Characterization of Cytosolic Cyclophilin from Guard Cells of Vicia faba L.
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概要
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The effect of immunosuppressant cyclosporin A(CsA) on inward-rectifying K^+-channels and biochemical analysis have indicated the presence of cyclophilin in guard cells of Vicia faba. In this study, we identified a full-length cDNA sequence, vcCyP, encoding cyclophilin(CyP), a peptidyl-prolyl cis-trans isomerase of guard cell protoplasts(GCPs) from Vicia faba L. The deduced amino acid sequence revealed that vcCyP contained 171 amino acid residues and exhibited a strong similarity to previously described cytosolic CyP isoforms from other plants. vcCyP had seven extra amino acid residues, which is a characteristic of the cytosolic form of plant CyPs. A complex of recombinant vcCyP and CsA inhibited the phosphatase activity of bovine calcineurin, a type 2B protein phosphatase, with a half-inhibitory concentration of 0.2 μM. Protein phosphatase activity was measured in the cytosolic fraction of GCPs using a ^<32>P-labeled myelin basic protein(^<32>P-MBP) and the activity was increased by a physiological concentration of Ca^<2+> (1 μM). This Ca^<2+>-stimulated phosphatase activity was inhibited by CsA, suggesting the presence of both cytosolic CyP and calcineurin-like protein phosphatase in guard cells. Northern blot analysis showed that the transcription level of vcCyP was much higher in GCPs than in root and leaf tissues of Vicia.
- 日本植物生理学会の論文
著者
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KINOSHITA Toshinori
Department of Biology, Faculty of Science, Kyushu University
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SHIMAZAKI Ken-ichiro
Department of Biology, Faculty of Science, Kyushu University
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Kinoshita Toshinori
Department Of Biology Faculty Of Science Kyushu University
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Shimazaki Ken-ichiro
Department Of Biology Faculty Of Science Kyushu University
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