot and seven dicot plants (Figure 1A). Multiple amino acid sequence alignments showed that OsCYP21-4 shares high similarity with its homologs from monocots (84% similarity with B. distachyon, 81% with H. vulgare, and 81% with Z. mays) and less conserved sequence homology with CYP21-4 homologs from dicots (76% similarity with V. vinifera, 70% with Arabidopsis, 69% with C. sativa, and Brassica, and 67% with S. lycopersicum). Moreover, the results of phylogenetic tree analysis based on the full-length sequences of these homologs are good in agreement with the evolutionary relationships among these species (Figure 1B): OsCYP21-4 has a closer evolutionary relationship with CYP21-4 homologs from monocots than from dicots.

Bottom Line: 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.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.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.

View Article: PubMed Central - PubMed

Affiliation: Sustainable Bioresource Research Center, Korea Research Institute of Bioscience and Biotechnology Daejeon, South Korea.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus