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논문 기본 정보

자료유형
학술저널
저자정보
Chun, Jae-An (Department of Biotechnology, Donga University) Seo, Jee-Young (Department of Biotechnology, Donga University) Han, Mi-Ok (Department of Biotechnology, Donga University) Lee, Jin-Woo (Department of Biotechnology, Donga University) Yi, Young-Byung (Environmental Biotechnology, Donga University) Park, Gun-Yong (National Agricultural Products Quality Management Service) Lee, Shin-Woo (Department of Biotechnology, Jinju National University) Bae, Shin-Chul (National Institute of Agricultural Biotechnology) Cho, Kang-Jin (National Institute of Agricultural Biotechnology) Chung, Chung-Han (Department of Biotechnology, Donga University)
저널정보
한국식물학회 식물학회지 식물학회지 제49권 제6호
발행연도
2006.1
수록면
507 - 512 (6page)

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The differential transcription activity of dehydroascorbate reductase (DHAR) was scrutinized in the transformed hairy roots, leaves, stems, roots, and developing seeds of sesame (Sesamum indicum L.). Its relative levels of expression were compared via the threshold cycle $(C_T)$ method, using real-time RT-PCR. Ubiquitous expression of DHAR in all organs was confirmed with both real-time and conventional RT-PCR. With the former, DHAR transcript levels were, unexpectedly, 4.7-fold higher in the stem tissue than in the hairy roots; the lowest levels were detected in the seeds. It was possible to determine the transcription activity of hairy root DHAR, with a low amount of total RNA (0.5 ng), using real-time RT-PCR but not with conventional RT-PCR gel analysis. This indicated that the former is more sensitive and efficient than the latter for the detection of gene expression. We also characterized DHAR cDNA cloned from transformed hairy roots, and found that sequence identity for the deduced amino acids of the DHAR enzyme was shared at 60 to 83% among plant species. The algorithm prediction and phylogenetic analysis suggested that the cloned cDNA polypeptide is cytosolic DHAR. Another feature of the cloned cDNA polypeptide was the presence of a CXXS instead of CXXC motif in the active center of the DHAR enzyme.

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