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Cloning and Characterization of GDP-mannose Pyrophosphorylase from Solanum Tuberosum L.
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  • Cloning and Characterization of GDP-mannose Pyrophosphorylase from Solanum Tuberosum L.
저자명
Hyun. Tae-Kyung,Lim. Jung-Dae,Kim. Jae-Kwang,Seong. Eun-Soo,Lee. Jae-Geun,Yoon. Byeong-Sung,Kim. Myong-Jo,Cho. Dong-Ha,Yu. Chang
간행물명
韓國藥用作物學會誌
권/호정보
2005년|13권 5호|pp.276-283 (8 pages)
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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Ascorbic acid is a great antioxidant and helps protect the body against pollutants. GDP-mannose pyrophosphorylase (GMPase) is a key enzyme in manufacturing GDP-mannose, a glycosyl donor for ascorbate and cell wall biosynthesis as well as for protein glycosylation. In this study, we described molecular cloning of a full-length cDNA from Potato (Solanum tuberosum L. cv. Jasim), using tuber. The cDNA isolated encoded a GDP-mannose pyrophosphrylase. The nucleotide sequence of pGMPC showed about 95%, 89% and 80% homology with S. tuberosum (AF022716), N. tabacum (AB066279) and A. thaliana (AF076484) cDNAs clone known as GMPase, respectively. We detected the expression of GMPase using RT-PCR. The highest expression of GMPase was found in stems, and the largest amount of ascorbic acid was also presented in stems. In contrast, the leaf showed minimal level of GMPase transcript and ascorbic acid content. We propose that GMPase expression patterns were similar to the changes of ascorbic acid content in the leaves treated with diverse stresses.